Histone deacetylase 1 - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot Q13547 (HDAC1_HUMAN)

Last modified September 2, 2008. Version 103. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Histone deacetylase 1
      Short name=HD1
    EC=3.5.1.98

Gene names

Name:	HDAC1
Synonyms:	RPD3L1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	482 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes.
Catalytic activity	Hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone.
Subunit structure	Part of the core histone deacetylase (HDAC) complex composed of HDAC1, HDAC2, RBBP4 and RBBP7. The core complex associates with MTA2, MBD2, MBD3, MTA1L1, CHD3 and CHD4 to form the nucleosome remodeling and histone deacetylation (NuRD) complex, or with SIN3, SAP18 and SAP30 to form the SIN3 HDAC complex. Component of a BHC histone deacetylase complex that contains HDAC1, HDAC2, HMG20B/BRAF35, AOF2/LSD1, RCOR1/CoREST and PHF21A/BHC80. The BHC complex may also contain ZMYM2, ZNF217, ZMYM3, GSE1 and GTF2I. Associates with the 9-1-1 complex; interacts with HUS1. Found in a complex with DNMT3A and HDAC7. Interacts with BCOR, BRMS1L, DAXX, DNMT1, EP300, HCFC1, PCAF, PHB2, MIER1, JMJD2A/JHDM3A, MINT, NRIP1, RERE, SETDB1, SUV39H1, TGIF, TGIF2, UHRF1 and UHRF2. Interacts with the non-histone region of H2AFY. Interacts with HDAC9. Component of a mSin3A corepressor complex that contains SIN3A, SAP130, SUDS3/SAP45, ARID4B/SAP180, HDAC1 and HDAC2. Interacts with BANP, CBFA2T3 and JARID1B. Interacts with SAP30L. Interacts with E4F1. Interacts with KFL1 By similarity.
Subcellular location	Nucleus.
Tissue specificity	Ubiquitous, with higher levels in heart, pancreas and testis, and lower levels in kidney and brain.
Post-translational modification	Sumoylated on Lys-444 and Lys-476; which promotes enzymatic activity. Desumoylated by SENP1. Phosphorylation on Ser-421 and Ser-423 promotes enzymatic activity and interactions with NuRD and SIN3 complexes.
Sequence similarities	Belongs to the histone deacetylase family. Type 1 subfamily.

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Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Molecular function	Chromatin regulator Hydrolase Repressor
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure
Gene Ontology (GO)
Biological process	anti-apoptosis Traceable author statement. Source: ProtInc chromatin modification Traceable author statement. Source: UniProtKB
Cellular component	cytoplasm Traceable author statement. Source: UniProtKB histone deacetylase complex Traceable author statement. Source: UniProtKB
Molecular function	enzyme binding Inferred from physical interaction. Source: UniProtKB histone deacetylase activity Ref.1 Traceable author statement. Source: UniProtKB identical protein binding Inferred from physical interaction. Source: IntAct transcription factor activity Ref.2 Traceable author statement. Source: ProtInc transcription factor binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		1	EBI-301834,EBI-301834
BRMS1	Q9HCU9	2	EBI-301834,EBI-714781
DAXX	Q9UER7	1	EBI-301834,EBI-77321
DNMT3L	Q9UJW3	2	EBI-301834,EBI-740967
HCFC1	P51610	1	EBI-301834,EBI-396176
HDAC2	Q92769	2	EBI-301834,EBI-301821
HIST1H4A	P62805	1	EBI-301834,EBI-302023
MBD1	Q9UIS9	2	EBI-301834,EBI-867196
MORF4L2	Q15014	1	EBI-301834,EBI-399257
NCOR2	Q9Y618	1	EBI-301834,EBI-80830
NFKB1	P19838	2	EBI-301834,EBI-300010
RB1	P06400	1	EBI-301834,EBI-491274
RBBP4	Q09028	1	EBI-301834,EBI-620823
RBBP7	Q16576	1	EBI-301834,EBI-352227
RELA	Q04206	2	EBI-301834,EBI-73886
Rere	Q80TZ9	1	EBI-301834,EBI-904076	From a different organism.
RFX1	P22670	1	EBI-301834,EBI-716037
SAP18	O00422	2	EBI-301834,EBI-1044156
SUV39H1	O43463	2	EBI-301834,EBI-349968
TP53	P04637	1	EBI-301834,EBI-366083

