STRP1_HUMAN
ID STRP1_HUMAN Reviewed; 837 AA.
AC Q5VSL9; Q0V925; Q5VSL8; Q658K2; Q6ZV31; Q8N598; Q96SN2; Q9C0A2;
DT 02-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Striatin-interacting protein 1;
DE AltName: Full=Protein FAM40A;
GN Name=STRIP1; Synonyms=FAM40A, KIAA1761;
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=Brain;
RX PubMed=11214970; DOI=10.1093/dnares/7.6.347;
RA Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:347-355(2000).
RN [2]
RP SEQUENCE REVISION.
RA Ohara O., Nagase T., Kikuno R.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta, and Uterus;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP 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 [12]
RP INTERACTION WITH CTTNBP2NL.
RX PubMed=18782753; DOI=10.1074/mcp.m800266-mcp200;
RA Goudreault M., D'Ambrosio L.M., Kean M.J., Mullin M.J., Larsen B.G.,
RA Sanchez A., Chaudhry S., Chen G.I., Sicheri F., Nesvizhskii A.I.,
RA Aebersold R., Raught B., Gingras A.C.;
RT "A PP2A phosphatase high density interaction network identifies a novel
RT striatin-interacting phosphatase and kinase complex linked to the cerebral
RT cavernous malformation 3 (CCM3) protein.";
RL Mol. Cell. Proteomics 8:157-171(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [16]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21834987; DOI=10.1186/1741-7007-9-54;
RA Bai S.W., Herrera-Abreu M.T., Rohn J.L., Racine V., Tajadura V.,
RA Suryavanshi N., Bechtel S., Wiemann S., Baum B., Ridley A.J.;
RT "Identification and characterization of a set of conserved and new
RT regulators of cytoskeletal organisation, cell morphology and migration.";
RL BMC Biol. 9:54-54(2011).
RN [17]
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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335, AND IDENTIFICATION BY
RP 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 [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59 AND SER-335, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59; SER-335 AND SER-788, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
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 [22]
RP INTERACTION WITH CDC42BPB; STRN3 AND SIKE1.
RX PubMed=25743393; DOI=10.1038/ncomms7449;
RA Lant B., Yu B., Goudreault M., Holmyard D., Knight J.D., Xu P., Zhao L.,
RA Chin K., Wallace E., Zhen M., Gingras A.C., Derry W.B.;
RT "CCM-3/STRIPAK promotes seamless tube extension through endocytic
RT recycling.";
RL Nat. Commun. 6:6449-6449(2015).
RN [23]
RP VARIANT ASN-628.
RX PubMed=26566883; DOI=10.1136/jmedgenet-2015-103179;
RA Rafiullah R., Aslamkhan M., Paramasivam N., Thiel C., Mustafa G.,
RA Wiemann S., Schlesner M., Wade R.C., Rappold G.A., Berkel S.;
RT "Homozygous missense mutation in the LMAN2L gene segregates with
RT intellectual disability in a large consanguineous Pakistani family.";
RL J. Med. Genet. 53:138-144(2016).
CC -!- FUNCTION: Plays a role in the regulation of cell morphology and
CC cytoskeletal organization. Required in the cortical actin filament
CC dynamics and cell shape. {ECO:0000269|PubMed:21834987}.
CC -!- SUBUNIT: Component of striatin-interacting phosphatase and kinase
CC (STRIPAK) complex (By similarity). Interacts with CDC42BPB
CC (PubMed:25743393). Interacts with CTTNBP2NL (PubMed:18782753).
CC {ECO:0000250|UniProtKB:Q8C079, ECO:0000269|PubMed:18782753,
CC ECO:0000269|PubMed:25743393}.
CC -!- INTERACTION:
CC Q5VSL9; Q9P2B4: CTTNBP2NL; NbExp=4; IntAct=EBI-1773588, EBI-1774273;
CC Q5VSL9; P67775: PPP2CA; NbExp=7; IntAct=EBI-1773588, EBI-712311;
CC Q5VSL9; P62714: PPP2CB; NbExp=5; IntAct=EBI-1773588, EBI-1044367;
CC Q5VSL9; Q9Y6E0: STK24; NbExp=4; IntAct=EBI-1773588, EBI-740175;
CC Q5VSL9; Q9P289: STK26; NbExp=3; IntAct=EBI-1773588, EBI-618239;
CC Q5VSL9; Q9Y228: TRAF3IP3; NbExp=2; IntAct=EBI-1773588, EBI-765817;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21834987}.
