ID   SH2D5_HUMAN             Reviewed;         423 AA.
AC   Q6ZV89; B7Z3W3; Q5SSJ2;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 2.
DT   24-JAN-2024, entry version 158.
DE   RecName: Full=SH2 domain-containing protein 5 {ECO:0000312|HGNC:HGNC:28819};
GN   Name=SH2D5 {ECO:0000312|HGNC:HGNC:28819};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Hippocampus, and Thalamus;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [5]
RP   INTERACTION WITH BCR.
RX   PubMed=25331951; DOI=10.1074/jbc.m114.615112;
RA   Gray E.J., Petsalaki E., James D.A., Bagshaw R.D., Stacey M.M., Rocks O.,
RA   Gingras A.C., Pawson T.;
RT   "src homology 2 domain containing protein 5 (sh2d5) binds the breakpoint
RT   cluster region protein, BCR, and regulates levels of Rac1-GTP.";
RL   J. Biol. Chem. 289:35397-35408(2014).
CC   -!- FUNCTION: May be involved in synaptic plasticity regulation through the
CC       control of Rac-GTP levels. {ECO:0000250|UniProtKB:Q8JZW5}.
CC   -!- SUBUNIT: Interacts with BCR. {ECO:0000269|PubMed:25331951}.
CC   -!- INTERACTION:
CC       Q6ZV89-1; P11274: BCR; NbExp=2; IntAct=EBI-15101685, EBI-712838;
CC   -!- SUBCELLULAR LOCATION: Postsynaptic density
CC       {ECO:0000250|UniProtKB:Q8JZW5}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6ZV89-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6ZV89-2; Sequence=VSP_045938;
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC85974.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AK124869; BAC85974.1; ALT_INIT; mRNA.
DR   EMBL; AK296431; BAH12349.1; -; mRNA.
DR   EMBL; AL663074; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471134; EAW94947.1; -; Genomic_DNA.
DR   CCDS; CCDS41280.1; -. [Q6ZV89-2]
DR   CCDS; CCDS44080.1; -. [Q6ZV89-1]
DR   RefSeq; NP_001096630.1; NM_001103160.1. [Q6ZV89-2]
DR   RefSeq; NP_001096631.1; NM_001103161.1. [Q6ZV89-1]
DR   RefSeq; XP_011539761.1; XM_011541459.1.
DR   RefSeq; XP_011539762.1; XM_011541460.1. [Q6ZV89-1]
DR   RefSeq; XP_011539763.1; XM_011541461.2. [Q6ZV89-1]
DR   AlphaFoldDB; Q6ZV89; -.
DR   SMR; Q6ZV89; -.
DR   BioGRID; 134738; 9.
DR   IntAct; Q6ZV89; 5.
DR   MINT; Q6ZV89; -.
DR   STRING; 9606.ENSP00000406026; -.
DR   iPTMnet; Q6ZV89; -.
DR   PhosphoSitePlus; Q6ZV89; -.
DR   BioMuta; SH2D5; -.
DR   DMDM; 363548475; -.
DR   EPD; Q6ZV89; -.
DR   jPOST; Q6ZV89; -.
DR   MassIVE; Q6ZV89; -.
DR   PaxDb; 9606-ENSP00000406026; -.
DR   PeptideAtlas; Q6ZV89; -.
DR   ProteomicsDB; 68401; -. [Q6ZV89-1]
DR   Antibodypedia; 48002; 120 antibodies from 25 providers.
DR   DNASU; 400745; -.
DR   Ensembl; ENST00000375031.5; ENSP00000364171.1; ENSG00000189410.12. [Q6ZV89-2]
DR   Ensembl; ENST00000444387.7; ENSP00000406026.2; ENSG00000189410.12. [Q6ZV89-1]
DR   GeneID; 400745; -.
DR   KEGG; hsa:400745; -.
DR   MANE-Select; ENST00000444387.7; ENSP00000406026.2; NM_001103161.2; NP_001096631.1.