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Molecule processing

Chain

1 – 482

482

Histone deacetylase 1

Regions

Region

9 – 321

313

Histone deacetylase

Sites

Active site

141

By similarity

Amino acid modifications

Modified residue

221

Phosphotyrosine

Modified residue

393

Phosphoserine

Modified residue

421

Phosphoserine; by CK2

Modified residue

423

Phosphoserine; by CK2

Cross-link

444

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)

Cross-link

476

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)

Experimental info

Mutagenesis

391 – 482

Missing: Strongly decreases deacetylase activity, and disrupts interaction with NuRD and SIN3 complexes

Mutagenesis

421

S → A: Strongly decreases deacetylase activity, and disrupts interaction with NuRD and SIN3 complexes

Mutagenesis

421

S → D or E: Slightly decreases deacetylase activity

Mutagenesis

423

S → A: Strongly decreases deacetylase activity, and disrupts interaction with NuRD and SIN3 complexes

Mutagenesis

423

S → D or E: Decreases deacetylase activity

Mutagenesis

424

E → A: Slightly decreases deacetylase activity, no effect on interaction with NuRD and SIN3 complexes

Mutagenesis

425

E → A: No effect on deacetylase activity, no effect on interaction with NuRD and SIN3 complexes

Mutagenesis

426

E → A: Decreases deacetylase activity, and disrupts interaction with NuRD and SIN3 complexes

Sequence conflict

312

W → R in BAA08909. Ref.2

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Sequences

Sequence

Length

Mass (Da)

Tools

Q13547-1 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 4D35B7C1ED7838D6
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FASTA

482

55,103

        10         20         30         40         50         60 
MAQTQGTRRK VCYYYDGDVG NYYYGQGHPM KPHRIRMTHN LLLNYGLYRK MEIYRPHKAN 

        70         80         90        100        110        120 
AEEMTKYHSD DYIKFLRSIR PDNMSEYSKQ MQRFNVGEDC PVFDGLFEFC QLSTGGSVAS 

       130        140        150        160        170        180 
AVKLNKQQTD IAVNWAGGLH HAKKSEASGF CYVNDIVLAI LELLKYHQRV LYIDIDIHHG 

       190        200        210        220        230        240 
DGVEEAFYTT DRVMTVSFHK YGEYFPGTGD LRDIGAGKGK YYAVNYPLRD GIDDESYEAI 

       250        260        270        280        290        300 
FKPVMSKVME MFQPSAVVLQ CGSDSLSGDR LGCFNLTIKG HAKCVEFVKS FNLPMLMLGG 

       310        320        330        340        350        360 
GGYTIRNVAR CWTYETAVAL DTEIPNELPY NDYFEYFGPD FKLHISPSNM TNQNTNEYLE 

       370        380        390        400        410        420 
KIKQRLFENL RMLPHAPGVQ MQAIPEDAIP EESGDEDEDD PDKRISICSS DKRIACEEEF 

       430        440        450        460        470        480 
SDSEEEGEGG RKNSSNFKKA KRVKTEDEKE KDPEEKKEVT EEEKTKEEKP EAKGVKEEVK 


