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SI1L2_MOUSE
ID   SI1L2_MOUSE             Reviewed;        1722 AA.
AC   Q80TE4; E9QPK7; Q6PDY1;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 3.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=Signal-induced proliferation-associated 1-like protein 2;
DE            Short=SIPA1-like protein 2;
GN   Name=Sipa1l2; Synonyms=Kiaa0545;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Brain;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 538-1722 (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT   The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-380; SER-384; SER-1461;
RP   SER-1472; SER-1478; SER-1488; SER-1549; SER-1552 AND SER-1591, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Heart, Kidney, Lung, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q80TE4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80TE4-2; Sequence=VSP_016999;
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DR   EMBL; AC073946; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC058408; AAH58408.1; -; mRNA.
DR   EMBL; BC072593; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AK122501; BAC65783.1; -; mRNA.
DR   CCDS; CCDS40518.1; -. [Q80TE4-1]
DR   RefSeq; NP_001074806.1; NM_001081337.1. [Q80TE4-1]
DR   RefSeq; XP_006531087.1; XM_006531024.1. [Q80TE4-1]
DR   AlphaFoldDB; Q80TE4; -.
DR   SMR; Q80TE4; -.
DR   BioGRID; 232676; 15.
DR   IntAct; Q80TE4; 1.
DR   MINT; Q80TE4; -.
DR   STRING; 10090.ENSMUSP00000104405; -.
DR   iPTMnet; Q80TE4; -.
DR   PhosphoSitePlus; Q80TE4; -.
DR   CPTAC; non-CPTAC-3497; -.
DR   MaxQB; Q80TE4; -.
DR   PaxDb; Q80TE4; -.
DR   PRIDE; Q80TE4; -.
DR   ProteomicsDB; 261035; -. [Q80TE4-1]
DR   ProteomicsDB; 261036; -. [Q80TE4-2]
DR   Antibodypedia; 11728; 139 antibodies from 27 providers.
DR   Ensembl; ENSMUST00000108775; ENSMUSP00000104405; ENSMUSG00000001995. [Q80TE4-1]
DR   Ensembl; ENSMUST00000212987; ENSMUSP00000148536; ENSMUSG00000001995. [Q80TE4-1]
DR   GeneID; 244668; -.
DR   KEGG; mmu:244668; -.
DR   UCSC; uc009nye.1; mouse. [Q80TE4-1]
DR   CTD; 57568; -.
DR   MGI; MGI:2676970; Sipa1l2.
DR   VEuPathDB; HostDB:ENSMUSG00000001995; -.
DR   eggNOG; KOG3686; Eukaryota.
DR   GeneTree; ENSGT00940000157388; -.
DR   HOGENOM; CLU_002127_0_2_1; -.
DR   InParanoid; Q80TE4; -.
DR   OMA; GSRSMIH; -.
DR   OrthoDB; 28453at2759; -.
DR   PhylomeDB; Q80TE4; -.
DR   TreeFam; TF318626; -.
DR   BioGRID-ORCS; 244668; 1 hit in 72 CRISPR screens.
DR   ChiTaRS; Sipa1l2; mouse.
DR   PRO; PR:Q80TE4; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; Q80TE4; protein.
DR   Bgee; ENSMUSG00000001995; Expressed in pontine nuclear group and 256 other tissues.
DR   ExpressionAtlas; Q80TE4; baseline and differential.
DR   Genevisible; Q80TE4; MM.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR   GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR   GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IEA:InterPro.
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; IPR031203; SIPA1L2.
DR   InterPro; IPR021818; SIPA1L_C.
DR   PANTHER; PTHR15711:SF7; PTHR15711:SF7; 1.
