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Reviewed, UniProtKB/Swiss-Prot Q96Q27 (ASB2_HUMAN)

Last modified July 22, 2008. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Ankyrin repeat and SOCS box protein 2
      Short name=ASB-2
Gene names
Name: ASB2
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length587 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Probable substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Component of a probable ECS E3 ubiquitin-protein ligase complex which contains CUL5, either RBX1 or RNF7/RBX2, Elongin BC complex (TCEB1 and TCEB2) and ASB2.

Induction

By all-trans retinoic acid (ATRA).

Domain

The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin-protein ligase complexes By similarity.

Sequence similarities

Contains 12 ANK repeats.

Contains 1 SOCS box domain.

Ontologies

Keywords

   Biological processUbl conjugation pathway
   Coding sequence diversityPolymorphism
   DomainANK repeat
Repeat

Gene Ontology (GO)

   Biological processsignal transduction

Traceable author statement. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Chain1 – 587587Ankyrin repeat and SOCS box protein 2

Regions

Repeat56 – 8530ANK 1
Repeat89 – 11931ANK 2
Repeat123 – 15230ANK 3
Repeat156 – 18530ANK 4
Repeat189 – 21830ANK 5
Repeat222 – 25130ANK 6
Repeat255 – 28430ANK 7
Repeat288 – 31730ANK 8
Repeat320 – 34930ANK 9
Repeat362 – 39130ANK 10
Repeat392 – 42130ANK 11
Repeat428 – 45629ANK 12
Domain533 – 58755SOCS box

Natural variations

Natural variant1601P → S: dbSNP rs2295213.

Experimental info

Mutagenesis5481L → P: No interaction with Elongin BC complex
Mutagenesis551 – 5522LC → PF: No interaction with CUL5 or RNF7
Mutagenesis5521C → P: No interaction with Elongin BC complex
Mutagenesis571 – 5744LPLP → AAAA: No interaction with CUL5 or RNF7
Sequence conflict2241Missing in AAD45345. Ref.5
Sequence conflict4601Missing in AAD45345. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q96Q27-1 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 866A2B6010C4C1F9

FASTA58765,084
        10         20         30         40         50         60 
MTRFSYAEYF SLFHSCSAPS RSTAPPESSP ARAPMGLFQG VMQKYSSSLF KTSQLAPADP 

        70         80         90        100        110        120 
LIKAIKDGDE EALKTMIKEG KNLAEPNKEG WLPLHEAAYY GQVGCLKVLQ RAYPGTIDQR 

       130        140        150        160        170        180 
TLQEETAVYL ATCRGHLDCL LSLLQAGAEP DISNKSRETP LYKACERKNA EAVKILVQHN 

       190        200        210        220        230        240 
ADTNHRCNRG WTALHESVSR NDLEVMQILV SGGAKVESKN AYGITPLFVA AQSGQLEALR 

       250        260        270        280        290        300 
FLAKYGADIN TQASDNASAL YEACKNEHEE VVEFLLSQGA DANKTNKDGL LPLHIASKKG 

       310        320        330        340        350        360 
NYRIVQMLLP VTSRTRIRRS GVSPLHLAAE RNHDEVLEAL LSARFDVNTP LAPERARLYE 

       370        380        390        400        410        420 
DRRSSALYFA VVNNNVYATE LLLQHGADPN RDVISPLLVA IRHGCLRTMQ LLLDHGANID 

       430        440        450        460        470        480 
AYIATHPTAF PATIMFAMKC LSLLKFLMDL GCDGEPCFSC LYGNGPHPPA PQPSSRFNDA 

       490        500        510        520        530        540 
PAADKEPSVV QFCEFVSAPE VSRWAGPIID VLLDYVGNVQ LCSRLKEHID SFEDWAVIKE 

