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O95400 (CD2B2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
CD2 antigen cytoplasmic tail-binding protein 2

Short name=CD2 cytoplasmic domain-binding protein 2
Short name=CD2 tail-binding protein 2
Alternative name(s):
U5 snRNP 52K protein
Short name=U5-52K
Gene names
Name:CD2BP2
Synonyms:KIAA1178
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length341 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in pre-mRNA splicing as component of the U5 snRNP complex that is involved in spliceosome assembly. Ref.6

Subunit structure

Component of the U5 snRNP complex composed of the U5 snRNA and at least PRPF6, PRPF8, SNRNP200, EFTUD2, SNRNP40, DDX23, TXNL4A and CD2BP2. Interacts directly with TXNL4A and PRPF6. Interacts (via GYF domain) with CD2 (via Pro-rich sequence in the cytoplasmic domain). Ref.1 Ref.6 Ref.8 Ref.18 Ref.19

Subcellular location

Cytoplasm. Nucleus. Note: Predominantly nuclear. Ref.6 Ref.9 Ref.18

Sequence similarities

Contains 1 GYF domain.

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 residue441N6-acetyllysine By similarity
Modified residue491Phosphoserine Ref.7 Ref.10 Ref.11 Ref.13 Ref.14 Ref.16
Modified residue1181Phosphoserine Ref.14
Modified residue1941Phosphoserine Ref.14
Modified residue1951Phosphoserine Ref.14

Natural variations

Natural variant2311G → D.
Corresponds to variant rs13330462 [ dbSNP | Ensembl ].
VAR_050772
Natural variant2621T → I.
Corresponds to variant rs34391305 [ dbSNP | Ensembl ].
VAR_050773

Secondary structure

............ 341
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O95400 [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH CD2.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung.
[5]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 218-341.
Tissue: Brain.
[6]"The human U5 snRNP 52K protein (CD2BP2) interacts with U5-102K (hPrp6), a U4/U6.U5 tri-snRNP bridging protein, but dissociates upon tri-snRNP formation."
Laggerbauer B., Liu S., Makarov E., Vornlocher H.P., Makarova O., Ingelfinger D., Achsel T., Luhrmann R.
RNA 11:598-608(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, INTERACTION WITH PRPF6 AND TXNL4A, SUBCELLULAR LOCATION.
[7]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"The network of protein-protein interactions within the human U4/U6.U5 tri-snRNP."
Liu S., Rauhut R., Vornlocher H.-P., Luehrmann R.
RNA 12:1418-1430(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
[9]"Investigating the functional role of CD2BP2 in T cells."
Heinze M., Kofler M., Freund C.
Int. Immunol. 19:1313-1318(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[10]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[11]"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: T-cell.
[12]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[14]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49; SER-118; SER-194 AND SER-195, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"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] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 280-341.
[18]"Dynamic interaction of CD2 with the GYF and the SH3 domain of compartmentalized effector molecules."
Freund C., Kuhne R., Yang H., Park S., Reinherz E.L., Wagner G.
EMBO J. 21:5985-5995(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 280-341, INTERACTION WITH CD2 PEPTIDE, SUBCELLULAR LOCATION.
[19]"Structural basis for the bifunctionality of the U5 snRNP 52K protein (CD2BP2)."
Nielsen T.K., Liu S., Luhrmann R., Ficner R.
J. Mol. Biol. 369:902-908(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 256-341 IN COMPLEX WITH TXNL4A, INTERACTION WITH TXNL4A.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF104222 mRNA. Translation: AAC84141.1.
AK315708 mRNA. Translation: BAG38069.1.
CH471192 Genomic DNA. Translation: EAW52260.1.
BC000495 mRNA. Translation: AAH00495.1.
BC001947 mRNA. Translation: AAH01947.1.
AB033004 mRNA. Translation: BAA86492.1.
RefSeqNP_001230575.1. NM_001243646.1.
NP_006101.1. NM_006110.2.
UniGeneHs.202677.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GYFNMR-A280-341[»]
1L2ZNMR-A280-341[»]
1SYXX-ray2.35B/D/F256-341[»]
ProteinModelPortalO95400.
SMRO95400. Positions 280-341.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115690. 51 interactions.
IntActO95400. 9 interactions.
MINTMINT-99472.
STRING9606.ENSP00000304903.

PTM databases

PhosphoSiteO95400.

Proteomic databases

PaxDbO95400.
PRIDEO95400.

Protocols and materials databases

DNASU10421.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000305596; ENSP00000304903; ENSG00000169217.
ENST00000569466; ENSP00000456935; ENSG00000169217.
GeneID10421.
KEGGhsa:10421.
UCSCuc002dxr.3. human.

Organism-specific databases

CTD10421.
GeneCardsGC16M030363.
HGNCHGNC:1656. CD2BP2.
HPAHPA041508.
MIM604470. gene.
neXtProtNX_O95400.
PharmGKBPA26209.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG301637.
HOGENOMHOG000007061.
HOVERGENHBG056920.
InParanoidO95400.
KOK13099.
OMARDNWLDN.
OrthoDBEOG7VMP6C.
PhylomeDBO95400.
TreeFamTF313042.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.

Gene expression databases

ArrayExpressO95400.
BgeeO95400.
CleanExHS_CD2BP2.
GenevestigatorO95400.

Family and domain databases

Gene3D3.30.1490.40. 1 hit.
InterProIPR003169. GYF.
[Graphical view]
PfamPF02213. GYF. 1 hit.
[Graphical view]
SMARTSM00444. GYF. 1 hit.
[Graphical view]
SUPFAMSSF55277. SSF55277. 1 hit.
PROSITEPS50829. GYF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCD2BP2. human.
EvolutionaryTraceO95400.
GeneWikiCD2BP2.
GenomeRNAi10421.
NextBio39496.
PROO95400.
SOURCESearch...

Entry information

Entry nameCD2B2_HUMAN
AccessionPrimary (citable) accession number: O95400
Secondary accession number(s): B2RDX2, Q9ULP2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2003
Last sequence update: May 1, 1999
Last modified: April 16, 2014
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM