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Reviewed, UniProtKB/Swiss-Prot O95400 (CD2B2_HUMAN)

Last modified December 16, 2008. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    CD2 antigen cytoplasmic tail-binding protein 2
Alternative name(s):
    CD2 cytoplasmic domain-binding protein
    CD2 tail-binding protein
    CD_antigen=CD2
Gene names
Name: CD2BP2
Synonyms: KIAA1178
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length341 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Subunit structure

Binds the cytoplasmic domain of CD2 through the GYF domain.

Subcellular location

Cytoplasm.

Sequence similarities

Contains 1 GYF domain.

Ontologies

Keywords

   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   PTMPhosphoprotein
   Technical term3D-structure

Gene Ontology (GO)

   Biological processnuclear mRNA splicing, via spliceosome

Inferred from Experiment. Source: Reactome

   Cellular componentcytoplasm Ref.1

Traceable author statement. Source: ProtInc

   Molecular functionprotein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 341341CD2 antigen cytoplasmic tail-binding protein 2
PRO_0000089437

Regions

Domain280 – 33859GYF

Amino acid modifications

Modified residue491Phosphoserine Ref.4 Ref.6 Ref.7 Ref.9
Modified residue1181Phosphoserine Ref.8
Modified residue1951Phosphoserine Ref.4 Ref.5

Natural variations

Natural variant2311G → D: dbSNP rs13330462.
VAR_050772
Natural variant2621T → I: dbSNP rs34391305.
VAR_050773

Secondary structure

............ 341
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O95400-1 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 8E9A7EE0C40474D5

FASTA34137,646
        10         20         30         40         50         60 
MPKRKVTFQG VGDEEDEDEI IVPKKKLVDP VAGSGGPGSR FKGKHSLDSD EEEDDDDGGS 

        70         80         90        100        110        120 
SKYDILASED VEGQEAATLP SEGGVRITPF NLQEEMEEGH FDADGNYFLN RDAQIRDSWL 

       130        140        150        160        170        180 
DNIDWVKIRE RPPGQRQASD SEEEDSLGQT SMSAQALLEG LLELLLPRET VAGALRRLGA 

       190        200        210        220        230        240 
RGGGKGRKGP GQPSSPQRLD RLSGLADQMV ARGNLGVYQE TRERLAMRLK GLGCQTLGPH 

       250        260        270        280        290        300 
NPTPPPSLDM FAEELAEEEL ETPTPTQRGE AESRGDGLVD VMWEYKWENT GDAELYGPFT 

       310        320        330        340 
SAQMQTWVSE GYFPDGVYCR KLDPPGGQFY NSKRIDFDLY T 

« Hide

References

« Hide 'large scale' references
[1]"Identification of a proline-binding motif regulating CD2-triggered T lymphocyte activation."
Nishizawa K., Freund C., Li J., Wagner G., Reinherz E.L.
Proc. Natl. Acad. Sci. U.S.A. 95:14897-14902(1998) [PubMed: 9843987] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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.
[3]"Characterization of cDNA clones selected by the GeneMark analysis from size-fractionated cDNA libraries from human brain."
Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.
DNA Res. 6:329-336(1999) [PubMed: 10574461] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 218-341.
Tissue: Brain.
[4]"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-49 AND SER-195, MASS SPECTROMETRY.
Tissue: Epithelium.
[5]"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-195, MASS SPECTROMETRY.
Tissue: Epithelium.
[6]"Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction."
Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.
Mol. Cell. Proteomics 6:1952-1967(2007) [PubMed: 17693683] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, MASS SPECTROMETRY.
[7]"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-49, MASS SPECTROMETRY.
[8]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, MASS SPECTROMETRY.
[9]"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-49, MASS SPECTROMETRY.
Tissue: Liver.
[10]"The GYF domain is a novel structural fold that is involved in lymphoid signaling through proline-rich sequences."
Freund C., Dotsch V., Nishizawa K., Reinherz E.L., Wagner G.
Nat. Struct. Biol. 6:656-660(1999) [PubMed: 10404223] [Abstract]
Cited for: STRUCTURE BY NMR OF 280-341.
+Additional computationally mapped references.

Cross-references

Sequence databases

AF104222 mRNA. Translation: AAC84141.1.
BC000495 mRNA. Translation: AAH00495.1.
BC001947 mRNA. Translation: AAH01947.1.
AB033004 mRNA. Translation: BAA86492.1.
RefSeqNP_006101.1.
UniGeneHs.700708

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1GYFNMR-A280-341[»]
1L2ZNMR-A280-341[»]
1SYXX-ray2.35B/D/F256-341[»]
ModBaseSearch...

Protein-protein interaction databases

IntActO95400. 27 interactions.

PTM databases

PhosphoSiteO95400.

Proteomic databases

PRIDEO95400.

Genome annotation databases

EnsemblENSG00000169217. Homo sapiens. [Contig view]
GeneID10421.
KEGGhsa:10421.

Organism-specific databases

GeneCardsGC16M030272.
H-InvDBHIX0012951.
HGNCHGNC:1656. CD2BP2.
MIM604470. gene.
PharmGKBPA26209.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

HOGENOMO95400.
HOVERGENO95400.

Enzyme and pathway databases

ReactomeREACT_1675. mRNA Processing.
REACT_6167. Influenza Infection.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressO95400.
CleanExHS_CD2BP2.
GermOnlineENSG00000169217. Homo sapiens.

Family and domain databases

InterProIPR003169. GYF.
[Graphical view]
PfamPF02213. GYF. 1 hit.
[Graphical view]
SMARTSM00444. GYF. 1 hit.
[Graphical view]
PROSITEPS50829. GYF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

LinkHubO95400.
NextBio39496.
SOURCESearch...

Entry information

Entry nameCD2B2_HUMAN
AccessionPrimary (citable) accession number: O95400
Secondary accession number(s): Q9ULP2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2003
Last sequence update: May 1, 1999
Last modified: December 16, 2008
This is version 66 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 16

Human chromosome 16: 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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