LA

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p." Taunton J., Hassig C.A., Schreiber S.L. Science 272:408-411(1996) [PubMed: 8602529] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: T-cell.
[2]	"Isolation and mapping of a human gene (RPD3L1) that is homologous to RPD3, a transcription factor in Saccharomyces cerevisiae." Furukawa Y., Kawakami T., Sudo K., Inazawa J., Matsumine A., Akiyama T., Nakamura Y. Cytogenet. Cell Genet. 73:130-133(1996) [PubMed: 8646880] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Fetal lung.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lung.
[4]	"MEF-2 function is modified by a novel co-repressor, MITR." Sparrow D.B., Miska E.A., Langley E., Reynaud-Deonauth S., Kotecha S., Towers N., Spohr G., Kouzarides T., Mohun T.J. EMBO J. 18:5085-5098(1999) [PubMed: 10487760] [Abstract] Cited for: INTERACTION WITH HDAC9.
[5]	"BCoR, a novel corepressor involved in BCL-6 repression." Huynh K.D., Fischle W., Verdin E., Bardwell V.J. Genes Dev. 14:1810-1823(2000) [PubMed: 10898795] [Abstract] Cited for: INTERACTION WITH BCOR.
[6]	"HDAC1, a histone deacetylase, forms a complex with Hus1 and Rad9, two G2/M checkpoint Rad proteins." Cai R.L., Yan-Neale Y., Cueto M.A., Xu H., Cohen D. J. Biol. Chem. 275:27909-27916(2000) [PubMed: 10846170] [Abstract] Cited for: INTERACTION WITH THE 9-1-1 COMPLEX AND HUS1.
[7]	"Receptor-interacting protein 140 directly recruits histone deacetylases for gene silencing." Wei L.-N., Hu X., Chandra D., Seto E., Farooqui M. J. Biol. Chem. 275:40782-40787(2000) [PubMed: 11006275] [Abstract] Cited for: INTERACTION WITH NRIP1.
[8]	"Sequestration and inhibition of Daxx-mediated transcriptional repression by PML." Li H., Leo C., Zhu J., Wu X., O'Neil J., Park E.-J., Chen J.D. Mol. Cell. Biol. 20:1784-1796(2000) [PubMed: 10669754] [Abstract] Cited for: INTERACTION WITH DAXX.
[9]	"Identification of a transcriptional repressor related to the noncatalytic domain of histone deacetylases 4 and 5." Zhou X., Richon V.M., Rifkind R.A., Marks P.A. Proc. Natl. Acad. Sci. U.S.A. 97:1056-1061(2000) [PubMed: 10655483] [Abstract] Cited for: INTERACTION WITH HDAC9.
[10]	"Histone deacetylase 1 phosphorylation promotes enzymatic activity and complex formation." Pflum M.K.H., Tong J.K., Lane W.S., Schreiber S.L. J. Biol. Chem. 276:47733-47741(2001) [PubMed: 11602581] [Abstract] Cited for: PHOSPHORYLATION AT SER-421 AND SER-423, MUTAGENESIS OF SER-421 AND SER-423, MASS SPECTROMETRY.
[11]	"Sharp, an inducible cofactor that integrates nuclear receptor repression and activation." Shi Y., Downes M., Xie W., Kao H.-Y., Ordentlich P., Tsai C.-C., Hon M., Evans R.M. Genes Dev. 15:1140-1151(2001) [PubMed: 11331609] [Abstract] Cited for: INTERACTION WITH MINT.
[12]	"Stable histone deacetylase complexes distinguished by the presence of SANT domain proteins CoREST/kiaa0071 and Mta-L1." Humphrey G.W., Wang Y., Russanova V.R., Hirai T., Qin J., Nakatani Y., Howard B.H. J. Biol. Chem. 276:6817-6824(2001) [PubMed: 11102443] [Abstract] Cited for: INTERACTION WITH MBD2 AND MBD3.
[13]	"TGIF2 interacts with histone deacetylase 1 and represses transcription." Melhuish T.A., Gallo C.M., Wotton D. J. Biol. Chem. 276:32109-32114(2001) [PubMed: 11427533] [Abstract] Cited for: INTERACTION WITH TGIF2.
[14]	"ETO, a target of t(8;21) in acute leukemia, makes distinct contacts with multiple histone deacetylases and binds mSin3A through its oligomerization domain." Amann J.M., Nip J., Strom D.K., Lutterbach B., Harada H., Lenny N., Downing J.R., Meyers S., Hiebert S.W. Mol. Cell. Biol. 21:6470-6483(2001) [PubMed: 11533236] [Abstract] Cited for: INTERACTION WITH CBFA2T3.
[15]	"The SUMO E3 ligase RanBP2 promotes modification of the HDAC4 deacetylase." Kirsh O., Seeler J.-S., Pichler A., Gast A., Mueller S., Miska E., Mathieu M., Harel-Bellan A., Kouzarides T., Melchior F., Dejean A. EMBO J. 21:2682-2691(2002) [PubMed: 12032081] [Abstract] Cited for: SUMOYLATION.
[16]	"SUMO-1 modification of histone deacetylase 1 (HDAC1) modulates its biological activities." David G., Neptune M.A., DePinho R.A. J. Biol. Chem. 277:23658-23663(2002) [PubMed: 11960997] [Abstract] Cited for: SUMOYLATION AT LYS-444 AND LYS-476.
[17]	"Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1." Wysocka J., Myers M.P., Laherty C.D., Eisenman R.N., Herr W. Genes Dev. 17:896-911(2003) [PubMed: 12670868] [Abstract] Cited for: INTERACTION WITH HCFC1.
