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O95400

- CD2B2_HUMAN

UniProt

O95400 - CD2B2_HUMAN

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Protein

CD2 antigen cytoplasmic tail-binding protein 2

Gene
CD2BP2, KIAA1178
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Involved in pre-mRNA splicing as component of the U5 snRNP complex that is involved in spliceosome assembly.1 Publication

GO - Molecular functioni

  1. protein binding Source: IntAct
  2. ribonucleoprotein complex binding Source: BHF-UCL

GO - Biological processi

  1. gene expression Source: Reactome
  2. mRNA splicing, via spliceosome Source: Reactome
  3. negative regulation of phosphatase activity Source: UniProtKB
  4. RNA splicing Source: Reactome
  5. spliceosomal tri-snRNP complex assembly Source: BHF-UCL
Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA splicing

Enzyme and pathway databases

ReactomeiREACT_467. mRNA Splicing - Major Pathway.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:CD2BP2
Synonyms:KIAA1178
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:1656. CD2BP2.

Subcellular locationi

Cytoplasm. Nucleus
Note: Predominantly nuclear.3 Publications

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. nucleoplasm Source: BHF-UCL
  3. nucleus Source: BHF-UCL
  4. U5 snRNP Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26209.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 341341CD2 antigen cytoplasmic tail-binding protein 2PRO_0000089437Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei44 – 441N6-acetyllysine By similarity
Modified residuei49 – 491Phosphoserine6 Publications
Modified residuei118 – 1181Phosphoserine1 Publication
Modified residuei194 – 1941Phosphoserine1 Publication
Modified residuei195 – 1951Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO95400.
PaxDbiO95400.
PRIDEiO95400.

PTM databases

PhosphoSiteiO95400.

Expressioni

Gene expression databases

ArrayExpressiO95400.
BgeeiO95400.
CleanExiHS_CD2BP2.
GenevestigatoriO95400.

Organism-specific databases

HPAiHPA041508.

Interactioni

Subunit structurei

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). Interacts with PQBP1.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CD2P067293EBI-768015,EBI-3912464
PPP1CAP621362EBI-768015,EBI-357253
PRPF6O949064EBI-768015,EBI-536755
TXNL4AP838762EBI-768015,EBI-746539

Protein-protein interaction databases

BioGridi115690. 51 interactions.
IntActiO95400. 9 interactions.
MINTiMINT-99472.
STRINGi9606.ENSP00000304903.

Structurei

Secondary structure

1
341
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi282 – 29312
Beta strandi296 – 3005
Helixi301 – 3099
Beta strandi318 – 3247
Helixi332 – 3343
Helixi337 – 3404

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GYFNMR-A280-341[»]
1L2ZNMR-A280-341[»]
1SYXX-ray2.34B/D/F262-341[»]
4BWSX-ray2.50C/F280-341[»]
ProteinModelPortaliO95400.
SMRiO95400. Positions 280-341.

Miscellaneous databases

EvolutionaryTraceiO95400.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini280 – 33859GYFAdd
BLAST

Sequence similaritiesi

Contains 1 GYF domain.

Phylogenomic databases

eggNOGiNOG301637.
HOGENOMiHOG000007061.
HOVERGENiHBG056920.
InParanoidiO95400.
KOiK13099.
OMAiRDNWLDN.
OrthoDBiEOG7VMP6C.
PhylomeDBiO95400.
TreeFamiTF313042.

Family and domain databases

Gene3Di3.30.1490.40. 1 hit.
InterProiIPR003169. GYF.
[Graphical view]
PfamiPF02213. GYF. 1 hit.
[Graphical view]
SMARTiSM00444. GYF. 1 hit.
[Graphical view]
SUPFAMiSSF55277. SSF55277. 1 hit.
PROSITEiPS50829. GYF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O95400-1 [UniParc]FASTAAdd to Basket

