O95400 (CD2B2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
CD2 antigen cytoplasmic tail-binding protein 2
Short name=CD2 cytoplasmic domain-binding protein 2
Short name=CD2 tail-binding protein 2

Gene names

Name:	CD2BP2
Synonyms:	KIAA1178

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	341 AA.
Sequence status	Complete.
Protein existence	Evidence 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 component	Cytoplasm
Coding sequence diversity	Polymorphism
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	assembly of spliceosomal tri-snRNP Non-traceable author statement. Source: BHF-UCL negative regulation of phosphatase activity Inferred from direct assay. Source: UniProtKB
Cellular component	U5 snRNP Inferred from direct assay. Source: BHF-UCL cytoplasm Traceable author statement. Source: ProtInc nucleoplasm Inferred from direct assay. Source: BHF-UCL
Molecular function	protein binding Inferred from physical interaction. Source: BHF-UCL ribonucleoprotein complex binding Inferred from direct assay. Source: BHF-UCL
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 341

341

CD2 antigen cytoplasmic tail-binding protein 2

PRO_0000089437

Regions

Domain

280 – 338

59

GYF

Amino acid modifications

Modified residue

46

1

Phosphoserine Ref.10

Modified residue

49

1

Phosphoserine Ref.6 Ref.8 Ref.9 Ref.11 Ref.13

Modified residue

118

1

Phosphoserine Ref.12

Modified residue

194

1

Phosphoserine Ref.14

Modified residue

195

1

Phosphoserine Ref.6 Ref.7

Natural variations

Natural variant

231

1

G → D.
Corresponds to variant rs13330462 [ dbSNP | Ensembl ].

VAR_050772

Natural variant

262

1

T → I.
Corresponds to variant rs34391305 [ dbSNP | Ensembl ].

VAR_050773

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

341

Helix Strand Turn

Details...

Beta strand

282 – 293

12

Beta strand

296 – 300

5

Helix

301 – 309

9

Beta strand

318 – 324

7

Helix

332 – 334

3

Helix

337 – 340

4

Sequences

	Sequence		Length	Mass (Da)
	O95400 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 8E9A7EE0C40474D5	FASTA	341	37,646
	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

References

	« Hide 'large scale' referencesShow '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]	"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: 14702039] [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. , 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: 15489334] [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: 10574461] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 218-341. Tissue: Brain.
[6]	"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: Cervix carcinoma.
[7]	"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: Cervix carcinoma.
[8]	"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. Tissue: Embryonic kidney.
[9]	"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. Tissue: Embryonic kidney.
[10]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[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: 19367720] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, MASS SPECTROMETRY. 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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, MASS SPECTROMETRY. 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: 18318008] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, MASS SPECTROMETRY. Tissue: Liver.
[14]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]	"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

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.

IPI

IPI00006103.

RefSeq

NP_001230575.1. NM_001243646.1.
NP_006101.1. NM_006110.2.

UniGene

Hs.202677.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GYF	NMR	-	A	280-341	[»]
1L2Z	NMR	-	A	280-341	[»]
1SYX	X-ray	2.35	B/D/F	256-341	[»]

ProteinModelPortal

O95400.

SMR

O95400. Positions 280-341.

ModBase

Search...

Protein-protein interaction databases

IntAct

O95400. 2 interactions.

MINT

MINT-99472.

STRING

O95400.

PTM databases

PhosphoSite

O95400.

Proteomic databases

PRIDE

O95400.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000305596; ENSP00000304903; ENSG00000169217.

GeneID

10421.

KEGG

hsa:10421.

UCSC

uc002dxr.1. human.

Organism-specific databases

CTD

10421.

GeneCards

GC16M030363.

H-InvDB

HIX0202240.

HGNC

HGNC:1656. CD2BP2.

MIM

604470. gene.

neXtProt

NX_O95400.

PharmGKB

PA26209.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG06964.

HOGENOM

HBG715317.

HOVERGEN

HBG056920.

InParanoid

O95400.

OMA

QTWVNEG.

OrthoDB

EOG4R503D.

PhylomeDB

O95400.

Enzyme and pathway databases

Reactome

REACT_1675. mRNA Processing.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

O95400.

Bgee

O95400.

CleanEx

HS_CD2BP2.

Genevestigator

O95400.

GermOnline

ENSG00000169217. Homo sapiens.

Family and domain databases

InterPro

IPR003169. GYF.
[Graphical view]

KO

K13099.

Pfam

PF02213. GYF. 1 hit.
[Graphical view]

SMART

SM00444. GYF. 1 hit.
[Graphical view]

SUPFAM

SSF55277. GYF. 1 hit.

PROSITE

PS50829. GYF. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

39496.

SOURCE

Search...

Entry information

Entry name

CD2B2_HUMAN

Accession

Primary (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:	January 25, 2012
This is version 99 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.