       550        560        570        580 
KAEPPRPLAH LCRLRVRKAI GKYRIKLLDT LPLPGRLIRY LKYENTQ 

« Hide

References

« Hide 'large scale' references
[1]"ATRA-regulated Asb-2 gene induced in differentiation of HL-60 leukemia cells."
Kohroki J., Fujita S., Itoh N., Yamada Y., Imai H., Yumoto N., Nakanishi T., Tanaka K.
FEBS Lett. 505:223-228(2001) [PubMed: 11566180] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
[2]"ASB-2 inhibits growth and promotes commitment in myeloid leukemia cells."
Guibal F.C., Moog-Lutz C., Smolewski P., Di Gioia Y., Darzynkiewicz Z., Lutz P.G., Cayre Y.E.
J. Biol. Chem. 277:218-224(2002) [PubMed: 11682484] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
[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: Blood.
[4]The German cDNA consortium
Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 31-587.
Tissue: Uterus.
[5]"Cloning and characterization of the genes encoding the ankyrin repeat and SOCS box-containing proteins Asb-1, Asb-2, Asb-3 and Asb-4."
Kile B.T., Viney E.M., Willson T.A., Brodnicki T.C., Cancilla M.R., Herlihy A.S., Croker B.A., Baca M., Nicola N.A., Hilton D.J., Alexander W.S.
Gene 258:31-41(2000) [PubMed: 11111040] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 42-587.
[6]"ASB proteins interact with cullin5 and Rbx2 to form E3 ubiquitin ligase complexes."
Kohroki J., Nishiyama T., Nakamura T., Masuho Y.
FEBS Lett. 579:6796-6802(2005) [PubMed: 16325183] [Abstract]
Cited for: FUNCTION, SUBUNIT, INTERACTION WITH CUL5 AND RNF7, MUTAGENESIS OF 551-LEU-CYS-552 AND 571-LEU--PRO-574.
[7]"ASB2 is an elongin BC-interacting protein that can assemble with cullin 5 and Rbx1 to reconstitute an E3 ubiquitin ligase complex."
Heuze M.L., Guibal F.C., Banks C.A., Conaway J.W., Conaway R.C., Cayre Y.E., Benecke A., Lutz P.G.
J. Biol. Chem. 280:5468-5474(2005) [PubMed: 15590664] [Abstract]
Cited for: FUNCTION, SUBUNIT, INTERACTION WITH TCEB1, MUTAGENESIS OF LEU-548 AND CYS-552.

Cross-references

Sequence databases

AB056723 mRNA. Translation: BAB64532.1.
AJ251238 mRNA. Translation: CAC17765.1.
BC032354 mRNA. Translation: AAH32354.1.
AL137735 mRNA. Translation: CAB70899.1.
AF159164 mRNA. Translation: AAD45345.1.
PIRT46507.
RefSeqNP_057234.2.
UniGeneHs.510327

3D structure databases

HSSPHSSP built from PDB template 2MYO based on UniProtKB P80144.
ModBaseSearch...

Genome annotation databases

EnsemblENSG00000100628. Homo sapiens. [Contig view]
GeneID51676.
KEGGhsa:51676.

Organism-specific databases

H-InvDBHIX0011920.
HGNCHGNC:16012. ASB2.
HPAHPA001546.
MIM605759. gene.
PharmGKBPA25030.
GenAtlasSearch...
GeneCardsSearch...

Phylogenomic databases

HOGENOMQ96Q27.
HOVERGENQ96Q27.

Gene expression databases

ArrayExpressQ96Q27.
CleanExHS_ASB2.
GermOnlineENSG00000100628. Homo sapiens.

Family and domain databases

InterProIPR002110. ANK.
IPR001496. SOCS_C.
[Graphical view]
Gene3DG3DSA:1.25.40.20. ANK. 2 hits.
PfamPF00023. Ank. 10 hits.
PF07525. SOCS_box. 1 hit.
[Graphical view]
PRINTSPR01415. ANKYRIN.
SMARTSM00248. ANK. 11 hits.
[Graphical view]
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 9 hits.
PS50225. SOCS. 1 hit.
[Graphical view]
ProDomQ96Q27.
[Graphical view] [Entries sharing at least one domain]
BLOCKSSearch...

Other Resources

SOURCESearch...
ProtoNetSearch...

Entry information

Entry nameASB2_HUMAN
AccessionPrimary (citable) accession number: Q96Q27
Secondary accession number(s): Q9NSU5, Q9Y567
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2002
Last sequence update: December 1, 2001
Last modified: July 22, 2008
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

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 · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents