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SH3L2_HUMAN
ID   SH3L2_HUMAN             Reviewed;         107 AA.
AC   Q9UJC5; A8MQU2; Q2VPC2; Q5VV96; Q6NSK8; Q6P9E8; Q7Z734; Q8IWD3; Q9BPY5;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-2002, sequence version 2.
DT   03-AUG-2022, entry version 162.
DE   RecName: Full=SH3 domain-binding glutamic acid-rich-like protein 2;
DE   AltName: Full=Fovea-associated SH3 domain-binding protein;
GN   Name=SH3BGRL2; Synonyms=FASH3;
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 [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=12095696; DOI=10.1016/s0378-1119(02)00602-9;
RA   Mazzocco M., Maffei M., Egeo A., Vergano A., Arrigo P., Di Lisi R.,
RA   Ghiotto F., Scartezzini P.;
RT   "The identification of a novel human homologue of the SH3 binding glutamic
RT   acid-rich (SH3BGR) gene establishes a new family of highly conserved small
RT   proteins related to Thioredoxin Superfamily.";
RL   Gene 291:233-239(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Bowes Rickman C., Yarovinsky T.O., McKay B.S., Stone E.M., Ritter R.,
RA   Rickman D.W., Edwards A.O.;
RT   "Characterization of a novel candidate gene, FASH3, expressed in the
RT   primate fovea and linked to the disease gene, ELOVL4, associated with
RT   Stargardt-like dominant progressive macular dystrophy.";
RL   Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain, Eye, and Placenta;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [8]
RP   STRUCTURE BY NMR OF 1-98.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the SH3 domain-binding glutamic acid-rich-like
RT   protein 2.";
RL   Submitted (NOV-2005) to the PDB data bank.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12095696}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain, placenta, liver and
CC       kidney. Expressed in retina. {ECO:0000269|PubMed:12095696}.
CC   -!- SIMILARITY: Belongs to the SH3BGR family. {ECO:0000305}.
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DR   EMBL; AJ297972; CAC35771.1; -; mRNA.
DR   EMBL; AF340151; AAK37526.1; -; mRNA.
DR   EMBL; AK311757; BAG34700.1; -; mRNA.
DR   EMBL; AL035700; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL451064; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471051; EAW48703.1; -; Genomic_DNA.
DR   EMBL; BC040489; AAH40489.2; -; mRNA.
DR   EMBL; BC052987; AAH52987.2; -; mRNA.
DR   EMBL; BC060799; AAH60799.2; -; mRNA.
DR   EMBL; BC070059; AAH70059.2; -; mRNA.
DR   EMBL; BC109043; AAI09044.2; -; mRNA.
DR   EMBL; BC109044; AAI09045.2; -; mRNA.
DR   CCDS; CCDS4991.1; -.
DR   RefSeq; NP_113657.1; NM_031469.3.
DR   RefSeq; XP_016866833.1; XM_017011344.1.
DR   PDB; 2CT6; NMR; -; A=1-98.
DR   PDBsum; 2CT6; -.
DR   AlphaFoldDB; Q9UJC5; -.
DR   BMRB; Q9UJC5; -.
DR   SMR; Q9UJC5; -.
DR   BioGRID; 123733; 20.
DR   IntAct; Q9UJC5; 7.
DR   STRING; 9606.ENSP00000358853; -.
DR   iPTMnet; Q9UJC5; -.
DR   PhosphoSitePlus; Q9UJC5; -.
DR   BioMuta; SH3BGRL2; -.
DR   DMDM; 24638476; -.
DR   UCD-2DPAGE; Q9UJC5; -.
DR   EPD; Q9UJC5; -.
DR   jPOST; Q9UJC5; -.
DR   MassIVE; Q9UJC5; -.
DR   MaxQB; Q9UJC5; -.
DR   PaxDb; Q9UJC5; -.
DR   PeptideAtlas; Q9UJC5; -.
DR   PRIDE; Q9UJC5; -.
DR   ProteomicsDB; 84618; -.
DR   TopDownProteomics; Q9UJC5; -.
DR   Antibodypedia; 64235; 27 antibodies from 15 providers.
DR   DNASU; 83699; -.
DR   Ensembl; ENST00000369838.6; ENSP00000358853.4; ENSG00000198478.8.
DR   GeneID; 83699; -.
DR   KEGG; hsa:83699; -.
DR   MANE-Select; ENST00000369838.6; ENSP00000358853.4; NM_031469.4; NP_113657.1.
DR   UCSC; uc003piz.2; human.
DR   CTD; 83699; -.
DR   DisGeNET; 83699; -.
DR   GeneCards; SH3BGRL2; -.
DR   HGNC; HGNC:15567; SH3BGRL2.
DR   HPA; ENSG00000198478; Tissue enhanced (salivary).
DR   MIM; 615678; gene.
DR   neXtProt; NX_Q9UJC5; -.
DR   OpenTargets; ENSG00000198478; -.
DR   PharmGKB; PA37978; -.
DR   VEuPathDB; HostDB:ENSG00000198478; -.
DR   eggNOG; KOG4023; Eukaryota.
DR   GeneTree; ENSGT00940000159157; -.
DR   HOGENOM; CLU_084862_3_0_1; -.
DR   InParanoid; Q9UJC5; -.
DR   OMA; MYKNIPK; -.
DR   OrthoDB; 1508713at2759; -.
DR   PhylomeDB; Q9UJC5; -.
DR   TreeFam; TF105574; -.
DR   PathwayCommons; Q9UJC5; -.
DR   SignaLink; Q9UJC5; -.
DR   BioGRID-ORCS; 83699; 5 hits in 1072 CRISPR screens.
DR   ChiTaRS; SH3BGRL2; human.
DR   EvolutionaryTrace; Q9UJC5; -.
DR   GenomeRNAi; 83699; -.
DR   Pharos; Q9UJC5; Tdark.
DR   PRO; PR:Q9UJC5; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; Q9UJC5; protein.
DR   Bgee; ENSG00000198478; Expressed in parotid gland and 186 other tissues.
DR   Genevisible; Q9UJC5; HS.
DR   GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR   CDD; cd03030; GRX_SH3BGR; 1.
DR   InterPro; IPR006993; Glut_rich_SH3-bd.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF04908; SH3BGR; 1.
DR   PIRSF; PIRSF008142; SH3-bind_E-rich_L; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Nucleus; Reference proteome; SH3-binding.
FT   CHAIN           1..107
FT                   /note="SH3 domain-binding glutamic acid-rich-like protein
FT                   2"
FT                   /id="PRO_0000220747"
FT   MOTIF           61..67
FT                   /note="SH3-binding"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        7
FT                   /note="I -> V (in Ref. 6; AAH70059)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        39
FT                   /note="I -> T (in Ref. 6; AAH40489)"
FT                   /evidence="ECO:0000305"
FT   STRAND          3..7
FT                   /evidence="ECO:0007829|PDB:2CT6"
FT   HELIX           14..29
FT                   /evidence="ECO:0007829|PDB:2CT6"
FT   STRAND          34..38
FT                   /evidence="ECO:0007829|PDB:2CT6"
FT   TURN            39..41
FT                   /evidence="ECO:0007829|PDB:2CT6"
FT   HELIX           43..51
FT                   /evidence="ECO:0007829|PDB:2CT6"
FT   TURN            55..57
FT                   /evidence="ECO:0007829|PDB:2CT6"
FT   STRAND          60..63
FT                   /evidence="ECO:0007829|PDB:2CT6"
FT   STRAND          68..71
FT                   /evidence="ECO:0007829|PDB:2CT6"
FT   STRAND          74..78
FT                   /evidence="ECO:0007829|PDB:2CT6"
FT   HELIX           79..86
FT                   /evidence="ECO:0007829|PDB:2CT6"
FT   TURN            87..89
FT                   /evidence="ECO:0007829|PDB:2CT6"
FT   HELIX           91..95
FT                   /evidence="ECO:0007829|PDB:2CT6"
SQ   SEQUENCE   107 AA;  12326 MW;  D160736103FA8635 CRC64;
     MVIRVFIASS SGFVAIKKKQ QDVVRFLEAN KIEFEEVDIT MSEEQRQWMY KNVPPEKKPT
     QGNPLPPQIF NGDRYCGDYD SFFESKESNT VFSFLGLKPR LASKAEP
 
 
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