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

Alternative name(s):
U5 snRNP 52K protein
Short name=U5-52K

Gene names

Name:	CD2BP2
Synonyms:	KIAA1178

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	341 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	mRNA processing mRNA splicing
Cellular component	Cytoplasm Nucleus
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 Ref.6. Source: BHF-UCL negative regulation of phosphatase activity Inferred from direct assay PubMed 19389623. Source: UniProtKB
Cellular_component	U5 snRNP Inferred from direct assay Ref.6. Source: BHF-UCL cytoplasm Traceable author statement Ref.1. Source: ProtInc nucleoplasm Inferred from direct assay Ref.6. Source: BHF-UCL
Molecular_function	ribonucleoprotein complex binding Inferred from direct assay Ref.6. 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

49

1

Phosphoserine Ref.7 Ref.10 Ref.11 Ref.13 Ref.14 Ref.16

Modified residue

118

1

Phosphoserine Ref.14

Modified residue

194

1

Phosphoserine Ref.14

Modified residue

195

1

Phosphoserine Ref.14

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] [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]	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] [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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, 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] [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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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.

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.

ModBase

Search...

Protein-protein interaction databases

IntAct

O95400. 4 interactions.

MINT

MINT-99472.

STRING

9606.ENSP00000304903.

PTM databases

PhosphoSite

O95400.

Proteomic databases

PaxDb

O95400.

PRIDE

O95400.

Protocols and materials databases

DNASU

10421.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000305596; ENSP00000304903; ENSG00000169217.
ENST00000569466; ENSP00000456935; ENSG00000169217.

GeneID

10421.

KEGG

hsa:10421.

UCSC

uc002dxr.3. human.

Organism-specific databases

CTD

10421.

GeneCards

GC16M030363.

HGNC

HGNC:1656. CD2BP2.

HPA

HPA041508.

MIM

604470. gene.

neXtProt

NX_O95400.

PharmGKB

PA26209.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG301637.

HOGENOM

HOG000007061.

HOVERGEN

HBG056920.

InParanoid

O95400.

KO

K13099.

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

Gene3D

3.30.1490.40. 1 hit.

InterPro

IPR003169. GYF.
[Graphical view]

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

ChiTaRS

CD2BP2. human.

EvolutionaryTrace

O95400.

GenomeRNAi

10421.

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:	May 29, 2013
This is version 112 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.