[18]	"A candidate X-linked mental retardation gene is a component of a new family of histone deacetylase-containing complexes." Hakimi M.-A., Dong Y., Lane W.S., Speicher D.W., Shiekhattar R. J. Biol. Chem. 278:7234-7239(2003) [PubMed: 12493763] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE BHC COMPLEX WITH PHF21A; HDAC2; HMG20B; AOF2; RCOR1; ZMYM2; ZNF217; ZMYM3; KIAA0182 AND GTF2I.
[19]	"Human MI-ER1 alpha and beta function as transcriptional repressors by recruitment of histone deacetylase 1 to their conserved ELM2 domain." Ding Z., Gillespie L.L., Paterno G.D. Mol. Cell. Biol. 23:250-258(2003) [PubMed: 12482978] [Abstract] Cited for: INTERACTION WITH MIER1.
[20]	"Identification and characterization of three new components of the mSin3A corepressor complex." Fleischer T.C., Yun U.J., Ayer D.E. Mol. Cell. Biol. 23:3456-3467(2003) [PubMed: 12724404] [Abstract] Cited for: IDENTIFICATION IN A MSIN3A COREPRESSOR COMPLEX WITH SIN3A; SAP130; SUDS3; ARID4B; HDAC1 AND HDAC2.
[21]	"Modulation of p120E4F transcriptional activity by the Gam1 adenoviral early protein." Colombo R., Draetta G.F., Chiocca S. Oncogene 22:2541-2547(2003) [PubMed: 12730668] [Abstract] Cited for: INTERACTION WITH E4F1.
[22]	"Identification of a novel BRMS1-homologue protein p40 as a component of the mSin3A/p33(ING1b)/HDAC1 deacetylase complex." Nikolaev A.Y., Papanikolaou N.A., Li M., Qin J., Gu W. Biochem. Biophys. Res. Commun. 323:1216-1222(2004) [PubMed: 15451426] [Abstract] Cited for: INTERACTION WITH BRMS1L.
[23]	"SENP1 enhances androgen receptor-dependent transcription through desumoylation of histone deacetylase 1." Cheng J., Wang D., Wang Z., Yeh E.T.H. Mol. Cell. Biol. 24:6021-6028(2004) [PubMed: 15199155] [Abstract] Cited for: DESUMOYLATION BY SENP1.
[24]	"ICBP90, an E2F-1 target, recruits HDAC1 and binds to methyl-CpG through its SRA domain." Unoki M., Nishidate T., Nakamura Y. Oncogene 23:7601-7610(2004) [PubMed: 15361834] [Abstract] Cited for: INTERACTION WITH UHRF1 AND UHRF2.
[25]	"NuRD and SIN3 histone deacetylase complexes in development." Ahringer J. Trends Genet. 16:351-356(2000) [PubMed: 10904264] [Abstract] Cited for: REVIEW ON DEACETYLASE COMPLEXES.
[26]	"Functional characterization of JMJD2A, a histone deacetylase- and retinoblastoma-binding protein." Gray S.G., Iglesias A.H., Lizcano F., Villanueva R., Camelo S., Jingu H., Teh B.T., Koibuchi N., Chin W.W., Kokkotou E., Dangond F. J. Biol. Chem. 280:28507-28518(2005) [PubMed: 15927959] [Abstract] Cited for: INTERACTION WITH JMJD2A.
[27]	"Tumor suppressor SMAR1 mediates cyclin D1 repression by recruitment of the SIN3/histone deacetylase 1 complex." Rampalli S., Pavithra L., Bhatt A., Kundu T.K., Chattopadhyay S. Mol. Cell. Biol. 25:8415-8429(2005) [PubMed: 16166625] [Abstract] Cited for: INTERACTION WITH BANP.
[28]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-221, MASS SPECTROMETRY.
[29]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393; SER-421 AND SER-423, MASS SPECTROMETRY. Tissue: Epithelium.
[30]	"SAP30L interacts with members of the Sin3A corepressor complex and targets Sin3A to the nucleolus." Viiri K.M., Korkeamaeki H., Kukkonen M.K., Nieminen L.K., Lindfors K., Peterson P., Maeki M., Kainulainen H., Lohi O. Nucleic Acids Res. 34:3288-3298(2006) [PubMed: 16820529] [Abstract] Cited for: INTERACTION WITH SAP30L.
[31]	"Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line." Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S. Electrophoresis 28:2027-2034(2007) [PubMed: 17487921] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393, MASS SPECTROMETRY.
[32]	"Breast cancer associated transcriptional repressor PLU-1/JARID1B interacts directly with histone deacetylases." Barrett A., Santangelo S., Tan K., Catchpole S., Roberts K., Spencer-Dene B., Hall D., Scibetta A., Burchell J., Verdin E., Freemont P., Taylor-Papadimitriou J. Int. J. Cancer 121:265-275(2007) [PubMed: 17373667] [Abstract] Cited for: INTERACTION WITH JARID1B.
[33]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421 AND SER-423, MASS SPECTROMETRY.
[34]	"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography." Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J. Proteomics 8:1346-1361(2008) [PubMed: 18318008] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421 AND SER-423, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

