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UniProtKB/Swiss-Prot entry P78314


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name 3BP2_HUMAN
Primary accession number P78314
Secondary accession numbers A6NNC2 B2R5R6 O00500 O15373 P78315
Integrated into Swiss-Prot on July 15, 1998
Sequence was last modified on July 15, 1998 (Sequence version 2)
Annotations were last modified on    May 26, 2009 (Entry version 84)
Name and origin of the protein
Protein name SH3 domain-binding protein 2
Synonym 3BP-2
Gene name
Name: SH3BP2
Synonyms: 3BP2
ORFNames: RES4-23
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
TISSUE=Tonsil;
Gokemeijer J., Deligiannidis K.E., Ligris K., Ernst T.J.;
"3BP2 binds to phosphatidylinositols; linking the hemopoietic tyrosine kinase c-FES to the cytoplasmic membrane in a phosphorylation dependent mechanism.";
Blood 88:473A-473A(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
DOI=10.1006/geno.1997.4849; PubMed=9299232 [NCBI, ExPASy, EBI, Israel, Japan]
Bell S.M., Shaw M., Jou Y.-S., Myers R.M., Knowles M.A.;
"Identification and characterization of the human homologue of SH3BP2, an SH3 binding domain protein within a common region of deletion at 4p16.3 involved in bladder cancer.";
Genomics 44:163-170(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT), AND TISSUE SPECIFICITY.
TISSUE=Brain;
DOI=10.1093/dnares/5.3.177; PubMed=9734812 [NCBI, ExPASy, EBI, Israel, Japan]
Hadano S., Ishida Y., Ikeda J.-E.;
"The primary structure and genomic organization of five novel transcripts located close to the Huntington's disease gene on human chromosome 4p16.3.";
DNA Res. 5:177-186(1998).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
TISSUE=Cerebellum;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature03466; PubMed=15815621 [NCBI, ExPASy, EBI, Israel, Japan]
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2 and 4.";
Nature 434:724-731(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
TISSUE=Cervix;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
DOI=10.1186/gb-2004-5-2-r8; PubMed=14759258 [NCBI, ExPASy, EBI, Israel, Japan]
Hillman R.T., Green R.E., Brenner S.E.;
"An unappreciated role for RNA surveillance.";
Genome Biol. 5:RESEARCH008.1-RESEARCH008.16(2004).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[10]
STRUCTURE BY NMR OF 444-558.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the SH2 domain of human SH3BP2 protein.";
Submitted (NOV-2005) to the PDB data bank.
[11]
VARIANTS CRBM GLN-415; PRO-415; ARG-418; HIS-418; LEU-418; ARG-420 AND GLU-420.
DOI=10.1038/88832; PubMed=11381256 [NCBI, ExPASy, EBI, Israel, Japan]
Ueki Y., Tiziani V., Santanna C., Fukai N., Maulik C., Garfinkle J., Ninomiya C., doAmaral C., Peters H., Habal M., Rhee-Morris L., Doss J.B., Kreiborg S., Olsen B.R., Reichenberger E.;
"Mutations in the gene encoding c-Abl-binding protein SH3BP2 cause cherubism.";
Nat. Genet. 28:125-126(2001).
[12]
VARIANT CRBM ARG-420.
DOI=10.1002/ajmg.a.20226; PubMed=12900899 [NCBI, ExPASy, EBI, Israel, Japan]
Lo B., Faiyaz-Ul-Haque M., Kennedy S., Aviv R., Tsui L.-C., Teebi A.S.;
"Novel mutation in the gene encoding c-Abl-binding protein SH3BP2 causes cherubism.";
Am. J. Med. Genet. A 121:37-40(2003).
[13]
VARIANT CRBM ARG-418.
DOI=10.1597/1545-1569(2003)040<0632:AMMITS>2.0.CO;2; PubMed=14577811 [NCBI, ExPASy, EBI, Israel, Japan]
Imai Y., Kanno K., Moriya T., Kayano S., Seino H., Matsubara Y., Yamada A.;
"A missense mutation in the SH3BP2 gene on chromosome 4p16.3 found in a case of nonfamilial cherubism.";
Cleft Palate Craniofac. J. 40:632-638(2003).
Comments
  • FUNCTION: Binds differentially to the SH3 domains of certain proteins of signal transduction pathways. Binds to phosphatidylinositols; linking the hemopoietic tyrosine kinase fes to the cytoplasmic membrane in a phosphorylation dependent mechanism.
  • ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.
    NameLong
    Isoform IDP78314-1
    This is the isoform sequence displayed in this entry.
    NameShort
    Isoform IDP78314-2
    Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
    Features which should be applied to build the isoform sequence: VSP_004085, VSP_004086.
  • TISSUE SPECIFICITY: Expressed in a variety of tissues including lung, liver, skeletal muscle, kidney and pancreas.
  • DISEASE: Defects in SH3BP2 are the cause of cherubism (CRBM) [MIM:118400]. CRBM is an autosomal dominant inherited syndrome characterized by excessive bone degradation of the upper and lower jaws, which often begins around three years of age. It is followed by development of fibrous tissue masses, which causes a characteristic facial swelling.