« Hide

MPKRKVTFQG VGDEEDEDEI IVPKKKLVDP VAGSGGPGSR FKGKHSLDSD    50
EEEDDDDGGS SKYDILASED VEGQEAATLP SEGGVRITPF NLQEEMEEGH 100
FDADGNYFLN RDAQIRDSWL DNIDWVKIRE RPPGQRQASD SEEEDSLGQT 150
SMSAQALLEG LLELLLPRET VAGALRRLGA RGGGKGRKGP GQPSSPQRLD 200
RLSGLADQMV ARGNLGVYQE TRERLAMRLK GLGCQTLGPH NPTPPPSLDM 250
FAEELAEEEL ETPTPTQRGE AESRGDGLVD VMWEYKWENT GDAELYGPFT 300
SAQMQTWVSE GYFPDGVYCR KLDPPGGQFY NSKRIDFDLY T 341
Length:341
Mass (Da):37,646
Last modified:May 1, 1999 - v1
Checksum:i8E9A7EE0C40474D5
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti231 – 2311G → D.
Corresponds to variant rs13330462 [ dbSNP | Ensembl ].
VAR_050772
Natural varianti262 – 2621T → I.
Corresponds to variant rs34391305 [ dbSNP | Ensembl ].
VAR_050773

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS10675.1.
RefSeqiNP_001230575.1. NM_001243646.1.
NP_006101.1. NM_006110.2.
UniGeneiHs.202677.

Genome annotation databases

EnsembliENST00000305596; ENSP00000304903; ENSG00000169217.
ENST00000569466; ENSP00000456935; ENSG00000169217.
GeneIDi10421.
KEGGihsa:10421.
UCSCiuc002dxr.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS10675.1.
RefSeqi NP_001230575.1. NM_001243646.1.
NP_006101.1. NM_006110.2.
UniGenei Hs.202677.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1GYF NMR - A 280-341 [» ]
1L2Z NMR - A 280-341 [» ]
1SYX X-ray 2.34 B/D/F 262-341 [» ]
4BWS X-ray 2.50 C/F 280-341 [» ]
ProteinModelPortali O95400.
SMRi O95400. Positions 280-341.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115690. 51 interactions.
IntActi O95400. 9 interactions.
MINTi MINT-99472.
STRINGi 9606.ENSP00000304903.

PTM databases

PhosphoSitei O95400.

Proteomic databases

MaxQBi O95400.
PaxDbi O95400.
PRIDEi O95400.

Protocols and materials databases

DNASUi 10421.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000305596 ; ENSP00000304903 ; ENSG00000169217 .
ENST00000569466 ; ENSP00000456935 ; ENSG00000169217 .
GeneIDi 10421.
KEGGi hsa:10421.
UCSCi uc002dxr.3. human.

Organism-specific databases

CTDi 10421.
GeneCardsi GC16M030363.
HGNCi HGNC:1656. CD2BP2.
HPAi HPA041508.
MIMi 604470. gene.
neXtProti NX_O95400.
PharmGKBi PA26209.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG301637.
HOGENOMi HOG000007061.
HOVERGENi HBG056920.
InParanoidi O95400.
KOi K13099.
OMAi RDNWLDN.
OrthoDBi EOG7VMP6C.
PhylomeDBi O95400.
TreeFami TF313042.

Enzyme and pathway databases

Reactomei REACT_467. mRNA Splicing - Major Pathway.

Miscellaneous databases

ChiTaRSi CD2BP2. human.
EvolutionaryTracei O95400.
GeneWikii CD2BP2.
GenomeRNAii 10421.
NextBioi 39496.
PROi O95400.
SOURCEi Search...

Gene expression databases

ArrayExpressi O95400.
Bgeei O95400.
CleanExi HS_CD2BP2.
Genevestigatori O95400.

Family and domain databases

Gene3Di 3.30.1490.40. 1 hit.
InterProi IPR003169. GYF.
[Graphical view ]
Pfami PF02213. GYF. 1 hit.
[Graphical view ]
SMARTi SM00444. GYF. 1 hit.
[Graphical view ]
SUPFAMi SSF55277. SSF55277. 1 hit.
PROSITEi PS50829. GYF. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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. 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.
  20. "Mutations in the PQBP1 gene prevent its interaction with the spliceosomal protein U5-15 kD."
    Mizuguchi M., Obita T., Serita T., Kojima R., Nabeshima Y., Okazawa H.
    Nat. Commun. 5:3822-3822(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 280-341 IN COMPLEX WITH PQBP1 AND TXNL4A, SUBUNIT.

Entry informationi

Entry nameiCD2B2_HUMAN
AccessioniPrimary (citable) accession number: O95400
Secondary accession number(s): B2RDX2, Q9ULP2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2003
Last sequence update: May 1, 1999
Last modified: September 3, 2014
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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