SPN90_MOUSE
ID SPN90_MOUSE Reviewed; 714 AA.
AC Q9ESJ4; Q3UYF3; Q68G72;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=NCK-interacting protein with SH3 domain;
DE AltName: Full=54 kDa VacA-interacting protein;
DE Short=VIP54;
DE AltName: Full=90 kDa N-WASP-interacting protein;
DE AltName: Full=90 kDa SH3 protein interacting with Nck;
DE AltName: Full=SH3 adapter protein SPIN90;
DE AltName: Full=WASP-interacting SH3-domain protein;
DE Short=WISH;
DE AltName: Full=Wiskott-Aldrich syndrome protein-binding protein;
DE Short=N-WASP-binding protein;
GN Name=Nckipsd; Synonyms=Spin90, Wasbp;
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 [MRNA], AND POSSIBLE FUNCTION.
RC TISSUE=Myoblast;
RX PubMed=11157975; DOI=10.1083/jcb.152.3.471;
RA Fukuoka M., Suetsugu S., Miki H., Fukami K., Endo T., Takenawa T.;
RT "A novel neural Wiskott-Aldrich syndrome protein (N-WASP) binding protein,
RT WISH, induces Arp2/3 complex activation independent of Cdc42.";
RL J. Cell Biol. 152:471-482(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 216-646.
RX PubMed=10619843; DOI=10.1093/emboj/19.1.48;
RA de Bernard M., Moschioni M., Napolitani G., Rappuoli R., Montecucco C.;
RT "The VacA toxin of Helicobacter pylori identifies a new intermediate
RT filament-interacting protein.";
RL EMBO J. 19:48-56(2000).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120; SER-260; SER-286 AND
RP SER-673, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, and Spleen;
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 -!- FUNCTION: Has an important role in stress fiber formation induced by
CC active diaphanous protein homolog 1 (DRF1) (By similarity). Induces
CC microspike formation, in vivo. In vitro, stimulates N-WASP-induced
CC ARP2/3 complex activation in the absence of CDC42. May play an
CC important role in the maintenance of sarcomere and/or in the assembly
CC of myofibrils into sarcomeres. Implicated in regulation of actin
CC polymerization and cell adhesion. {ECO:0000250}.
CC -!- SUBUNIT: Associates with the intermediate filaments, vimentin and
CC desmin (By similarity). Binds the first and third SH3 domains of NCK
CC (By similarity). Binds the proline-rich domains of N-WASP through its
CC SH3 domain. Similarly, binds diaphanous protein homolog 1 (DRF1) (By
CC similarity). Binds the SH3 domains of GRB2 through its proline-rich
CC domains. Interacts with FASLG (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Colocalizes with DRF1
CC at membrane ruffles, and with Nck at Z-disks in mature cardiac
CC myocytes. {ECO:0000250}.
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DR EMBL; AF130313; AAF36503.2; -; mRNA.
DR EMBL; AK134725; BAE22259.1; -; mRNA.
DR EMBL; CH466560; EDL21315.1; -; Genomic_DNA.
DR EMBL; BC064818; AAH64818.1; -; mRNA.
DR CCDS; CCDS23538.1; -.
DR RefSeq; NP_109654.2; NM_030729.4.
DR AlphaFoldDB; Q9ESJ4; -.
DR SMR; Q9ESJ4; -.
DR BioGRID; 219860; 2.
DR IntAct; Q9ESJ4; 2.
DR MINT; Q9ESJ4; -.
DR STRING; 10090.ENSMUSP00000035218; -.
DR iPTMnet; Q9ESJ4; -.
DR PhosphoSitePlus; Q9ESJ4; -.
DR SwissPalm; Q9ESJ4; -.
DR EPD; Q9ESJ4; -.
DR jPOST; Q9ESJ4; -.
DR MaxQB; Q9ESJ4; -.
DR PaxDb; Q9ESJ4; -.
DR PeptideAtlas; Q9ESJ4; -.
DR PRIDE; Q9ESJ4; -.
DR ProteomicsDB; 258593; -.
DR Antibodypedia; 30227; 136 antibodies from 28 providers.
DR DNASU; 80987; -.