  • SIMILARITY: Contains 1 PH domain.
  • SIMILARITY: Contains 1 SH2 domain.
  • WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=SH3BP2";.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF000936; AAB59973.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U56386; AAB72034.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB000462; BAA19119.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB000463; BAA19120.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK312286; BAG35213.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL121750; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
CH471131; EAW82509.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC022996; AAH22996.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00218997; -.
IPI00219071; -.
RefSeq NP_001116153.1; -.
NP_003014.3; -.
UniGene Hs.167679
3D structure databases
PDB
2CR4; NMR; -; A=446-558.[ExPASy / RCSB / EBI]
PDBsum 2CR4; -.
ModBase P78314.
Protein-protein interaction databases
IntAct P78314; 1.
PTM databases
PhosphoSite P78314; -.
Enzyme and pathway databases
Pathway_Interaction_DB tcrpathway; TCR signaling in naive CD4+ T cells.
Organism-specific databases
GeneCards GC04P002831; -.
H-InvDB HIX0004037; -.
HGNC HGNC:10825; SH3BP2.
GenAtlas SH3BP2.
MIM 118400; phenotype. [NCBI / EBI]
602104; gene. [NCBI / EBI]
Orphanet 184; Cherubism.
PharmGKB PA35733; -.
Gene expression databases
ArrayExpress P78314; -.
Bgee P78314; -.
CleanEx HS_SH3BP2; -.
GermOnline ENSG00000087266; Homo sapiens.
Ontologies
GO
GO:0017124; Molecular function: SH3 domain binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005070; Molecular function: SH3/SH2 adaptor activity (traceable author statement from ProtInc).
GO:0007165; Biological process: signal transduction (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR011993; PH_type.
IPR001849; Pleckstrin_homology.
IPR000980; SH2.
Graphical view of domain structure.
Gene3D G3DSA:2.30.29.30; PH_type; 1.
G3DSA:3.30.505.10; SH2; 1.
Pfam PF00169; PH; 1.
PF00017; SH2; 1.
Pfam graphical view of domain structure.
ProDom PD000093; SH2; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00233; PH; 1.
SM00252; SH2; 1.
SMART graphical view of domain structure.
PROSITE PS50003; PH_DOMAIN; 1.
PS50001; SH2; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE P78314; -.
Genome annotation databases
Ensembl ENSG00000087266; Homo sapiens. [Contig view]
GeneID 6452; -.
KEGG hsa:6452; -.
Phylogenomic databases
HOVERGEN P78314; -.
OMA P78314; GYNRQPR.
Other
NextBio 25079; -.
SOURCE SH3BP2; Homo sapiens.
ProtoNet P78314.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Disease mutation; Phosphoprotein; SH2 domain; SH3-binding.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   561  561     SH3 domain-binding protein 2. PRO_0000064365
DOMAIN   26   130  105     PH. 
DOMAIN   457   555  99     SH2. 
MOTIF   201   210  10     SH3-binding. 
COMPBIAS   205   212  8     Poly-Pro. 
COMPBIAS   236   240  5     Poly-Pro. 
MOD_RES   278   278        Phosphoserine. 
VAR_SEQ   81    97        VMRAAEETTSNNVFPFK -> QPRPQPAQALSQTEAGP (in isoform Short). VSP_004085
VAR_SEQ   98   561        Missing (in isoform Short). VSP_004086
VARIANT   415   415  1     R -> P (in CRBM). VAR_013257 
VARIANT   415   415  1     R -> Q (in CRBM). VAR_013258 
VARIANT   418   418  1     P -> H (in CRBM). VAR_013259 
VARIANT   418   418  1     P -> L (in CRBM). VAR_013260 
VARIANT   418   418  1     P -> R (in CRBM). VAR_013261 
VARIANT   420   420  1     G -> E (in CRBM). VAR_013262 
VARIANT   420   420  1     G -> R (in CRBM). VAR_013263 
CONFLICT   27    27        V -> L (in Ref. 3; AAB59973). 
CONFLICT   224   224        H -> N (in Ref. 3; AAB59973). 
CONFLICT   249   249        L -> R (in Ref. 3; AAB59973). 
CONFLICT   251   251        A -> P (in Ref. 3; AAB59973). 
TURN   455   457  3      
HELIX   464   474  11      
STRAND   485   489  5      
STRAND   496   501  6      
TURN   503   505  3      
STRAND   506   508  3      
STRAND   514   516  3      
STRAND   519   525  7      
STRAND   527   530  4      
HELIX   531   538  8      
STRAND   544   548  5      
STRAND   553   556  4      
Sequence information
Length: 561 AA [This is the length of the unprocessed precursor] Molecular weight: 62244 Da [This is the MW of the unprocessed precursor] CRC64: 69E6846A4F6D8F15 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAAEEMHWPV PMKAIGAQNL LTMPGGVAKA GYLHKKGGTQ LQLLKWPLRF VIIHKRCVYY 

