SI1L1_HUMAN
ID SI1L1_HUMAN Reviewed; 1804 AA.
AC O43166; J3KP19; O95321; Q9UDU4; Q9UNU4;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 4.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Signal-induced proliferation-associated 1-like protein 1;
DE Short=SIPA1-like protein 1;
DE AltName: Full=High-risk human papilloma viruses E6 oncoproteins targeted protein 1;
DE Short=E6-targeted protein 1;
GN Name=SIPA1L1; Synonyms=E6TP1, KIAA0440;
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] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, AND
RP INTERACTION WITH HPV E6.
RX PubMed=9858596; DOI=10.1128/mcb.19.1.733;
RA Gao Q., Srinivasan S., Boyer S.N., Wazer D.E., Band V.;
RT "The E6 oncoproteins of high-risk papillomaviruses bind to a novel putative
RT GAP protein, E6TP1, and target it for degradation.";
RL Mol. Cell. Biol. 19:733-744(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9455477; DOI=10.1093/dnares/4.5.307;
RA Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VIII. 78
RT new cDNA clones from brain which code for large proteins in vitro.";
RL DNA Res. 4:307-313(1997).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [6]
RP IDENTIFICATION BY 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 [7]
RP INTERACTION WITH EPHA4.
RX PubMed=18094260; DOI=10.1523/jneurosci.2746-07.2007;
RA Richter M., Murai K.K., Bourgin C., Pak D.T., Pasquale E.B.;
RT "The EphA4 receptor regulates neuronal morphology through SPAR-mediated
RT inactivation of Rap GTPases.";
RL J. Neurosci. 27:14205-14215(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1270, 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-1585, 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 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162; SER-288; SER-1549 AND
RP SER-1585, AND IDENTIFICATION BY 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1255; SER-1270; SER-1433;
RP SER-1549; THR-1551; SER-1554; SER-1565 AND SER-1568, 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1181; SER-1270; SER-1431;
RP SER-1433; SER-1549; SER-1585 AND SER-1734, AND IDENTIFICATION BY MASS
RP 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162; SER-208; SER-255;
RP SER-288; SER-1078; SER-1087; SER-1116; SER-1149; SER-1170; SER-1255;
RP SER-1270; SER-1366; SER-1390; SER-1391; SER-1412; SER-1433; SER-1528;
RP SER-1549; THR-1551; SER-1565; SER-1568; SER-1585 AND SER-1588, 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187; SER-193; SER-255;
RP SER-1549; SER-1585 AND SER-1734, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [17]
RP VARIANT [LARGE SCALE ANALYSIS] ASP-996.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Stimulates the GTPase activity of RAP2A. Promotes
CC reorganization of the actin cytoskeleton and recruits DLG4 to F-actin.
CC Contributes to the regulation of dendritic spine morphogenesis (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with DLG4, PDLIM5, PDLIM7 and LZTS3. Interacts with
CC the actin cytoskeleton (By similarity). Interacts (via PDZ domain) with
CC EPHA4 (via PDZ motif); controls neuronal morphology through regulation
CC of the RAP1 (RAP1A or RAP1B) and RAP2 (RAP2A, RAP2B or RAP2C) GTPases.
CC Interacts with HPV E6. {ECO:0000250, ECO:0000269|PubMed:18094260,
CC ECO:0000269|PubMed:9858596}.
CC -!- INTERACTION:
CC O43166; P78352: DLG4; NbExp=2; IntAct=EBI-310678, EBI-80389;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC Postsynaptic density {ECO:0000250}. Synapse, synaptosome {ECO:0000250}.
CC Note=Associated with the actin cytoskeleton. Detected at synapses and
CC dendritic spines of cultured hippocampal neurons (By similarity).
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=E6TP1 beta;
CC IsoId=O43166-1; Sequence=Displayed;
CC Name=2; Synonyms=E6TP1 alpha;
CC IsoId=O43166-2; Sequence=VSP_010917;
CC Name=3;
CC IsoId=O43166-3; Sequence=VSP_010917, VSP_054774;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:9858596}.
