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Database: UniProt
Entry: A0A0U1RQI5_HUMAN
LinkDB: A0A0U1RQI5_HUMAN
Original site: A0A0U1RQI5_HUMAN 
ID   A0A0U1RQI5_HUMAN        Unreviewed;       507 AA.
AC   A0A0U1RQI5;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   SubName: Full=Sorbin and SH3 domain containing 1 {ECO:0000313|Ensembl:ENSP00000489022.1};
DE   Flags: Fragment;
GN   Name=SORBS1 {ECO:0000313|Ensembl:ENSP00000489022.1};
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 {ECO:0000313|Ensembl:ENSP00000489022.1, ECO:0000313|Proteomes:UP000005640};
RN   [1] {ECO:0000313|Ensembl:ENSP00000489022.1, ECO:0000313|Proteomes:UP000005640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164054; DOI=10.1038/nature02462;
RA   Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA   Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA   Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA   Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA   Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA   Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA   Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA   Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA   Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA   Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA   Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA   Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA   McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA   Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA   Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA   Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA   Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA   Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA   Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA   Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA   Durbin R., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 10.";
RL   Nature 429:375-381(2004).
RN   [2] {ECO:0007829|PubMed:18669648}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [3] {ECO:0007829|PubMed:20068231}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [4] {ECO:0007829|PubMed:21406692}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [5] {ECO:0007829|PubMed:23186163}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=23186163;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [6] {ECO:0007829|PubMed:24275569}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [7] {ECO:0000313|Ensembl:ENSP00000489022.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   EMBL; AL157890; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL158165; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   MassIVE; A0A0U1RQI5; -.
DR   PeptideAtlas; A0A0U1RQI5; -.
DR   Antibodypedia; 30624; 272 antibodies from 31 providers.
DR   Ensembl; ENST00000634504.1; ENSP00000489022.1; ENSG00000095637.23.
DR   HGNC; HGNC:14565; SORBS1.
DR   VEuPathDB; HostDB:ENSG00000095637; -.
DR   GeneTree; ENSGT00940000158658; -.
DR   ChiTaRS; SORBS1; human.
DR   Proteomes; UP000005640; Chromosome 10.
DR   Bgee; ENSG00000095637; Expressed in blood vessel layer and 200 other cell types or tissues.
DR   ExpressionAtlas; A0A0U1RQI5; baseline and differential.
DR   CDD; cd11919; SH3_Sorbs1_1; 1.
DR   CDD; cd11922; SH3_Sorbs1_2; 1.
DR   CDD; cd11916; SH3_Sorbs1_3; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 3.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR035606; SORBS1_SH3.
DR   InterPro; IPR035610; SORBS1_SH3_1.
DR   InterPro; IPR035611; SORBS1_SH3_2.
DR   PANTHER; PTHR14167; SH3 DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR14167:SF64; SORBIN AND SH3 DOMAIN-CONTAINING PROTEIN 1; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   Pfam; PF14604; SH3_9; 1.
DR   PRINTS; PR00499; P67PHOX.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00326; SH3; 3.
DR   SUPFAM; SSF50044; SH3-domain; 3.
DR   PROSITE; PS50002; SH3; 3.
PE   1: Evidence at protein level;
KW   Proteomics identification {ECO:0007829|EPD:A0A0U1RQI5,
KW   ECO:0007829|MaxQB:A0A0U1RQI5};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          266..325
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          340..401
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          446..507
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          26..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          166..189
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          415..443
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        42..62
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        171..185
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|Ensembl:ENSP00000489022.1"
SQ   SEQUENCE   507 AA;  58005 MW;  89B46606E87CEF88 CRC64;
     XPLSVPRSKS EMSYIDGEKV VKRSATLPLP ARSSSLKSSS ERNDWEPPDK KVDTRKYRAE
     PKSIYEYQPG KSSVLTNEKM SRDISPEEID LKNEPWYKFF SELEFGKPSS AISPTPEISS
     ETPGYIYSSN FHAVKRESDG APGDLTSLEN ERQIYKSVLE GGDIPLQGLS GLKRPSSSAS
     TKDSESPRHF IPADYLESTE EFIRRRHDDK EKLLADQRRL KREQEEADIA ARRHTGVIPT
     HHQFITNERF GDLLNIDDTA KRKSGSEMRP ARAKFDFKAQ TLKELPLQKG DIVYIYKQID
     QNWYEGEHHG RVGIFPRTYI ELLPPAEKAQ PKKLTPVQVL EYGEAIAKFN FNGDTQVEMS
     FRKGERITLL RQVDENWYEG RIPGTSRQGI FPITYVDVIK RPLVKNPVDY MDLPFSSSPS
     RSATASPQQP QAQQRRVTPD RSQTSQDLFS YQALYSYIPQ NDDELELRDG DIVDVMEKCD
     DGWFVGTSRR TKQFGTFPGN YVKPLYL
//
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