        70         80         90        100        110        120 
FKSSTSASPQ GAFSLSGYNR VMRAAEETTS NNVFPFKIIH ISKKHRTWFF SASSEEERKS 

       130        140        150        160        170        180 
WMALLRREIG HFHEKKDLPL DTSDSSSDTD SFYGAVERPV DISLSPYPTD NEDYEHDDED 

       190        200        210        220        230        240 
DSYLEPDSPE PGRLEDALMH PPAYPPPPVP TPRKPAFSDM PRAHSFTSKG PGPLLPPPPP 

       250        260        270        280        290        300 
KHGLPDVGLA AEDSKRDPLC PRRAEPCPRV PATPRRMSDP PLSTMPTAPG LRKPPCFRES 

       310        320        330        340        350        360 
ASPSPEPWTP GHGACSTSSA AIMATATSRN CDKLKSFHLS PRGPPTSEPP PVPANKPKFL 

       370        380        390        400        410        420 
KIAEEDPPRE AAMPGLFVPP VAPRPPALKL PVPEAMARPA VLPRPEKPQL PHLQRSPPDG 

       430        440        450        460        470        480 
QSFRSFSFEK PRQPSQADTG GDDSDEDYEK VPLPNSVFVN TTESCEVERL FKATSPRGEP 

       490        500        510        520        530        540 
QDGLYCIRNS STKSGKVLVV WDETSNKVRN YRIFEKDSKF YLEGEVLFVS VGSMVEHYHT 

       550        560 
HVLPSHQSLL LRHPYGYTGP R 

P78314 in FASTA format

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