CC -!- PTM: Ubiquitinated and degraded by the SCF(BTRC) following
CC phosphorylation by PLK2. {ECO:0000250}.
CC -!- PTM: Phosphorylated at Ser-1349 by CDK5, creating a docking site for
CC the POLO box domains of PLK2. Subsequently, PLK2 binds and
CC phosphorylates SIPA1L1, leading to ubiquitination and degradation by
CC the proteasome (By similarity). {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA23712.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF090989; AAD12543.1; -; mRNA.
DR EMBL; AF090990; AAD12544.1; -; mRNA.
DR EMBL; AB007900; BAA23712.2; ALT_INIT; mRNA.
DR EMBL; AK122930; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC004974; AAC83179.1; -; Genomic_DNA.
DR EMBL; AC004900; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC004968; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC005476; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC005994; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL391735; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS61490.1; -. [O43166-2]
DR CCDS; CCDS61491.1; -. [O43166-3]
DR CCDS; CCDS9807.1; -. [O43166-1]
DR RefSeq; NP_001271174.1; NM_001284245.1. [O43166-2]
DR RefSeq; NP_001271175.1; NM_001284246.1. [O43166-3]
DR RefSeq; NP_056371.1; NM_015556.2. [O43166-1]
DR RefSeq; XP_005267573.1; XM_005267516.4. [O43166-1]
DR RefSeq; XP_011534932.1; XM_011536630.1. [O43166-1]
DR RefSeq; XP_011534933.1; XM_011536631.1. [O43166-1]
DR RefSeq; XP_011534934.1; XM_011536632.1. [O43166-1]
DR RefSeq; XP_011534937.1; XM_011536635.2. [O43166-1]
DR RefSeq; XP_016876648.1; XM_017021159.1.
DR RefSeq; XP_016876649.1; XM_017021160.1.
DR RefSeq; XP_016876650.1; XM_017021161.1.
DR RefSeq; XP_016876651.1; XM_017021162.1.
DR RefSeq; XP_016876652.1; XM_017021163.1. [O43166-1]
DR RefSeq; XP_016876653.1; XM_017021164.1.
DR RefSeq; XP_016876654.1; XM_017021165.1.
DR RefSeq; XP_016876655.1; XM_017021166.1.
DR RefSeq; XP_016876656.1; XM_017021167.1.
DR RefSeq; XP_016876657.1; XM_017021168.1.
DR RefSeq; XP_016876658.1; XM_017021169.1.
DR RefSeq; XP_016876659.1; XM_017021170.1.
DR RefSeq; XP_016876660.1; XM_017021171.1.
DR RefSeq; XP_016876661.1; XM_017021172.1.
DR RefSeq; XP_016876662.1; XM_017021173.1.
DR RefSeq; XP_016876663.1; XM_017021174.1.
DR RefSeq; XP_016876664.1; XM_017021175.1.
DR RefSeq; XP_016876665.1; XM_017021176.1.
DR RefSeq; XP_016876666.1; XM_017021177.1. [O43166-1]
DR RefSeq; XP_016876667.1; XM_017021178.1. [O43166-1]
DR RefSeq; XP_016876668.1; XM_017021179.1. [O43166-1]
DR RefSeq; XP_016876669.1; XM_017021180.1. [O43166-1]
DR RefSeq; XP_016876675.1; XM_017021186.1.
DR RefSeq; XP_016876676.1; XM_017021187.1.
DR RefSeq; XP_016876677.1; XM_017021188.1.
DR RefSeq; XP_016876678.1; XM_017021189.1.
DR RefSeq; XP_016876679.1; XM_017021190.1.
DR RefSeq; XP_016876680.1; XM_017021191.1.
DR RefSeq; XP_016876681.1; XM_017021192.1.