DR Ensembl; ENSMUST00000035218; ENSMUSP00000035218; ENSMUSG00000032598.
DR GeneID; 80987; -.
DR KEGG; mmu:80987; -.
DR UCSC; uc009rqz.1; mouse.
DR CTD; 51517; -.
DR MGI; MGI:1931834; Nckipsd.
DR VEuPathDB; HostDB:ENSMUSG00000032598; -.
DR eggNOG; KOG4035; Eukaryota.
DR GeneTree; ENSGT00390000015725; -.
DR HOGENOM; CLU_012978_1_0_1; -.
DR InParanoid; Q9ESJ4; -.
DR OMA; TGFERQH; -.
DR OrthoDB; 649314at2759; -.
DR PhylomeDB; Q9ESJ4; -.
DR TreeFam; TF324522; -.
DR Reactome; R-MMU-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-MMU-5663213; RHO GTPases Activate WASPs and WAVEs.
DR BioGRID-ORCS; 80987; 4 hits in 73 CRISPR screens.
DR PRO; PR:Q9ESJ4; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9ESJ4; protein.
DR Bgee; ENSMUSG00000032598; Expressed in primary visual cortex and 69 other tissues.
DR ExpressionAtlas; Q9ESJ4; baseline and differential.
DR Genevisible; Q9ESJ4; MM.
DR GO; GO:0008180; C:COP9 signalosome; ISO:MGI.
DR GO; GO:0071933; F:Arp2/3 complex binding; IBA:GO_Central.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IMP:CACAO.
DR CDD; cd11849; SH3_SPIN90; 1.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR030125; SPIN90/Ldb17.
DR InterPro; IPR018556; SPIN90/Ldb17_LRD.
DR InterPro; IPR035514; SPIN90_SH3.
DR PANTHER; PTHR13357; PTHR13357; 1.
DR Pfam; PF09431; DUF2013; 1.
DR Pfam; PF00018; SH3_1; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Nucleus; Phosphoprotein; Reference proteome; SH3 domain; SH3-binding.
FT CHAIN 1..714
FT /note="NCK-interacting protein with SH3 domain"
FT /id="PRO_0000072131"
FT DOMAIN 1..58
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 103..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 139..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 168..185
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 107..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 174
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZQ3"
FT MOD_RES 260
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 673
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 714 AA; 78572 MW; 2111AB09799F4718 CRC64;
MYRALYAFRS AEPNAMAFAA GETFLVLERS STHWWLAARA RSGETGYVPP AYLHRLQGME
QDVLQAIDRA IEAVHNTAMR DGGKYSLEQR GVLQKLIHHR KETLSRRGTS ASSATVMTPS
TSDHHLDAAV SRQPNGVCRT GFERQHSLPS SEHLGTDGAL YQVPPQPRRA APTTPPPPVK
RRDREALVIS GSGGRTAIPS GGSSVSSGSS ASSTSMDTLY TGSSPSELGP SCSPTPPPVP
RRGAHTTVSQ PQPSPSKAPS PEPPTEEVAA ETNSTPDDLE AQDALSPETT EEKAAAETVV
PRTIGAELME LVRRNTGLSH ELCRVAIGVV VGHIQATVPA SSPIMEQVLL SLVEGKDLST
ALPSGQVCHD QQRLEVIFAD LARRKDDAQQ RSWALYEDED VIRCYLEELL HILTDADPEV
CKKMCKRSDF ESVLALVAYY QMEHRASLRL LLLKCFGAMC SLDAAIISTL VSSVLPVELA
RDMQTDTQDH QKLCYSALVL AMVFSMGEAV PYAHYEHLGT PFAQFLLSIV EDGLPMDTTE
QLPDLCMNLL LALNLHLTAP EQNVIMAALS RHTNVKIFSE KLLLLLNRGD DPVRIFRHEP
QPPHSVLKFL QDVFSSSATA AIFYHTDMMA LIDITVRQIA DLSPGDKLRM EYLSLMHAVV
RSTPYLQHRH RLSDLQATLR RILTEEEASP QCQMDRMIVQ EMYKEFPDLG EVPS