CC Note=Enriched on the plasma membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q5VSL9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5VSL9-2; Sequence=VSP_014857;
CC Name=3;
CC IsoId=Q5VSL9-3; Sequence=VSP_014856, VSP_014860, VSP_014861,
CC VSP_014862;
CC Name=4;
CC IsoId=Q5VSL9-4; Sequence=VSP_014858, VSP_014859;
CC -!- SIMILARITY: Belongs to the STRIP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH32644.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB051548; BAB21852.2; -; mRNA.
DR EMBL; AK027649; BAB55265.1; -; mRNA.
DR EMBL; AK125054; BAC86034.1; -; mRNA.
DR EMBL; AL834196; CAH56368.1; -; mRNA.
DR EMBL; AL772411; CAH70967.1; -; Genomic_DNA.
DR EMBL; AL160006; CAH70967.1; JOINED; Genomic_DNA.
DR EMBL; AL772411; CAH70968.1; -; Genomic_DNA.
DR EMBL; AL160006; CAH70968.1; JOINED; Genomic_DNA.
DR EMBL; AL160006; CAI22715.1; -; Genomic_DNA.
DR EMBL; AL772411; CAI22715.1; JOINED; Genomic_DNA.
DR EMBL; AL160006; CAI22716.1; -; Genomic_DNA.
DR EMBL; AL772411; CAI22716.1; JOINED; Genomic_DNA.
DR EMBL; BC032644; AAH32644.1; ALT_INIT; mRNA.
DR EMBL; BC094786; AAH94786.1; -; mRNA.
DR EMBL; BC119814; AAI19815.1; -; mRNA.
DR EMBL; BC121793; AAI21794.1; -; mRNA.
DR CCDS; CCDS30798.1; -. [Q5VSL9-1]
DR CCDS; CCDS59197.1; -. [Q5VSL9-2]
DR RefSeq; NP_001257697.1; NM_001270768.1. [Q5VSL9-2]
DR RefSeq; NP_149079.2; NM_033088.3. [Q5VSL9-1]
DR PDB; 7K36; EM; 3.30 A; I=1-837.
DR PDBsum; 7K36; -.
DR AlphaFoldDB; Q5VSL9; -.
DR SMR; Q5VSL9; -.
DR BioGRID; 124497; 87.
DR DIP; DIP-51621N; -.
DR IntAct; Q5VSL9; 49.
DR MINT; Q5VSL9; -.
DR STRING; 9606.ENSP00000358810; -.
DR iPTMnet; Q5VSL9; -.
DR PhosphoSitePlus; Q5VSL9; -.
DR BioMuta; STRIP1; -.
DR DMDM; 71648671; -.
DR EPD; Q5VSL9; -.
DR jPOST; Q5VSL9; -.
DR MassIVE; Q5VSL9; -.
DR MaxQB; Q5VSL9; -.
DR PaxDb; Q5VSL9; -.
DR PeptideAtlas; Q5VSL9; -.
DR PRIDE; Q5VSL9; -.
DR ProteomicsDB; 65267; -. [Q5VSL9-1]
DR ProteomicsDB; 65268; -. [Q5VSL9-2]
DR ProteomicsDB; 65269; -. [Q5VSL9-3]
DR ProteomicsDB; 65270; -. [Q5VSL9-4]
DR Antibodypedia; 53747; 184 antibodies from 21 providers.
DR DNASU; 85369; -.
DR Ensembl; ENST00000369795.8; ENSP00000358810.3; ENSG00000143093.15. [Q5VSL9-1]
DR Ensembl; ENST00000369796.5; ENSP00000358811.1; ENSG00000143093.15. [Q5VSL9-2]
DR Ensembl; ENST00000485775.5; ENSP00000476025.1; ENSG00000143093.15. [Q5VSL9-4]
DR GeneID; 85369; -.
DR KEGG; hsa:85369; -.
DR MANE-Select; ENST00000369795.8; ENSP00000358810.3; NM_033088.4; NP_149079.2.
DR UCSC; uc001dyz.2; human. [Q5VSL9-1]
DR CTD; 85369; -.
DR DisGeNET; 85369; -.
DR GeneCards; STRIP1; -.
DR HGNC; HGNC:25916; STRIP1.
DR HPA; ENSG00000143093; Low tissue specificity.
DR MIM; 617918; gene.
DR neXtProt; NX_Q5VSL9; -.
DR OpenTargets; ENSG00000143093; -.
DR PharmGKB; PA134939426; -.
DR VEuPathDB; HostDB:ENSG00000143093; -.
DR eggNOG; KOG3680; Eukaryota.
DR GeneTree; ENSGT00400000022095; -.
DR HOGENOM; CLU_011008_1_0_1; -.
DR InParanoid; Q5VSL9; -.
DR OMA; KPYSWRN; -.
DR OrthoDB; 1095402at2759; -.
DR PhylomeDB; Q5VSL9; -.
DR TreeFam; TF314205; -.
DR PathwayCommons; Q5VSL9; -.
DR SignaLink; Q5VSL9; -.
DR BioGRID-ORCS; 85369; 292 hits in 1083 CRISPR screens.
DR ChiTaRS; STRIP1; human.
DR GeneWiki; FAM40A; -.
DR GenomeRNAi; 85369; -.
DR Pharos; Q5VSL9; Tbio.
DR PRO; PR:Q5VSL9; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q5VSL9; protein.
DR Bgee; ENSG00000143093; Expressed in cortical plate and 160 other tissues.
DR Genevisible; Q5VSL9; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0031267; F:small GTPase binding; IEA:Ensembl.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0007010; P:cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0022604; P:regulation of cell morphogenesis; IMP:UniProtKB.
DR InterPro; IPR040185; Far11/STRP.
DR InterPro; IPR021819; Far11/STRP_C.
DR InterPro; IPR012486; Far11/STRP_N.
DR PANTHER; PTHR13239; PTHR13239; 1.
DR Pfam; PF11882; DUF3402; 2.
DR Pfam; PF07923; N1221; 1.
DR SMART; SM01293; DUF3402; 1.
DR SMART; SM01292; N1221; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..837
FT /note="Striatin-interacting protein 1"
FT /id="PRO_0000187017"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 333..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..33
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..67
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..377
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..392
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19367720, ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 339
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C079"
FT MOD_RES 788
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..264
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_014856"
FT VAR_SEQ 1..95
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_014857"
FT VAR_SEQ 194..212
FT /note="DNSAACSSAVRKPAISLAD -> EHCCVRPAVSALAGGQAQD (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_014858"
FT VAR_SEQ 213..837
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_014859"
FT VAR_SEQ 596
FT /note="Q -> QVPTGLSLLSCGLGPRALLLLQPTRTGALAFDPLELCMNVLRHGPSA
FT KAFHPWRKEGKVPRAAPFFFFFFSCWLQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_014860"
FT VAR_SEQ 630
FT /note="S -> R (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_014861"
FT VAR_SEQ 631..837
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_014862"
FT VARIANT 628
FT /note="K -> N"
FT /evidence="ECO:0000269|PubMed:26566883"
FT /id="VAR_076430"
FT CONFLICT 397
FT /note="P -> L (in Ref. 3; BAC86034)"
FT /evidence="ECO:0000305"
FT CONFLICT 744
FT /note="R -> Q (in Ref. 3; BAB55265)"
FT /evidence="ECO:0000305"
FT HELIX 78..83
FT /evidence="ECO:0007829|PDB:7K36"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:7K36"