DR   UCSC; uc001bdt.1; human. [Q6ZV89-1]
DR   AGR; HGNC:28819; -.
DR   CTD; 400745; -.
DR   DisGeNET; 400745; -.
DR   GeneCards; SH2D5; -.
DR   HGNC; HGNC:28819; SH2D5.
DR   HPA; ENSG00000189410; Tissue enhanced (brain, testis).
DR   neXtProt; NX_Q6ZV89; -.
DR   OpenTargets; ENSG00000189410; -.
DR   PharmGKB; PA142670927; -.
DR   VEuPathDB; HostDB:ENSG00000189410; -.
DR   eggNOG; ENOG502RXFM; Eukaryota.
DR   GeneTree; ENSGT00510000048936; -.
DR   HOGENOM; CLU_053535_0_0_1; -.
DR   InParanoid; Q6ZV89; -.
DR   OMA; QDCGPEG; -.
DR   OrthoDB; 5298750at2759; -.
DR   PhylomeDB; Q6ZV89; -.
DR   TreeFam; TF334487; -.
DR   PathwayCommons; Q6ZV89; -.
DR   SignaLink; Q6ZV89; -.
DR   BioGRID-ORCS; 400745; 15 hits in 1147 CRISPR screens.
DR   GenomeRNAi; 400745; -.
DR   Pharos; Q6ZV89; Tdark.
DR   PRO; PR:Q6ZV89; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q6ZV89; Protein.
DR   Bgee; ENSG00000189410; Expressed in nucleus accumbens and 108 other cell types or tissues.
DR   ExpressionAtlas; Q6ZV89; baseline and differential.
DR   GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
DR   CDD; cd13157; PTB_tensin-related; 1.
DR   CDD; cd00173; SH2; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 3.30.505.10; SH2 domain; 1.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR006020; PTB/PI_dom.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR036860; SH2_dom_sf.
DR   PANTHER; PTHR15832:SF3; SH2 DOMAIN-CONTAINING PROTEIN 5; 1.
DR   PANTHER; PTHR15832; SHC (SRC HOMOLOGY DOMAIN C-TERMINAL) ADAPTOR HOMOLOG; 1.
DR   SMART; SM00462; PTB; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF55550; SH2 domain; 1.
DR   PROSITE; PS01179; PID; 1.
DR   PROSITE; PS50001; SH2; 1.
DR   Genevisible; Q6ZV89; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Reference proteome; SH2 domain; Synapse.
FT   CHAIN           1..423
FT                   /note="SH2 domain-containing protein 5"
FT                   /id="PRO_0000231581"
FT   DOMAIN          28..146
FT                   /note="PID"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT   DOMAIN          296..392
FT                   /note="SH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT   REGION          392..423
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..84
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_045938"
SQ   SEQUENCE   423 AA;  46797 MW;  BD0C7D55C7FF8FDB CRC64;
     MQKAGAGGRR ASDCGLAPHR PRCITKFAQY VGSFPVDDLD TQESVWLVQQ QLWALKDCPR
     RRAVILKFSL QGLKIYSGEG EVLLMAHALR RILYSTWCPA DCQFAFMARN PRSPASKLFC
     HLFVGSQPGE VQILHLLLCR SFQLAYLLQH PEERAQPEPC PGPTGEVPLK PLSSSGGLVR
     EPFGRDQLSQ NVHALVSFRR LPAEGLVGSG KELPESEGRA RHARLGNPYC SPTLVRKKAI
     RSKVIRSGAY RGCTYETQLQ LSAREAFPAA WEAWPRGPGG HSCLVESEGS LTENIWAFAG
     ISRPCALALL RRDVLGAFLL WPELGASGQW CLSVRTQCGV VPHQVFRNHL GRYCLEHLPA
     EFPSLEALVE NHAVTERSLF CPLDMGRLNP TYEEQDCGPP GRPPRTLRPL SHAKSEAELQ
     GLG
//