SPN90_HUMAN
ID SPN90_HUMAN Reviewed; 722 AA.
AC Q9NZQ3; B4DFL5; Q6GU34; Q6SPF3; Q8TC10; Q9UGM8;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=NCK-interacting protein with SH3 domain;
DE AltName: Full=54 kDa VacA-interacting protein;
DE AltName: Full=54 kDa vimentin-interacting protein;
DE Short=VIP54;
DE AltName: Full=90 kDa SH3 protein interacting with Nck;
DE AltName: Full=AF3p21;
DE AltName: Full=Dia-interacting protein 1;
DE Short=DIP-1;
DE AltName: Full=Diaphanous protein-interacting protein;
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-interacting protein;
GN Name=NCKIPSD; Synonyms=AF3P21, SPIN90;
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] (ISOFORM 1), AND CHROMOSOMAL TRANSLOCATION WITH
RP KMT2A/MLL1.
RC TISSUE=Leukemia;
RX PubMed=10648423;
RA Sano K., Hayakawa A., Piao J.-H., Kosaka Y., Nakamura H.;
RT "Novel SH3 protein encoded by the AF3p21 gene is fused to the mixed lineage
RT leukemia protein in a therapy-related leukemia with t(3;11)(p21;q23).";
RL Blood 95:1066-1068(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH VACA, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Cervix carcinoma;
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RC TISSUE=Cervix carcinoma;
RX PubMed=11241789; DOI=10.1002/gcc.1102;
RA Hayakawa A., Matsuda Y., Daibata M., Nakamura H., Sano K.;
RT "Genomic organization, tissue expression and cellular localization of
RT AF3p21, a fusion partner of MLL in therapy-related leukemia.";
RL Genes Chromosomes Cancer 30:364-374(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Heart;
RX PubMed=11278500; DOI=10.1074/jbc.m009411200;
RA Lim C.S., Park E.S., Kim D.J., Song Y.H., Eom S.H., Chun J.-S., Kim J.H.,
RA Kim J.-K., Park D., Song W.K.;
RT "SPIN90 (SH3 protein interacting with Nck, 90 kDa), an adapter protein that
RT is developmentally regulated during cardiac myocyte differentiation.";
RL J. Biol. Chem. 276:12871-12878(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORMS 1 AND
RP 2).
RC TISSUE=Brain, and Placenta;
RX PubMed=11509578; DOI=10.1074/jbc.m107026200;
RA Satoh S., Tominaga T.;
RT "mDia-interacting protein acts downstream of rho-mDia and modifies src
RT activation and stress fiber formation.";
RL J. Biol. Chem. 276:39290-39294(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND INTERACTION WITH FHOD1.
RC TISSUE=Bone marrow;
RX PubMed=15095401; DOI=10.1002/jcb.20031;
RA Westendorf J.J., Koka S.;
RT "Identification of FHOD1-binding proteins and mechanisms of FHOD1-regulated
RT actin dynamics.";
RL J. Cell. Biochem. 92:29-41(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT SER-660.
RC TISSUE=Placenta, and Skin;
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 448-722 (ISOFORM 5).
RC TISSUE=Brain cortex;
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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [11]
RP INTERACTION WITH FASLG.
RX PubMed=19807924; DOI=10.1186/1471-2172-10-53;
RA Voss M., Lettau M., Janssen O.;
RT "Identification of SH3 domain interaction partners of human FasL (CD178) by
RT phage display screening.";
RL BMC Immunol. 10:53-53(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP FUNCTION IN ANGIOGENESIS, AND INTERACTION WITH TMIGD2.
RX PubMed=22419821; DOI=10.1091/mbc.e11-11-0934;
RA Rahimi N., Rezazadeh K., Mahoney J.E., Hartsough E., Meyer R.D.;
RT "Identification of IGPR-1 as a novel adhesion molecule involved in
RT angiogenesis.";
RL Mol. Biol. Cell 23:1646-1656(2012).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-181, AND IDENTIFICATION BY
RP 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 [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [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).
CC -!- FUNCTION: Has an important role in stress fiber formation induced by
CC active diaphanous protein homolog 1 (DRF1). Induces microspike
CC formation, in vivo (By similarity). In vitro, stimulates N-WASP-induced
CC ARP2/3 complex activation in the absence of CDC42 (By similarity). May
CC play an important role in the maintenance of sarcomeres and/or in the
CC assembly of myofibrils into sarcomeres. Implicated in regulation of
CC actin polymerization and cell adhesion. Plays a role in angiogenesis.