FT HELIX 93..108
FT /evidence="ECO:0007829|PDB:7K36"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:7K36"
FT HELIX 119..132
FT /evidence="ECO:0007829|PDB:7K36"
FT HELIX 138..153
FT /evidence="ECO:0007829|PDB:7K36"
FT HELIX 162..179
FT /evidence="ECO:0007829|PDB:7K36"
FT HELIX 181..193
FT /evidence="ECO:0007829|PDB:7K36"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:7K36"
FT HELIX 215..232
FT /evidence="ECO:0007829|PDB:7K36"
FT HELIX 242..252
FT /evidence="ECO:0007829|PDB:7K36"
FT HELIX 262..274
FT /evidence="ECO:0007829|PDB:7K36"
FT HELIX 283..298
FT /evidence="ECO:0007829|PDB:7K36"
FT HELIX 301..314
FT /evidence="ECO:0007829|PDB:7K36"
FT HELIX 324..329
FT /evidence="ECO:0007829|PDB:7K36"
FT HELIX 430..444
FT /evidence="ECO:0007829|PDB:7K36"
FT STRAND 445..447
FT /evidence="ECO:0007829|PDB:7K36"
FT STRAND 457..459
FT /evidence="ECO:0007829|PDB:7K36"
FT HELIX 461..472
FT /evidence="ECO:0007829|PDB:7K36"
FT HELIX 478..491
FT /evidence="ECO:0007829|PDB:7K36"
FT STRAND 492..496
FT /evidence="ECO:0007829|PDB:7K36"
FT HELIX 505..513
FT /evidence="ECO:0007829|PDB:7K36"
FT HELIX 514..516
FT /evidence="ECO:0007829|PDB:7K36"
FT HELIX 517..531
FT /evidence="ECO:0007829|PDB:7K36"
FT HELIX 544..547
FT /evidence="ECO:0007829|PDB:7K36"
FT HELIX 557..592
FT /evidence="ECO:0007829|PDB:7K36"
FT HELIX 594..606
FT /evidence="ECO:0007829|PDB:7K36"
FT HELIX 609..616
FT /evidence="ECO:0007829|PDB:7K36"
FT HELIX 621..626
FT /evidence="ECO:0007829|PDB:7K36"
FT HELIX 662..678
FT /evidence="ECO:0007829|PDB:7K36"
FT STRAND 679..681
FT /evidence="ECO:0007829|PDB:7K36"
FT HELIX 683..691
FT /evidence="ECO:0007829|PDB:7K36"
FT HELIX 695..701
FT /evidence="ECO:0007829|PDB:7K36"
FT HELIX 707..720
FT /evidence="ECO:0007829|PDB:7K36"
FT HELIX 722..724
FT /evidence="ECO:0007829|PDB:7K36"
FT HELIX 725..731
FT /evidence="ECO:0007829|PDB:7K36"
FT HELIX 734..742
FT /evidence="ECO:0007829|PDB:7K36"
FT HELIX 764..783
FT /evidence="ECO:0007829|PDB:7K36"
FT TURN 785..787
FT /evidence="ECO:0007829|PDB:7K36"
FT STRAND 790..792
FT /evidence="ECO:0007829|PDB:7K36"
FT HELIX 815..822
FT /evidence="ECO:0007829|PDB:7K36"
SQ SEQUENCE 837 AA; 95576 MW; 5F9BA1D4C7DE6925 CRC64;
MEPAVGGPGP LIVNNKQPQP PPPPPPAAAQ PPPGAPRAAA GLLPGGKARE FNRNQRKDSE
GYSESPDLEF EYADTDKWAA ELSELYSYTE GPEFLMNRKC FEEDFRIHVT DKKWTELDTN
QHRTHAMRLL DGLEVTAREK RLKVARAILY VAQGTFGECS SEAEVQSWMR YNIFLLLEVG
TFNALVELLN MEIDNSAACS SAVRKPAISL ADSTDLRVLL NIMYLIVETV HQECEGDKAE
WRTMRQTFRA ELGSPLYNNE PFAIMLFGMV TKFCSGHAPH FPMKKVLLLL WKTVLCTLGG
FEELQSMKAE KRSILGLPPL PEDSIKVIRN MRAASPPASA SDLIEQQQKR GRREHKALIK
QDNLDAFNER DPYKADDSRE EEEENDDDNS LEGETFPLER DEVMPPPLQH PQTDRLTCPK
GLPWAPKVRE KDIEMFLESS RSKFIGYTLG SDTNTVVGLP RPIHESIKTL KQHKYTSIAE
VQAQMEEEYL RSPLSGGEEE VEQVPAETLY QGLLPSLPQY MIALLKILLA AAPTSKAKTD
SINILADVLP EEMPTTVLQS MKLGVDVNRH KEVIVKAISA VLLLLLKHFK LNHVYQFEYM
AQHLVFANCI PLILKFFNQN IMSYITAKNS ISVLDYPHCV VHELPELTAE SLEAGDSNQF
CWRNLFSCIN LLRILNKLTK WKHSRTMMLV VFKSAPILKR ALKVKQAMMQ LYVLKLLKVQ
TKYLGRQWRK SNMKTMSAIY QKVRHRLNDD WAYGNDLDAR PWDFQAEECA LRANIERFNA
RRYDRAHSNP DFLPVDNCLQ SVLGQRVDLP EDFQMNYDLW LEREVFSKPI SWEELLQ
