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Protein

NCK-interacting protein with SH3 domain

Gene

Nckipsd

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Has an important role in stress fiber formation induced by active diaphanous protein homolog 1 (DRF1) (By similarity). Induces microspike formation, in vivo. In vitro, stimulates N-WASP-induced ARP2/3 complex activation in the absence of CDC42. May play an important role in the maintenance of sarcomere and/or in the assembly of myofibrils into sarcomeres. Implicated in regulation of actin polymerization and cell adhesion.By similarity

GO - Biological processi

  • positive regulation of neuron projection development Source: CACAO
Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-MMU-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-MMU-5663213. RHO GTPases Activate WASPs and WAVEs.

Names & Taxonomyi

Protein namesi
Recommended name:
NCK-interacting protein with SH3 domain
Alternative name(s):
54 kDa VacA-interacting protein
Short name:
VIP54
90 kDa N-WASP-interacting protein
90 kDa SH3 protein interacting with Nck
SH3 adapter protein SPIN90
WASP-interacting SH3-domain protein
Short name:
WISH
Wiskott-Aldrich syndrome protein-binding protein
Short name:
N-WASP-binding protein
Gene namesi
Name:Nckipsd
Synonyms:Spin90, Wasbp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1931834. Nckipsd.

Subcellular locationi

  • Nucleus By similarity

  • Note: Colocalizes with DRF1 at membrane ruffles, and with Nck at Z-disks in mature cardiac myocytes.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 714714NCK-interacting protein with SH3 domainPRO_0000072131Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei120 – 1201PhosphoserineCombined sources
Modified residuei174 – 1741PhosphothreonineBy similarity
Modified residuei260 – 2601PhosphoserineCombined sources
Modified residuei286 – 2861PhosphoserineCombined sources
Modified residuei673 – 6731PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9ESJ4.
MaxQBiQ9ESJ4.
PaxDbiQ9ESJ4.
PeptideAtlasiQ9ESJ4.
PRIDEiQ9ESJ4.

PTM databases

iPTMnetiQ9ESJ4.
PhosphoSiteiQ9ESJ4.

Expressioni

Gene expression databases

BgeeiQ9ESJ4.
CleanExiMM_NCKIPSD.
ExpressionAtlasiQ9ESJ4. baseline and differential.
GenevisibleiQ9ESJ4. MM.

Interactioni

Subunit structurei

Associates with the intermediate filaments, vimentin and desmin (By similarity). Binds the first and third SH3 domains of NCK (By similarity). Binds the proline-rich domains of N-WASP through its SH3 domain. Similarly, binds diaphanous protein homolog 1 (DRF1) (By similarity). Binds the SH3 domains of GRB2 through its proline-rich domains. Interacts with FASLG (By similarity).By similarity

Protein-protein interaction databases

BioGridi219860. 1 interaction.
IntActiQ9ESJ4. 3 interactions.
MINTiMINT-157148.
STRINGi10090.ENSMUSP00000035218.

Structurei

3D structure databases

ProteinModelPortaliQ9ESJ4.
SMRiQ9ESJ4. Positions 1-53.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 5858SH3PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi168 – 18518Nuclear localization signalSequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi200 – 23334Ser-richAdd
BLAST
Compositional biasi225 – 26440Pro-richAdd
BLAST
Compositional biasi434 – 47946Leu-richAdd
BLAST
Compositional biasi526 – 59368Leu-richAdd
BLAST

Sequence similaritiesi

Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

SH3 domain, SH3-binding

Phylogenomic databases

eggNOGiKOG4035. Eukaryota.
ENOG410Y8WT. LUCA.
GeneTreeiENSGT00390000015725.
HOGENOMiHOG000008184.
HOVERGENiHBG061630.
InParanoidiQ9ESJ4.
OMAiERSSAHW.
OrthoDBiEOG7966G7.
PhylomeDBiQ9ESJ4.
TreeFamiTF324522.

Family and domain databases

InterProiIPR018556. DUF2013.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF09431. DUF2013. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
SMARTiSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS50002. SH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9ESJ4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYRALYAFRS AEPNAMAFAA GETFLVLERS STHWWLAARA RSGETGYVPP
60 70 80 90 100
AYLHRLQGME QDVLQAIDRA IEAVHNTAMR DGGKYSLEQR GVLQKLIHHR
110 120 130 140 150
KETLSRRGTS ASSATVMTPS TSDHHLDAAV SRQPNGVCRT GFERQHSLPS
160 170 180 190 200
SEHLGTDGAL YQVPPQPRRA APTTPPPPVK RRDREALVIS GSGGRTAIPS
210 220 230 240 250
GGSSVSSGSS ASSTSMDTLY TGSSPSELGP SCSPTPPPVP RRGAHTTVSQ
260 270 280 290 300
PQPSPSKAPS PEPPTEEVAA ETNSTPDDLE AQDALSPETT EEKAAAETVV
310 320 330 340 350
PRTIGAELME LVRRNTGLSH ELCRVAIGVV VGHIQATVPA SSPIMEQVLL
360 370 380 390 400
SLVEGKDLST ALPSGQVCHD QQRLEVIFAD LARRKDDAQQ RSWALYEDED
410 420 430 440 450
VIRCYLEELL HILTDADPEV CKKMCKRSDF ESVLALVAYY QMEHRASLRL
460 470 480 490 500
LLLKCFGAMC SLDAAIISTL VSSVLPVELA RDMQTDTQDH QKLCYSALVL
510 520 530 540 550
AMVFSMGEAV PYAHYEHLGT PFAQFLLSIV EDGLPMDTTE QLPDLCMNLL
560 570 580 590 600
LALNLHLTAP EQNVIMAALS RHTNVKIFSE KLLLLLNRGD DPVRIFRHEP
610 620 630 640 650
QPPHSVLKFL QDVFSSSATA AIFYHTDMMA LIDITVRQIA DLSPGDKLRM
660 670 680 690 700
EYLSLMHAVV RSTPYLQHRH RLSDLQATLR RILTEEEASP QCQMDRMIVQ
710
EMYKEFPDLG EVPS
Length:714
Mass (Da):78,572
Last modified:January 4, 2005 - v2
Checksum:i2111AB09799F4718
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF130313 mRNA. Translation: AAF36503.2.
AK134725 mRNA. Translation: BAE22259.1.
CH466560 Genomic DNA. Translation: EDL21315.1.
BC064818 mRNA. Translation: AAH64818.1.
CCDSiCCDS23538.1.
RefSeqiNP_109654.2. NM_030729.4.
UniGeneiMm.192416.

Genome annotation databases

EnsembliENSMUST00000035218; ENSMUSP00000035218; ENSMUSG00000032598.
ENSMUST00000202637; ENSMUSP00000144069; ENSMUSG00000107055.
GeneIDi80987.
KEGGimmu:80987.
UCSCiuc009rqz.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF130313 mRNA. Translation: AAF36503.2.
AK134725 mRNA. Translation: BAE22259.1.
CH466560 Genomic DNA. Translation: EDL21315.1.
BC064818 mRNA. Translation: AAH64818.1.
CCDSiCCDS23538.1.
RefSeqiNP_109654.2. NM_030729.4.
UniGeneiMm.192416.

3D structure databases

ProteinModelPortaliQ9ESJ4.
SMRiQ9ESJ4. Positions 1-53.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi219860. 1 interaction.
IntActiQ9ESJ4. 3 interactions.
MINTiMINT-157148.
STRINGi10090.ENSMUSP00000035218.

PTM databases

iPTMnetiQ9ESJ4.
PhosphoSiteiQ9ESJ4.

Proteomic databases

EPDiQ9ESJ4.
MaxQBiQ9ESJ4.
PaxDbiQ9ESJ4.
PeptideAtlasiQ9ESJ4.
PRIDEiQ9ESJ4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000035218; ENSMUSP00000035218; ENSMUSG00000032598.
ENSMUST00000202637; ENSMUSP00000144069; ENSMUSG00000107055.
GeneIDi80987.
KEGGimmu:80987.
UCSCiuc009rqz.1. mouse.

Organism-specific databases

CTDi51517.
MGIiMGI:1931834. Nckipsd.

Phylogenomic databases

eggNOGiKOG4035. Eukaryota.
ENOG410Y8WT. LUCA.
GeneTreeiENSGT00390000015725.
HOGENOMiHOG000008184.
HOVERGENiHBG061630.
InParanoidiQ9ESJ4.
OMAiERSSAHW.
OrthoDBiEOG7966G7.
PhylomeDBiQ9ESJ4.
TreeFamiTF324522.

Enzyme and pathway databases

ReactomeiR-MMU-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-MMU-5663213. RHO GTPases Activate WASPs and WAVEs.

Miscellaneous databases

PROiQ9ESJ4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9ESJ4.
CleanExiMM_NCKIPSD.
ExpressionAtlasiQ9ESJ4. baseline and differential.
GenevisibleiQ9ESJ4. MM.

Family and domain databases

InterProiIPR018556. DUF2013.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF09431. DUF2013. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
SMARTiSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS50002. SH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A novel neural Wiskott-Aldrich syndrome protein (N-WASP) binding protein, WISH, induces Arp2/3 complex activation independent of Cdc42."
    Fukuoka M., Suetsugu S., Miki H., Fukami K., Endo T., Takenawa T.
    J. Cell Biol. 152:471-482(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], POSSIBLE FUNCTION.
    Tissue: Myoblast.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Medulla oblongata.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "The VacA toxin of Helicobacter pylori identifies a new intermediate filament-interacting protein."
    de Bernard M., Moschioni M., Napolitani G., Rappuoli R., Montecucco C.
    EMBO J. 19:48-56(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 216-646.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120; SER-260; SER-286 AND SER-673, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Kidney and Spleen.

Entry informationi

Entry nameiSPN90_MOUSE
AccessioniPrimary (citable) accession number: Q9ESJ4
Secondary accession number(s): Q3UYF3, Q68G72
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 5, 2001
Last sequence update: January 4, 2005
Last modified: July 6, 2016
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.