CC {ECO:0000250, ECO:0000269|PubMed:22419821}.
CC -!- SUBUNIT: Associates with the intermediate filaments, vimentin and
CC desmin. Binds the first and third SH3 domains of NCK. Binds the
CC proline-rich domains of N-WASP through its SH3 domain (By similarity).
CC Similarly, binds diaphanous protein homolog 1 (DRF1). Binds the SH3
CC domains of GRB2 through its proline-rich domains. Interacts with
CC Helicobacter pylori toxin vacA. Isoform 4 interacts with FHOD1.
CC Interacts with FASLG. Interacts with TMIGD2. {ECO:0000250,
CC ECO:0000269|PubMed:10619843, ECO:0000269|PubMed:15095401,
CC ECO:0000269|PubMed:19807924, ECO:0000269|PubMed:22419821}.
CC -!- INTERACTION:
CC Q9NZQ3; Q9UQB8: BAIAP2; NbExp=2; IntAct=EBI-745080, EBI-525456;
CC Q9NZQ3; P06241: FYN; NbExp=2; IntAct=EBI-745080, EBI-515315;
CC Q9NZQ3; O00233: PSMD9; NbExp=4; IntAct=EBI-745080, EBI-750973;
CC Q9NZQ3; O60504: SORBS3; NbExp=3; IntAct=EBI-745080, EBI-741237;
CC Q9NZQ3; Q60437: BAIAP2; Xeno; NbExp=3; IntAct=EBI-745080, EBI-7010040;
CC Q9NZQ3; Q9Z0W5: Pacsin1; Xeno; NbExp=6; IntAct=EBI-745080, EBI-1550185;
CC Q9NZQ3; Q9QY17: Pacsin2; Xeno; NbExp=2; IntAct=EBI-745080, EBI-491201;
CC Q9NZQ3-3; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-10963850, EBI-11096309;
CC Q9NZQ3-3; Q96FN4: CPNE2; NbExp=3; IntAct=EBI-10963850, EBI-7097057;
CC Q9NZQ3-3; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-10963850, EBI-744099;
CC Q9NZQ3-3; O60861-1: GAS7; NbExp=5; IntAct=EBI-10963850, EBI-11745923;
CC Q9NZQ3-3; P56470: LGALS4; NbExp=3; IntAct=EBI-10963850, EBI-720805;
CC Q9NZQ3-3; Q71SY5: MED25; NbExp=3; IntAct=EBI-10963850, EBI-394558;
CC Q9NZQ3-3; Q8IVT4: MGC50722; NbExp=3; IntAct=EBI-10963850, EBI-14086479;
CC Q9NZQ3-3; O43639: NCK2; NbExp=3; IntAct=EBI-10963850, EBI-713635;
CC Q9NZQ3-3; Q13526: PIN1; NbExp=3; IntAct=EBI-10963850, EBI-714158;
CC Q9NZQ3-3; Q99959-2: PKP2; NbExp=3; IntAct=EBI-10963850, EBI-10987518;
CC Q9NZQ3-3; Q9BUI4: POLR3C; NbExp=3; IntAct=EBI-10963850, EBI-5452779;
CC Q9NZQ3-3; Q8WWY3: PRPF31; NbExp=3; IntAct=EBI-10963850, EBI-1567797;
CC Q9NZQ3-3; Q9UIG4: PSORS1C2; NbExp=3; IntAct=EBI-10963850, EBI-11974061;
CC Q9NZQ3-3; Q9NW64: RBM22; NbExp=5; IntAct=EBI-10963850, EBI-2602260;
CC Q9NZQ3-3; Q96R05: RBP7; NbExp=3; IntAct=EBI-10963850, EBI-2856326;
CC Q9NZQ3-3; P09234: SNRPC; NbExp=3; IntAct=EBI-10963850, EBI-766589;
CC Q9NZQ3-3; Q99469: STAC; NbExp=3; IntAct=EBI-10963850, EBI-2652799;
CC Q9NZQ3-3; Q7Z6J9: TSEN54; NbExp=3; IntAct=EBI-10963850, EBI-2559824;
CC Q9NZQ3-3; Q14119: VEZF1; NbExp=3; IntAct=EBI-10963850, EBI-11980193;
CC Q9NZQ3-3; Q9UFB7: ZBTB47; NbExp=3; IntAct=EBI-10963850, EBI-7781767;
CC Q9NZQ3-3; Q53FD0-2: ZC2HC1C; NbExp=3; IntAct=EBI-10963850, EBI-14104088;
CC -!- SUBCELLULAR LOCATION: Nucleus. Note=Colocalizes with DRF1 at membrane
CC ruffles, and with Nck at Z-disks in mature cardiac myocytes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q9NZQ3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NZQ3-2; Sequence=VSP_003971;
CC Name=3;
CC IsoId=Q9NZQ3-3; Sequence=VSP_039422;
CC Name=4; Synonyms=WISH-B;
CC IsoId=Q9NZQ3-4; Sequence=VSP_039422, VSP_039425, VSP_039426;
CC Name=5;
CC IsoId=Q9NZQ3-5; Sequence=VSP_039423, VSP_039424;
CC -!- TISSUE SPECIFICITY: Highest expression in heart, brain, skeletal
CC muscle, kidney and liver. Lower levels in placenta, lung, small
CC intestine and leukocytes. Weak expression in colon, thymus and spleen.
CC {ECO:0000269|PubMed:10619843}.
CC -!- DISEASE: Note=A chromosomal aberration involving NCKIPSD/AF3p21 is
CC found in therapy-related leukemia. Translocation t(3;11)(p21;q23) with
CC KMT2A/MLL1. {ECO:0000269|PubMed:10648423}.
CC -!- MISCELLANEOUS: [Isoform 5]: Found in a brain affected by Alzheimer
CC disease. May be due to intron retention. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAG57476.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/AF3p21ID228.html";
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DR EMBL; AF178432; AAF35985.1; -; mRNA.
DR EMBL; AJ242655; CAB65089.2; -; mRNA.
DR EMBL; AF303581; AAK09094.1; -; mRNA.
DR EMBL; AB069981; BAB63204.1; -; Genomic_DNA.
DR EMBL; AB069982; BAB63205.1; -; Genomic_DNA.
DR EMBL; AY453794; AAR83735.1; -; mRNA.
DR EMBL; AC141002; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC016052; AAH16052.1; -; mRNA.
DR EMBL; BC026280; AAH26280.1; -; mRNA.
DR EMBL; AK294151; BAG57476.1; ALT_INIT; mRNA.
DR CCDS; CCDS2776.1; -. [Q9NZQ3-1]
DR CCDS; CCDS46827.1; -. [Q9NZQ3-3]
DR RefSeq; NP_057537.1; NM_016453.3. [Q9NZQ3-1]
DR RefSeq; NP_909119.1; NM_184231.2. [Q9NZQ3-3]
DR PDB; 6DEC; X-ray; 4.60 A; M/P=269-722.
DR PDB; 6DED; X-ray; 2.20 A; A/B=350-722.
DR PDB; 6DEE; X-ray; 3.04 A; A=306-722.
DR PDBsum; 6DEC; -.
DR PDBsum; 6DED; -.
DR PDBsum; 6DEE; -.
DR AlphaFoldDB; Q9NZQ3; -.
DR SMR; Q9NZQ3; -.
DR BioGRID; 119583; 93.
DR IntAct; Q9NZQ3; 95.
DR MINT; Q9NZQ3; -.
DR STRING; 9606.ENSP00000294129; -.
DR GlyGen; Q9NZQ3; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NZQ3; -.
DR MetOSite; Q9NZQ3; -.
DR PhosphoSitePlus; Q9NZQ3; -.
DR BioMuta; NCKIPSD; -.
DR DMDM; 17433253; -.
DR EPD; Q9NZQ3; -.
DR jPOST; Q9NZQ3; -.
DR MassIVE; Q9NZQ3; -.
DR MaxQB; Q9NZQ3; -.
DR PaxDb; Q9NZQ3; -.
DR PeptideAtlas; Q9NZQ3; -.
DR PRIDE; Q9NZQ3; -.
DR ProteomicsDB; 83478; -. [Q9NZQ3-1]
DR ProteomicsDB; 83479; -. [Q9NZQ3-2]
DR ProteomicsDB; 83480; -. [Q9NZQ3-3]
DR ProteomicsDB; 83481; -. [Q9NZQ3-4]
DR ProteomicsDB; 83482; -. [Q9NZQ3-5]
DR Antibodypedia; 30227; 136 antibodies from 28 providers.
DR DNASU; 51517; -.
DR Ensembl; ENST00000294129.7; ENSP00000294129.2; ENSG00000213672.8. [Q9NZQ3-1]
DR Ensembl; ENST00000416649.6; ENSP00000389059.2; ENSG00000213672.8. [Q9NZQ3-3]
DR GeneID; 51517; -.
DR KEGG; hsa:51517; -.
DR MANE-Select; ENST00000294129.7; ENSP00000294129.2; NM_016453.4; NP_057537.1.
DR UCSC; uc003cum.5; human. [Q9NZQ3-1]
DR CTD; 51517; -.
DR DisGeNET; 51517; -.
DR GeneCards; NCKIPSD; -.
DR HGNC; HGNC:15486; NCKIPSD.
DR HPA; ENSG00000213672; Tissue enhanced (parathyroid).
DR MIM; 606671; gene.
DR neXtProt; NX_Q9NZQ3; -.
DR OpenTargets; ENSG00000213672; -.
DR PharmGKB; PA134872724; -.
DR VEuPathDB; HostDB:ENSG00000213672; -.
DR eggNOG; KOG4035; Eukaryota.
DR GeneTree; ENSGT00390000015725; -.
DR HOGENOM; CLU_012978_1_0_1; -.
DR InParanoid; Q9NZQ3; -.
DR OMA; HSYSDKG; -.
DR OrthoDB; 649314at2759; -.
DR PhylomeDB; Q9NZQ3; -.
DR TreeFam; TF324522; -.
DR PathwayCommons; Q9NZQ3; -.
DR Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-HSA-5663213; RHO GTPases Activate WASPs and WAVEs.
DR Reactome; R-HSA-9664422; FCGR3A-mediated phagocytosis.
DR SignaLink; Q9NZQ3; -.
DR SIGNOR; Q9NZQ3; -.
DR BioGRID-ORCS; 51517; 11 hits in 1081 CRISPR screens.
DR ChiTaRS; NCKIPSD; human.
DR GeneWiki; NCKIPSD; -.
DR GenomeRNAi; 51517; -.
DR Pharos; Q9NZQ3; Tbio.
DR PRO; PR:Q9NZQ3; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9NZQ3; protein.
DR Bgee; ENSG00000213672; Expressed in right frontal lobe and 181 other tissues.
DR ExpressionAtlas; Q9NZQ3; baseline and differential.
DR Genevisible; Q9NZQ3; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005882; C:intermediate filament; NAS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0071933; F:Arp2/3 complex binding; IBA:GO_Central.
DR GO; GO:0008092; F:cytoskeletal protein binding; NAS:UniProtKB.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0007010; P:cytoskeleton organization; NAS:UniProtKB.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IEA:Ensembl.
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 3D-structure; Alternative splicing; Chromosomal rearrangement; Nucleus;
KW Phosphoprotein; Proto-oncogene; Reference proteome; SH3 domain;
KW SH3-binding.
FT CHAIN 1..722
FT /note="NCK-interacting protein with SH3 domain"
FT /id="PRO_0000072130"
FT DOMAIN 1..58
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 101..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 149..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 175..192
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 107..122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..184
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 57..58
FT /note="Breakpoint for translocation to form KMT2A/MLL1-
FT AF3P21 oncogene"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ESJ4"
FT MOD_RES 181
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 294
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ESJ4"
FT VAR_SEQ 165..171
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15095401,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_039422"
FT VAR_SEQ 567..596
FT /note="AADQNVIMAALSKHANVKIFSEKLLLLLNR -> GGVGPGWAVAEHMVALRL
FT STLSIPMSFLSC (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_039423"
FT VAR_SEQ 597..722
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_039424"
FT VAR_SEQ 656..722
FT /note="LRMEYLSLMHAIVRTTPYLQHRHRLPDLQAILRRILNEEETSPQCQMDRMIV
FT REMCKEFLVLGEAPS -> GPFGAGQRPWPGVPRLLEPGSTPSREPHPVERSGVPALTS
FT SWASGCPRPLHPALQLVIDSAFGGRSV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10619843"
FT /id="VSP_003971"
FT VAR_SEQ 656..658
FT /note="LRM -> GVH (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15095401"
FT /id="VSP_039425"
FT VAR_SEQ 659..722
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15095401"
FT /id="VSP_039426"
FT VARIANT 324
FT /note="T -> S (in dbSNP:rs6785620)"
FT /id="VAR_051378"
FT VARIANT 660
FT /note="Y -> S (in dbSNP:rs17855516)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_063400"
FT HELIX 312..324
FT /evidence="ECO:0007829|PDB:6DEE"
FT HELIX 328..345
FT /evidence="ECO:0007829|PDB:6DEE"
FT HELIX 350..359
FT /evidence="ECO:0007829|PDB:6DEE"
FT HELIX 377..390
FT /evidence="ECO:0007829|PDB:6DED"
FT HELIX 401..404
FT /evidence="ECO:0007829|PDB:6DED"
FT HELIX 407..423
FT /evidence="ECO:0007829|PDB:6DED"
FT HELIX 426..450
FT /evidence="ECO:0007829|PDB:6DED"
FT HELIX 454..470
FT /evidence="ECO:0007829|PDB:6DED"
FT HELIX 472..480
FT /evidence="ECO:0007829|PDB:6DED"
FT HELIX 483..493
FT /evidence="ECO:0007829|PDB:6DED"
FT HELIX 498..511
FT /evidence="ECO:0007829|PDB:6DED"
FT TURN 512..514
FT /evidence="ECO:0007829|PDB:6DED"
FT HELIX 520..524
FT /evidence="ECO:0007829|PDB:6DED"
FT HELIX 528..539
FT /evidence="ECO:0007829|PDB:6DED"
FT HELIX 550..562
FT /evidence="ECO:0007829|PDB:6DED"
FT STRAND 568..570
FT /evidence="ECO:0007829|PDB:6DED"
FT HELIX 572..578
FT /evidence="ECO:0007829|PDB:6DED"
FT HELIX 584..596
FT /evidence="ECO:0007829|PDB:6DED"
FT HELIX 613..621
FT /evidence="ECO:0007829|PDB:6DED"
FT HELIX 625..628
FT /evidence="ECO:0007829|PDB:6DED"
FT HELIX 633..649
FT /evidence="ECO:0007829|PDB:6DED"
FT HELIX 657..670
FT /evidence="ECO:0007829|PDB:6DED"
FT HELIX 673..676
FT /evidence="ECO:0007829|PDB:6DED"
FT HELIX 680..691
FT /evidence="ECO:0007829|PDB:6DED"
FT HELIX 698..713
FT /evidence="ECO:0007829|PDB:6DED"
FT HELIX 715..717
FT /evidence="ECO:0007829|PDB:6DED"
SQ SEQUENCE 722 AA; 78960 MW; 7683046B94647332 CRC64;
MYRALYAFRS AEPNALAFAA GETFLVLERS SAHWWLAARA RSGETGYVPP AYLRRLQGLE
QDVLQAIDRA IEAVHNTAMR DGGKYSLEQR GVLQKLIHHR KETLSRRGPS ASSVAVMTSS
TSDHHLDAAA ARQPNGVCRA GFERQHSLPS SEHLGADGGL YQIPLPSSQI PPQPRRAAPT
TPPPPVKRRD REALMASGSG GHNTMPSGGN SVSSGSSVSS TSLDTLYTSS SPSEPGSSCS
PTPPPVPRRG THTTVSQVQP PPSKASAPEP PAEEEVATGT TSASDDLEAL GTLSLGTTEE
KAAAEAAVPR TIGAELMELV RRNTGLSHEL CRVAIGIIVG HIQASVPASS PVMEQVLLSL
VEGKDLSMAL PSGQVCHDQQ RLEVIFADLA RRKDDAQQRS WALYEDEGVI RCYLEELLHI
LTDADPEVCK KMCKRNEFES VLALVAYYQM EHRASLRLLL LKCFGAMCSL DAAIISTLVS
SVLPVELARD MQTDTQDHQK LCYSALILAM VFSMGEAVPY AHYEHLGTPF AQFLLNIVED
GLPLDTTEQL PDLCVNLLLA LNLHLPAADQ NVIMAALSKH ANVKIFSEKL LLLLNRGDDP
VRIFKHEPQP PHSVLKFLQD VFGSPATAAI FYHTDMMALI DITVRHIADL SPGDKLRMEY
LSLMHAIVRT TPYLQHRHRL PDLQAILRRI LNEEETSPQC QMDRMIVREM CKEFLVLGEA
PS