DR   Pfam; PF00595; PDZ; 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; GTPase activation; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..1722
FT                   /note="Signal-induced proliferation-associated 1-like
FT                   protein 2"
FT                   /id="PRO_0000056750"
FT   DOMAIN          596..813
FT                   /note="Rap-GAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00165"
FT   DOMAIN          951..1027
FT                   /note="PDZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          44..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          362..405
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1068..1246
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1331..1360
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1652..1712
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        45..60
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        385..402
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1092..1106
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1114..1133
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1196..1214
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1215..1242
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         149
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P2F8"
FT   MOD_RES         380
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         384
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1030
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P2F8"
FT   MOD_RES         1245
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5JCS6"
FT   MOD_RES         1461
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1472
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1478
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1488
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1549
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1552
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1591
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   VAR_SEQ         1587..1605
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_016999"
FT   CONFLICT        1361
FT                   /note="G -> S (in Ref. 3; BAC65783)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1649
FT                   /note="R -> Q (in Ref. 3; BAC65783)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1722 AA;  189413 MW;  1E25D598014B1792 CRC64;
     MSDPRPSQAE KHKLGRAAAK LKDPSRTMQA DDYFARKFKA INGSMGPATL NTSSSSEGGG
     GGGGPANGTP AVPKMGVRAR VSEWPPKKDC SKDLACKTLW ESRSQSSYES VTSIIQNGQN
     DQGDRQPEEQ LDLDFVEAKY TIGDIFVHSP QRGLHPIRQR SNSDITISDI DTEDVLDQHA
     VNPNTGAALH REYGSTSSID RQGLSGENVF AMLRGYRIES YDPKVTGSFG FPDFFPCDTA
     ISPSLHAAAQ ISRGEFVRIS GLDYMDGGLL MGRDRDKPFK RRLKSESVET SLFRKLRAVK
     SEHETFKFTS DLEEGRLDRG IRPWSCQRCF AHYDVQSILF NINEAMATRA SVGKRKNITT
     GASAASQTPV PVGPAGGCES PLGSKEDLNS KENPDADEGD GKSNDLVLSC PYFRNETGGE
     GDRRIALSRA NSASFSSGES CSFESSLSSH CTNAGVSVLE VPRESQPIHR EKVKRYIIEH
     VDLGAYYYRK FFYGKEHQNY FGIDENLGPV AVSIRREKVE DPREKEGSQF NYRVAFRTSE
     LTTLRGAILE DAVPSTARHG TARGLPLKEV LEYVIPELSI QCLRQAANSP KVPEQLLKLD
     EQGLSFQHKI GILYCRAGQS TEEEMYNNET AGPAFEEFLD LLGQRVRLKG FSKYRAQLDN
     KTDSTGTHSL YTTYKDFELM FHVSTLLPYM PNNRQQLLRK RHIGNDIVTI VFQEPGALPF
     TPKNIRSHFQ HVFVIVKVHN PCTENVCYSV GVSRSKDVPP FGPPIPKGVT FPKSAVFRDF
     LLAKVINAEN AAHKSEKFRA MATRTRQEYL KDLAENFVTT ATVDTSAKFS FITLGAKKKE
     RVKPRKDAHL FSIGAIMWHV VARDFGQSAD IECLLGISNE FIMLIEKDSK NVVFNCSCRD
     VIGWTSGLVS IKAFYERGEC LLLSSVDNRS EDIREIVQRL LIVTRGCETV EMTLRRNGLG
     QLGFHVNFEG IVADVEPFGF AWKAGLRQGS RLVEICKVAV ATLTHEQMID LLRTSVTVKV
     VIIQPHEDGS PRRGCSELCR IPMVEYKLDS EGTPCEYKTP FRRNTTWHRV PTPALQPVSR
     ASPVPGTPDR LQCQPLLQQA QAAIPRSTSF DRKLPDGTRS SPSNQSSSSD PGPGGSGPWR
     PQVGYDGCPS PLLLEHQGPG SVECDGTGEQ EDLLEGGRLP ETKWHGPPSK VLSSYKERVL
     QKDGSCKESP NKLSHIGDKS CSSHSSSNTL SSNTSSNSDD KHFGSGDLMD PELLGLTYIK
     GASTDSGIDT TPCMPATILG PVHLTGSRSL MHSRAEQWAD AADVSVADDD PAKMYALHGY
     ASAISSSAAD GSMGDLSEVS SHSSGSQHSG SPSAHCSKST GSLDSSKVYI VTHGGGQQAP
     GAVTKPYHRQ GAANKYVIGW KKSEGSPPPE EPEVTECPRI YGEMDIMSTA TQHPAVVGDS
     VSETQHVLSK DDFLKLMLPD SPLVEEGRRK FSFYGNVSPR RSLYRTLSDE SVCSNRRGSS
     FASSRSSILE QALPNDILFS TTPPYHSTLP PRTHPAPSMG SLRNEFWFSD GSLSDKSKCA
     DPGLMPLPDT AAGLDWSHLV DAARAFEGLD SDEELGLLCH HASYLDQRVA SFCTLTDLQH
     GQELEGAPEL SLCVDPTSGK EFMDTPGERS PSTLTGKVNQ LELILRQLQT DLRKEKQDKA
     VLQAEVQHLR QDNMRLQEES QTATAQLRKF TEWFFSTIDK KA
 
 
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