DR RefSeq; XP_016876682.1; XM_017021193.1.
DR AlphaFoldDB; O43166; -.
DR SMR; O43166; -.
DR BioGRID; 117503; 154.
DR IntAct; O43166; 45.
DR MINT; O43166; -.
DR STRING; 9606.ENSP00000450832; -.
DR GlyConnect; 2075; 1 N-Linked glycan (1 site).
DR GlyGen; O43166; 3 sites, 2 N-linked glycans (1 site), 1 O-linked glycan (2 sites).
DR iPTMnet; O43166; -.
DR PhosphoSitePlus; O43166; -.
DR BioMuta; SIPA1L1; -.
DR EPD; O43166; -.
DR jPOST; O43166; -.
DR MassIVE; O43166; -.
DR MaxQB; O43166; -.
DR PaxDb; O43166; -.
DR PeptideAtlas; O43166; -.
DR PRIDE; O43166; -.
DR ProteomicsDB; 48783; -. [O43166-1]
DR ProteomicsDB; 48784; -. [O43166-2]
DR Antibodypedia; 132; 56 antibodies from 24 providers.
DR DNASU; 26037; -.
DR Ensembl; ENST00000358550.6; ENSP00000351352.2; ENSG00000197555.10. [O43166-3]
DR Ensembl; ENST00000381232.8; ENSP00000370630.3; ENSG00000197555.10. [O43166-2]
DR Ensembl; ENST00000555818.5; ENSP00000450832.1; ENSG00000197555.10. [O43166-1]
DR GeneID; 26037; -.
DR KEGG; hsa:26037; -.
DR MANE-Select; ENST00000381232.8; ENSP00000370630.3; NM_001386936.1; NP_001373865.1. [O43166-2]
DR UCSC; uc001xms.5; human. [O43166-1]
DR CTD; 26037; -.
DR DisGeNET; 26037; -.
DR GeneCards; SIPA1L1; -.
DR HGNC; HGNC:20284; SIPA1L1.
DR HPA; ENSG00000197555; Tissue enhanced (brain).
DR MIM; 617504; gene.
DR neXtProt; NX_O43166; -.
DR OpenTargets; ENSG00000197555; -.
DR PharmGKB; PA134940118; -.
DR VEuPathDB; HostDB:ENSG00000197555; -.
DR eggNOG; KOG3686; Eukaryota.
DR GeneTree; ENSGT00940000155944; -.
DR HOGENOM; CLU_002127_0_1_1; -.
DR InParanoid; O43166; -.
DR OMA; CHLPAMS; -.
DR OrthoDB; 28453at2759; -.
DR PhylomeDB; O43166; -.
DR TreeFam; TF318626; -.
DR PathwayCommons; O43166; -.
DR Reactome; R-HSA-6794361; Neurexins and neuroligins.
DR SignaLink; O43166; -.
DR BioGRID-ORCS; 26037; 9 hits in 1079 CRISPR screens.
DR ChiTaRS; SIPA1L1; human.
DR GeneWiki; SIPA1L1; -.
DR GenomeRNAi; 26037; -.
DR Pharos; O43166; Tdark.
DR PRO; PR:O43166; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; O43166; protein.
DR Bgee; ENSG00000197555; Expressed in nucleus accumbens and 185 other tissues.
DR ExpressionAtlas; O43166; baseline and differential.
DR Genevisible; O43166; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:HPA.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0043197; C:dendritic spine; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
DR GO; GO:0046875; F:ephrin receptor binding; IEA:Ensembl.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB.
DR GO; GO:0090630; P:activation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0048013; P:ephrin receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0050770; P:regulation of axonogenesis; ISS:UniProtKB.
DR GO; GO:0048814; P:regulation of dendrite morphogenesis; IEA:InterPro.
DR GO; GO:0061001; P:regulation of dendritic spine morphogenesis; ISS:UniProtKB.
DR GO; GO:0043087; P:regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IEA:InterPro.
DR GO; GO:0048167; P:regulation of synaptic plasticity; ISS:UniProtKB.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.40.50.11210; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR035974; Rap/Ran-GAP_sf.
DR InterPro; IPR000331; Rap/Ran_GAP_dom.
DR InterPro; IPR030770; SIPA1L1.
DR InterPro; IPR021818; SIPA1L_C.
DR PANTHER; PTHR15711:SF10; PTHR15711:SF10; 1.
DR Pfam; PF02145; Rap_GAP; 1.
DR Pfam; PF11881; SPAR_C; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF111347; SSF111347; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50085; RAPGAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW GTPase activation; Methylation; Phosphoprotein; Reference proteome;
KW Synapse; Synaptosome; Ubl conjugation.
FT CHAIN 1..1804
FT /note="Signal-induced proliferation-associated 1-like
FT protein 1"
FT /id="PRO_0000056746"
FT DOMAIN 613..830
FT /note="Rap-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00165"
FT DOMAIN 967..1045
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 1..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1067..1128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1144..1207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1268..1306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1327..1366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1379..1475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1505..1536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1735..1795
FT /evidence="ECO:0000255"
FT COMPBIAS 80..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1067..1093
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1144..1166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1182..1207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1270..1299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1327..1349
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1379..1393
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1394..1440
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1455..1475
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1505..1524
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 162
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 288
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1078
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1087
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1116
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1127
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C0T5"
FT MOD_RES 1149
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1170
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1181
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 1255
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1270
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1326
FT /note="Phosphoserine; by PLK2"
FT /evidence="ECO:0000250|UniProtKB:O35412"
FT MOD_RES 1330
FT /note="Phosphothreonine; by PLK2"
FT /evidence="ECO:0000250|UniProtKB:O35412"
FT MOD_RES 1349
FT /note="Phosphoserine; by CDK5"
FT /evidence="ECO:0000250|UniProtKB:O35412"
FT MOD_RES 1366
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1390
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1391
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1412
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1431
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 1433
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 1528
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1549
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 1551
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1554
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1565
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1568
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1585
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 1588
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1601
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8C0T5"
FT MOD_RES 1603
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C0T5"
FT MOD_RES 1645
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C0T5"
FT MOD_RES 1647
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C0T5"
FT MOD_RES 1650
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C0T5"
FT MOD_RES 1708
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C0T5"
FT MOD_RES 1711
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C0T5"
FT MOD_RES 1728
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C0T5"
FT MOD_RES 1729
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C0T5"
FT MOD_RES 1734
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1216..1236
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:9858596"
FT /id="VSP_010917"
FT VAR_SEQ 1728
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054774"
FT VARIANT 56
FT /note="P -> T (in dbSNP:rs12884638)"
FT /id="VAR_049152"
FT VARIANT 996
FT /note="E -> D (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035549"
FT CONFLICT 1387
FT /note="K -> R (in Ref. 4; AK122930)"
FT /evidence="ECO:0000305"
FT CONFLICT 1722
FT /note="A -> P (in Ref. 2; BAA23712)"
FT /evidence="ECO:0000305"
FT CONFLICT 1730
FT /note="Missing (in Ref. 2; BAA23712)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1804 AA; 200029 MW; 91AB6AB4E7F47B2F CRC64;
MTSLKRSQTE RPLATDRASV VGTDGTPKVH TDDFYMRRFR SQNGSLGSSV MAPVGPPRSE
GSHHITSTPG VPKMGVRARI ADWPPRKENI KESSRSSQEI ETSSCLDSLS SKSSPVSQGS
SVSLNSNDSA MLKSIQNTLK NKTRPSENMD SRFLMPEAYP SSPRKALRRI RQRSNSDITI
SELDVDSFDE CISPTYKTGP SLHREYGSTS SIDKQGTSGE SFFDLLKGYK DDKSDRGPTP
TKLSDFLITG GGKGSGFSLD VIDGPISQRE NLRLFKEREK PLKRRSKSET GDSSIFRKLR
NAKGEELGKS SDLEDNRSED SVRPWTCPKC FAHYDVQSIL FDLNEAIMNR HNVIKRRNTT
TGASAAAVAS LVSGPLSHSA SFSSPMGSTE DLNSKGSLSM DQGDDKSNEL VMSCPYFRNE
IGGEGERKIS LSKSNSGSFS GCESASFEST LSSHCTNAGV AVLEVPKENL VLHLDRVKRY
IVEHVDLGAY YYRKFFYQKE HWNYFGADEN LGPVAVSIRR EKPDEMKENG SPYNYRIIFR
TSELMTLRGS VLEDAIPSTA KHSTARGLPL KEVLEHVVPE LNVQCLRLAF NTPKVTEQLM
KLDEQGLNYQ QKVGIMYCKA GQSTEEEMYN NESAGPAFEE FLQLLGERVR LKGFEKYRAQ
LDTKTDSTGT HSLYTTYKDY EIMFHVSTML PYTPNNKQQL LRKRHIGNDI VTIVFQEPGA
QPFSPKNIRS HFQHVFVIVR VHNPCSDSVC YSVAVTRSRD VPSFGPPIPK GVTFPKSNVF
RDFLLAKVIN AENAAHKSEK FRAMATRTRQ EYLKDLAEKN VTNTPIDPSG KFPFISLASK
KKEKSKPYPG AELSSMGAIV WAVRAEDYNK AMELDCLLGI SNEFIVLIEQ ETKSVVFNCS
CRDVIGWTST DTSLKIFYER GECVSVGSFI NIEEIKEIVK RLQFVSKGCE SVEMTLRRNG
LGQLGFHVNY EGIVADVEPY GYAWQAGLRQ GSRLVEICKV AVATLSHEQM IDLLRTSVTV
KVVIIPPHDD CTPRRSCSET YRMPVMEYKM NEGVSYEFKF PFRNNNKWQR NASKGPHSPQ
VPSQVQSPMT SRLNAGKGDG KMPPPERAAN IPRSISSDGR PLERRLSPGS DIYVTVSSMA
LARSQCRNSP SNLSSSSDTG SVGGTYRQKS MPEGFGVSRR SPASIDRQNT QSDIGGSGKS
TPSWQRSEDS IADQMAYSYR GPQDFNSFVL EQHEYTEPTC HLPAVSKVLP AFRESPSGRL
MRQDPVVHLS PNKQGHSDSH YSSHSSSNTL SSNASSAHSD EKWYDGDRTE SELNSYNYLQ
GTSADSGIDT TSYGPSHGST ASLGAATSSP RSGPGKEKVA PLWHSSSEVI SMADRTLETE
SHGLDRKTES SLSLDIHSKS QAGSTPLTRE NSTFSINDAA SHTSTMSSRH SASPVVFTSA
RSSPKEELHP AAPSQLAPSF SSSSSSSSGP RSFYPRQGAT SKYLIGWKKP EGTINSVGFM
DTRKRHQSDG NEIAHTRLRA STRDLRASPK PTSKSTIEED LKKLIDLESP TPESQKSFKF
HALSSPQSPF PSTPTSRRAL HRTLSDESIY NSQREHFFTS RASLLDQALP NDVLFSSTYP
SLPKSLPLRR PSYTLGMKSL HGEFSASDSS LTDIQETRRQ PMPDPGLMPL PDTAADLDWS
NLVDAAKAYE VQRASFFAAS DENHRPLSAA SNSDQLEDQA LAQMKPYSSS KDSSPTLASK
VDQLEGMLKM LREDLKKEKE DKAHLQAEVQ HLREDNLRLQ EESQNASDKL KKFTEWVFNT
IDMS
