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Signal-induced proliferation-associated 1-like protein 1 (SIPA1-like protein 1) (High-risk human papilloma viruses E6 oncoproteins targeted protein 1) (E6-targeted protein 1)

 SI1L1_HUMAN             Reviewed;        1804 AA.
O43166; J3KP19; O95321; Q9UDU4; Q9UNU4;
19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
03-OCT-2006, sequence version 4.
10-OCT-2018, entry version 163.
RecName: Full=Signal-induced proliferation-associated 1-like protein 1;
Short=SIPA1-like protein 1;
AltName: Full=High-risk human papilloma viruses E6 oncoproteins targeted protein 1;
Short=E6-targeted protein 1;
Name=SIPA1L1; Synonyms=E6TP1, KIAA0440;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, AND
INTERACTION WITH HPV E6.
PubMed=9858596; DOI=10.1128/MCB.19.1.733;
Gao Q., Srinivasan S., Boyer S.N., Wazer D.E., Band V.;
"The E6 oncoproteins of high-risk papillomaviruses bind to a novel
putative GAP protein, E6TP1, and target it for degradation.";
Mol. Cell. Biol. 19:733-744(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=9455477; DOI=10.1093/dnares/4.5.307;
Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N.,
Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. VIII.
78 new cDNA clones from brain which code for large proteins in
vitro.";
DNA Res. 4:307-313(1997).
[3]
SEQUENCE REVISION.
PubMed=12168954; DOI=10.1093/dnares/9.3.99;
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
"Construction of expression-ready cDNA clones for KIAA genes: manual
curation of 330 KIAA cDNA clones.";
DNA Res. 9:99-106(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12508121; DOI=10.1038/nature01348;
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
Quetier F., Waterston R., Hood L., Weissenbach J.;
"The DNA sequence and analysis of human chromosome 14.";
Nature 421:601-607(2003).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[7]
INTERACTION WITH EPHA4.
PubMed=18094260; DOI=10.1523/JNEUROSCI.2746-07.2007;
Richter M., Murai K.K., Bourgin C., Pak D.T., Pasquale E.B.;
"The EphA4 receptor regulates neuronal morphology through SPAR-
mediated inactivation of Rap GTPases.";
J. Neurosci. 27:14205-14215(2007).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1270, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1585, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162; SER-288; SER-1549
AND SER-1585, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1255; SER-1270;
SER-1433; SER-1549; THR-1551; SER-1554; SER-1565 AND SER-1568, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1181; SER-1270;
SER-1431; SER-1433; SER-1549; SER-1585 AND SER-1734, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162; SER-208; SER-255;
SER-288; SER-1078; SER-1087; SER-1116; SER-1149; SER-1170; SER-1255;
SER-1270; SER-1366; SER-1390; SER-1391; SER-1412; SER-1433; SER-1528;
SER-1549; THR-1551; SER-1565; SER-1568; SER-1585 AND SER-1588, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187; SER-193; SER-255;
SER-1549; SER-1585 AND SER-1734, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[17]
VARIANT [LARGE SCALE ANALYSIS] ASP-996.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Stimulates the GTPase activity of RAP2A. Promotes
reorganization of the actin cytoskeleton and recruits DLG4 to F-
actin. Contributes to the regulation of dendritic spine
morphogenesis (By similarity). {ECO:0000250}.
-!- SUBUNIT: Interacts with DLG4, PDLIM5, PDLIM7 and LZTS3. Interacts
with the actin cytoskeleton (By similarity). Interacts (via PDZ
domain) with EPHA4 (via PDZ motif); controls neuronal morphology
through regulation of the RAP1 (RAP1A or RAP1B) and RAP2 (RAP2A,
RAP2B or RAP2C) GTPases. Interacts with HPV E6. {ECO:0000250,
ECO:0000269|PubMed:18094260, ECO:0000269|PubMed:9858596}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell
junction, synapse, postsynaptic cell membrane, postsynaptic
density {ECO:0000250}. Cell junction, synapse, synaptosome
{ECO:0000250}. Note=Associated with the actin cytoskeleton.
Detected at synapses and dendritic spines of cultured hippocampal
neurons (By similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=E6TP1 beta;
IsoId=O43166-1; Sequence=Displayed;
Name=2; Synonyms=E6TP1 alpha;
IsoId=O43166-2; Sequence=VSP_010917;
Name=3;
IsoId=O43166-3; Sequence=VSP_010917, VSP_054774;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed.
{ECO:0000269|PubMed:9858596}.
-!- PTM: Ubiquitinated and degraded by the SCF(BTRC) following
phosphorylation by PLK2. {ECO:0000250}.
-!- PTM: Phosphorylated at Ser-1349 by CDK5, creating a docking site
for the POLO box domains of PLK2. Subsequently, PLK2 binds and
phosphorylates SIPA1L1, leading to ubiquitination and degradation
by the proteasome (By similarity). {ECO:0000250}.
-!- SEQUENCE CAUTION:
Sequence=BAA23712.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AF090989; AAD12543.1; -; mRNA.
EMBL; AF090990; AAD12544.1; -; mRNA.
EMBL; AB007900; BAA23712.2; ALT_INIT; mRNA.
EMBL; AK122930; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AC004974; AAC83179.1; -; Genomic_DNA.
EMBL; AC004900; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC004968; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC005476; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC005994; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL391735; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS61490.1; -. [O43166-2]
CCDS; CCDS61491.1; -. [O43166-3]
CCDS; CCDS9807.1; -. [O43166-1]
RefSeq; NP_001271174.1; NM_001284245.1. [O43166-2]
RefSeq; NP_001271175.1; NM_001284246.1. [O43166-3]
RefSeq; NP_056371.1; NM_015556.2. [O43166-1]
RefSeq; XP_005267573.1; XM_005267516.4. [O43166-1]
RefSeq; XP_011534932.1; XM_011536630.1. [O43166-1]
RefSeq; XP_011534933.1; XM_011536631.1. [O43166-1]
RefSeq; XP_011534934.1; XM_011536632.1. [O43166-1]
RefSeq; XP_011534937.1; XM_011536635.2. [O43166-1]
RefSeq; XP_016876648.1; XM_017021159.1.
RefSeq; XP_016876649.1; XM_017021160.1.
RefSeq; XP_016876650.1; XM_017021161.1.
RefSeq; XP_016876651.1; XM_017021162.1.
RefSeq; XP_016876652.1; XM_017021163.1. [O43166-1]
RefSeq; XP_016876653.1; XM_017021164.1.
RefSeq; XP_016876654.1; XM_017021165.1.
RefSeq; XP_016876655.1; XM_017021166.1.
RefSeq; XP_016876656.1; XM_017021167.1.
RefSeq; XP_016876657.1; XM_017021168.1.
RefSeq; XP_016876658.1; XM_017021169.1.
RefSeq; XP_016876659.1; XM_017021170.1.
RefSeq; XP_016876660.1; XM_017021171.1.
RefSeq; XP_016876661.1; XM_017021172.1.
RefSeq; XP_016876662.1; XM_017021173.1.
RefSeq; XP_016876663.1; XM_017021174.1.
RefSeq; XP_016876664.1; XM_017021175.1.
RefSeq; XP_016876665.1; XM_017021176.1.
RefSeq; XP_016876666.1; XM_017021177.1. [O43166-1]
RefSeq; XP_016876667.1; XM_017021178.1. [O43166-1]
RefSeq; XP_016876668.1; XM_017021179.1. [O43166-1]
RefSeq; XP_016876669.1; XM_017021180.1. [O43166-1]
RefSeq; XP_016876675.1; XM_017021186.1.
RefSeq; XP_016876676.1; XM_017021187.1.
RefSeq; XP_016876677.1; XM_017021188.1.
RefSeq; XP_016876678.1; XM_017021189.1.
RefSeq; XP_016876679.1; XM_017021190.1.
RefSeq; XP_016876680.1; XM_017021191.1.
RefSeq; XP_016876681.1; XM_017021192.1.
RefSeq; XP_016876682.1; XM_017021193.1.
UniGene; Hs.654657; -.
ProteinModelPortal; O43166; -.
SMR; O43166; -.
BioGrid; 117503; 100.
IntAct; O43166; 22.
MINT; O43166; -.
STRING; 9606.ENSP00000450832; -.
iPTMnet; O43166; -.
PhosphoSitePlus; O43166; -.
BioMuta; SIPA1L1; -.
EPD; O43166; -.
MaxQB; O43166; -.
PaxDb; O43166; -.
PeptideAtlas; O43166; -.
PRIDE; O43166; -.
ProteomicsDB; 48783; -.
ProteomicsDB; 48784; -. [O43166-2]
Ensembl; ENST00000358550; ENSP00000351352; ENSG00000197555. [O43166-3]
Ensembl; ENST00000381232; ENSP00000370630; ENSG00000197555. [O43166-2]
Ensembl; ENST00000555818; ENSP00000450832; ENSG00000197555. [O43166-1]
GeneID; 26037; -.
KEGG; hsa:26037; -.
UCSC; uc001xms.5; human. [O43166-1]
CTD; 26037; -.
DisGeNET; 26037; -.
EuPathDB; HostDB:ENSG00000197555.9; -.
GeneCards; SIPA1L1; -.
HGNC; HGNC:20284; SIPA1L1.
HPA; HPA002875; -.
MIM; 617504; gene.
neXtProt; NX_O43166; -.
OpenTargets; ENSG00000197555; -.
PharmGKB; PA134940118; -.
eggNOG; KOG3686; Eukaryota.
eggNOG; ENOG410XTIX; LUCA.
GeneTree; ENSGT00760000119182; -.
HOGENOM; HOG000154319; -.
HOVERGEN; HBG056135; -.
InParanoid; O43166; -.
KO; K17701; -.
OMA; PTCHLPA; -.
OrthoDB; EOG091G016P; -.
PhylomeDB; O43166; -.
TreeFam; TF318626; -.
Reactome; R-HSA-6794361; Neurexins and neuroligins.
ChiTaRS; SIPA1L1; human.
GeneWiki; SIPA1L1; -.
GenomeRNAi; 26037; -.
PMAP-CutDB; O43166; -.
PRO; PR:O43166; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000197555; Expressed in 228 organ(s), highest expression level in caudate nucleus.
CleanEx; HS_SIPA1L1; -.
ExpressionAtlas; O43166; baseline and differential.
Genevisible; O43166; HS.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0043197; C:dendritic spine; ISS:UniProtKB.
GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
GO; GO:0046875; F:ephrin receptor binding; IEA:Ensembl.
GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
GO; GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB.
GO; GO:0090630; P:activation of GTPase activity; ISS:UniProtKB.
GO; GO:0048013; P:ephrin receptor signaling pathway; ISS:UniProtKB.
GO; GO:0050770; P:regulation of axonogenesis; ISS:UniProtKB.
GO; GO:0061001; P:regulation of dendritic spine morphogenesis; ISS:UniProtKB.
GO; GO:0043087; P:regulation of GTPase activity; ISS:UniProtKB.
GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IEA:InterPro.
GO; GO:0048167; P:regulation of synaptic plasticity; ISS:UniProtKB.
Gene3D; 3.40.50.11210; -; 1.
InterPro; IPR001478; PDZ.
InterPro; IPR036034; PDZ_sf.
InterPro; IPR035974; Rap/Ran-GAP_sf.
InterPro; IPR000331; Rap_GAP_dom.
InterPro; IPR030770; SIPA1L1.
InterPro; IPR021818; SIPA1L_C.
PANTHER; PTHR15711:SF10; PTHR15711:SF10; 1.
Pfam; PF02145; Rap_GAP; 1.
Pfam; PF11881; SPAR_C; 1.
SMART; SM00228; PDZ; 1.
SUPFAM; SSF111347; SSF111347; 1.
SUPFAM; SSF50156; SSF50156; 1.
PROSITE; PS50106; PDZ; 1.
PROSITE; PS50085; RAPGAP; 1.
1: Evidence at protein level;
Alternative splicing; Cell junction; Cell membrane; Coiled coil;
Complete proteome; Cytoplasm; Cytoskeleton; GTPase activation;
Membrane; Methylation; Phosphoprotein; Polymorphism;
Postsynaptic cell membrane; Reference proteome; Synapse; Synaptosome;
Ubl conjugation.
CHAIN 1 1804 Signal-induced proliferation-associated
1-like protein 1.
/FTId=PRO_0000056746.
DOMAIN 613 830 Rap-GAP. {ECO:0000255|PROSITE-
ProRule:PRU00165}.
DOMAIN 967 1045 PDZ. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
COILED 1735 1795 {ECO:0000255}.
COMPBIAS 107 143 Ser-rich.
COMPBIAS 1154 1157 Poly-Ser.
COMPBIAS 1291 1486 Ser-rich.
MOD_RES 162 162 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 187 187 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 193 193 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 208 208 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 255 255 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 288 288 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 1078 1078 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1087 1087 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1116 1116 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1127 1127 Phosphoserine.
{ECO:0000250|UniProtKB:Q8C0T5}.
MOD_RES 1149 1149 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1170 1170 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1181 1181 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 1255 1255 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1270 1270 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1326 1326 Phosphoserine; by PLK2.
{ECO:0000250|UniProtKB:O35412}.
MOD_RES 1330 1330 Phosphothreonine; by PLK2.
{ECO:0000250|UniProtKB:O35412}.
MOD_RES 1349 1349 Phosphoserine; by CDK5.
{ECO:0000250|UniProtKB:O35412}.
MOD_RES 1366 1366 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1390 1390 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1391 1391 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1412 1412 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1431 1431 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 1433 1433 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1528 1528 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1549 1549 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1551 1551 Phosphothreonine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1554 1554 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 1565 1565 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1568 1568 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1585 1585 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1588 1588 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1601 1601 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q8C0T5}.
MOD_RES 1603 1603 Phosphoserine.
{ECO:0000250|UniProtKB:Q8C0T5}.
MOD_RES 1645 1645 Phosphoserine.
{ECO:0000250|UniProtKB:Q8C0T5}.
MOD_RES 1647 1647 Phosphoserine.
{ECO:0000250|UniProtKB:Q8C0T5}.
MOD_RES 1650 1650 Phosphoserine.
{ECO:0000250|UniProtKB:Q8C0T5}.
MOD_RES 1708 1708 Phosphoserine.
{ECO:0000250|UniProtKB:Q8C0T5}.
MOD_RES 1711 1711 Phosphoserine.
{ECO:0000250|UniProtKB:Q8C0T5}.
MOD_RES 1728 1728 Phosphoserine.
{ECO:0000250|UniProtKB:Q8C0T5}.
MOD_RES 1729 1729 Phosphoserine.
{ECO:0000250|UniProtKB:Q8C0T5}.
MOD_RES 1734 1734 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:24275569}.
VAR_SEQ 1216 1236 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:9858596}.
/FTId=VSP_010917.
VAR_SEQ 1728 1728 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_054774.
VARIANT 56 56 P -> T (in dbSNP:rs12884638).
/FTId=VAR_049152.
VARIANT 996 996 E -> D (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035549.
CONFLICT 1387 1387 K -> R (in Ref. 4; AK122930).
{ECO:0000305}.
CONFLICT 1722 1722 A -> P (in Ref. 2; BAA23712).
{ECO:0000305}.
CONFLICT 1730 1730 Missing (in Ref. 2; BAA23712).
{ECO:0000305}.
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


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