U50079 mRNA. Translation: AAC50475.1.
D50405 mRNA. Translation: BAA08909.1.
BC000301 mRNA. Translation: AAH00301.1.

RefSeq

NP_004955.2.

UniGene

Hs.88556

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1TYI	model	-	A	1-482	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:24184N.

IntAct

Q13547.

PTM databases

PhosphoSite

Q13547.

Proteomic databases

PeptideAtlas

Q13547.

Genome annotation databases

Ensembl

ENSG00000116478. Homo sapiens. [Contig view]

GeneID

3065.

KEGG

hsa:3065.

Organism-specific databases

H-InvDB

HIX0000369.
HIX0077545.

HGNC

HGNC:4852. HDAC1.

HPA

CAB005017.

MIM

601241. gene.

PharmGKB

PA29226.

GenAtlas

Search...

GeneCards

Search...

Phylogenomic databases

HOGENOM

Q13547.

HOVERGEN

Q13547.

Gene expression databases

ArrayExpress

Q13547.

CleanEx

HS_HDAC1.

GermOnline

ENSG00000116478. Homo sapiens.

Family and domain databases

InterPro

IPR000286. His_deacetylse.
IPR003084. His_deacetylse_1.
[Graphical view]

Gene3D

G3DSA:3.40.800.20. His_deacetylse. 1 hit.

PANTHER

PTHR10625. His_deacetylse. 1 hit.
PTHR10625:SF28. His_deacetylse_1. 1 hit.

Pfam

PF00850. Hist_deacetyl. 1 hit.
[Graphical view]

PIRSF

PIRSF037913. His_deacetylse_1. 1 hit.

PRINTS

PR01270. HDASUPER.
PR01271. HISDACETLASE.

ProDom

Q13547.
[Graphical view] [Entries sharing at least one domain]

BLOCKS

Search...

Other Resources

DrugBank

DB02546. Vorinostat.

LinkHub

Q13547.

SOURCE

Search...

ProtoNet

Search...

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Entry information

Entry name

HDAC1_HUMAN

Accession

Primary (citable) accession number: Q13547
Secondary accession number(s): Q92534

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	September 2, 2008
This is version 103 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Keywords

Gene Ontology (GO)

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents