KDIS_HUMAN
ID KDIS_HUMAN Reviewed; 1771 AA.
AC Q9ULH0; A1L4N4; Q4VC08; Q6MZU2; Q9H889; Q9H9E4; Q9NT37; Q9UF42;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 3.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Kinase D-interacting substrate of 220 kDa;
DE AltName: Full=Ankyrin repeat-rich membrane-spanning protein;
GN Name=KIDINS220; Synonyms=ARMS, KIAA1250;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:337-345(1999).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1636-1771 (ISOFORM 1), AND VARIANT HIS-1608.
RC TISSUE=Thyroid;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1089-1771 (ISOFORM 4), NUCLEOTIDE SEQUENCE [LARGE
RP SCALE MRNA] OF 1526-1771 (ISOFORM 1), AND VARIANT HIS-1608.
RC TISSUE=Esophageal carcinoma, and Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1478-1771, AND VARIANT HIS-1608.
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 [6]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=18089783; DOI=10.1158/0008-5472.can-07-1930;
RA Liao Y.-H., Hsu S.-M., Huang P.-H.;
RT "ARMS depletion facilitates UV irradiation induced apoptotic cell death in
RT melanoma.";
RL Cancer Res. 67:11547-11556(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-918; SER-1365 AND SER-1521,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1555, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1555 AND SER-1633, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-882; SER-885; THR-914;
RP SER-918; SER-1163; SER-1296; SER-1352; SER-1359; SER-1361; SER-1362;
RP SER-1365; SER-1521; SER-1526; SER-1555; SER-1574; SER-1623; SER-1633;
RP THR-1679; SER-1681 AND THR-1684, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-918, AND IDENTIFICATION BY
RP 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).
RN [16]
RP INVOLVEMENT IN SINO, VARIANTS SINO 1350-TRP--LEU-1771 DEL AND
RP 1366-GLN--LEU-1771 DEL, AND CHARACTERIZATION OF VARIANT SINO
RP 1350-TRP--LEU-1771 DEL AND 1366-GLN--LEU-1771 DEL.
RX PubMed=27005418; DOI=10.1093/hmg/ddw082;
RG DDD Study;
RA Josifova D.J., Monroe G.R., Tessadori F., de Graaff E., van der Zwaag B.,
RA Mehta S.G., Harakalova M., Duran K.J., Savelberg S.M., Nijman I.J.,
RA Jungbluth H., Hoogenraad C.C., Bakkers J., Knoers N.V., Firth H.V.,
RA Beales P.L., van Haaften G., van Haelst M.M.;
RT "Heterozygous KIDINS220/ARMS nonsense variants cause spastic paraplegia,
RT intellectual disability, nystagmus, and obesity.";
RL Hum. Mol. Genet. 25:2158-2167(2016).
RN [17]
RP INVOLVEMENT IN VENARG.
RX PubMed=28934391; DOI=10.1093/hmg/ddx263;
RA Mero I.L., Moerk H.H., Sheng Y., Blomhoff A., Opheim G.L., Erichsen A.,
RA Vigeland M.D., Selmer K.K.;
RT "Homozygous KIDINS220 loss-of-function variants in fetuses with cerebral
RT ventriculomegaly and limb contractures.";
RL Hum. Mol. Genet. 26:3792-3796(2017).
RN [18]
RP INVOLVEMENT IN VENARG.
RX PubMed=32909676; DOI=10.1002/ajmg.a.61858;
RA El-Dessouky S.H., Issa M.Y., Aboulghar M.M., Gaafar H.M., Elarab A.E.,
RA Ateya M.I., Omar H.H., Beetz C., Zaki M.S.;
RT "Prenatal delineation of a distinct lethal fetal syndrome caused by a
RT homozygous truncating KIDINS220 variant.";
RL Am. J. Med. Genet. A 182:2867-2876(2020).
RN [19]
RP VARIANT VENARG 713-GLN--LEU-715 DEL.
RX PubMed=33205811; DOI=10.1093/hmg/ddaa245;
RA Jacquemin V., Antoine M., Duerinckx S., Massart A., Desir J., Perazzolo C.,
RA Cassart M., Thomas D., Segers V., Lecomte S., Abramowicz M., Pirson I.;
RT "TrkA mediates effect of novel KIDINS220 mutation in human brain
RT ventriculomegaly.";
RL Hum. Mol. Genet. 29:3757-3764(2021).
CC -!- FUNCTION: Promotes a prolonged MAP-kinase signaling by neurotrophins
CC through activation of a Rap1-dependent mechanism. Provides a docking
CC site for the CRKL-C3G complex, resulting in Rap1-dependent sustained
CC ERK activation. May play an important role in regulating postsynaptic
CC signal transduction through the syntrophin-mediated localization of
CC receptor tyrosine kinases such as EPHA4. In cooperation with SNTA1 can
CC enhance EPHA4-induced JAK/STAT activation. Plays a role in nerve growth
CC factor (NGF)-induced recruitment of RAPGEF2 to late endosomes and
CC neurite outgrowth. May play a role in neurotrophin- and ephrin-mediated
CC neuronal outgrowth and in axon guidance during neural development and
CC in neuronal regeneration (By similarity). Modulates stress-induced
CC apoptosis of melanoma cells via regulation of the MEK/ERK signaling
CC pathway. {ECO:0000250, ECO:0000269|PubMed:18089783}.
CC -!- SUBUNIT: Found in a complex, at least composed of KIDINS220, MAGI2,
CC NTRK1 and RAPGEF2; the complex is mainly formed at late endosomes in a
CC nerve growth factor (NGF)-dependent manner. Interacts with RAPGEF2; the
CC interaction is strengthened after NGF stimulation. Isoform 2 interacts
CC (via C-terminal domain) with MAGI2 isoform 1 (via PDZ domain).
CC Interacts with NTRK1, NTRK2, NTRK3, ERKL and NGFR. Can form a ternary
CC complex with NGFR and NTRK1 and this complex is affected by the
CC expression levels of KIDINS220/ARMS. An increase in KIDINS220/ARMS
CC expression leads to a decreased association of NGFR and NTRK1.
CC Interacts (via PDZ-binding motif) with SNTA1 and SNTB2 (via PDZ
CC domains). Interacts with EPHA4 and PRKD1.
CC {ECO:0000250|UniProtKB:Q9EQG6}.
CC -!- INTERACTION:
CC Q9ULH0-2; Q13643: FHL3; NbExp=3; IntAct=EBI-11046235, EBI-741101;
CC Q9ULH0-2; O76011: KRT34; NbExp=3; IntAct=EBI-11046235, EBI-1047093;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}. Late endosome {ECO:0000250}. Note=Localized at
CC late endosome before or after nerve growth factor (NGF) stimulation.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q9ULH0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ULH0-2; Sequence=VSP_031862, VSP_031866;
CC Name=3;
CC IsoId=Q9ULH0-3; Sequence=VSP_031863, VSP_031864, VSP_031865;
CC Name=4;
CC IsoId=Q9ULH0-4; Sequence=VSP_031867;
CC Name=5;
CC IsoId=Q9ULH0-5; Sequence=VSP_031861;
CC -!- TISSUE SPECIFICITY: Abundant in developing and adult neural tissues as
CC well as neuroendocrine cells and dendritic cells. Overexpressed in
CC melanoma and melanoma cell lines. {ECO:0000269|PubMed:18089783}.
CC -!- DOMAIN: The transmembrane domain mediates interaction with NTRK1.
CC {ECO:0000250}.
CC -!- PTM: Tyrosine phosphorylated by NTRK1, NTRK2, EPHB2 and EPHA4.
CC Phosphorylation at Ser-918 is induced by phorbol ester treatment.
CC Phosphorylation by NTRK2 is induced by brain-derived neurotrophic
CC factor (BDNF) and neurotrophin-4/5. Phosphorylation by NTRK1 is induced
CC by nerve growth factor (NGF) (By similarity). {ECO:0000250}.
CC -!- DISEASE: Spastic paraplegia, intellectual disability, nystagmus, and
CC obesity (SINO) [MIM:617296]: An autosomal dominant syndrome
CC characterized by rapid growth in infancy, obesity, global developmental
CC delay, intellectual disability, spastic paraplegia, ocular defects, and
CC dysmorphic facial features. {ECO:0000269|PubMed:27005418}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Ventriculomegaly and arthrogryposis (VENARG) [MIM:619501]: An
CC autosomal recessive disorder with fatal outcome, characterized by
CC prenatal onset of severe features including limb contractures,
CC arthrogryposis, and enlarged brain ventricles that may be associated
CC with hydrocephalus, abnormalities of the corpus callosum, and
CC cerebellar hypoplasia. Some affected fetuses may also have congenital
CC heart disease and hydrops fetalis. Death occurs in utero.
CC {ECO:0000269|PubMed:28934391, ECO:0000269|PubMed:32909676,
CC ECO:0000269|PubMed:33205811}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA86564.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB14728.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB033076; BAA86564.2; ALT_INIT; mRNA.
DR EMBL; AK022873; BAB14285.1; -; mRNA.
DR EMBL; AK023926; BAB14728.1; ALT_INIT; mRNA.
DR EMBL; AL133620; CAB63746.1; -; mRNA.
DR EMBL; AL137553; CAB70807.1; -; mRNA.
DR EMBL; BX640878; CAE45935.1; -; mRNA.
DR EMBL; BC094714; AAH94714.1; -; mRNA.
DR EMBL; BC130610; AAI30611.1; -; mRNA.
DR CCDS; CCDS42650.1; -. [Q9ULH0-1]
DR CCDS; CCDS86818.1; -. [Q9ULH0-4]
DR CCDS; CCDS86819.1; -. [Q9ULH0-3]
DR PIR; T43458; T43458.
DR RefSeq; NP_065789.1; NM_020738.2. [Q9ULH0-1]
DR AlphaFoldDB; Q9ULH0; -.
DR SMR; Q9ULH0; -.
DR BioGRID; 121565; 175.
DR IntAct; Q9ULH0; 73.
DR MINT; Q9ULH0; -.
DR STRING; 9606.ENSP00000256707; -.
DR TCDB; 8.A.28.1.8; the ankyrin (ankyrin) family.
DR iPTMnet; Q9ULH0; -.
DR MetOSite; Q9ULH0; -.
DR PhosphoSitePlus; Q9ULH0; -.
DR SwissPalm; Q9ULH0; -.
DR BioMuta; KIDINS220; -.
DR DMDM; 172044825; -.
DR EPD; Q9ULH0; -.
DR jPOST; Q9ULH0; -.
DR MassIVE; Q9ULH0; -.
DR MaxQB; Q9ULH0; -.
DR PaxDb; Q9ULH0; -.
DR PeptideAtlas; Q9ULH0; -.
DR PRIDE; Q9ULH0; -.
DR ProteomicsDB; 85020; -. [Q9ULH0-1]
DR ProteomicsDB; 85021; -. [Q9ULH0-2]
DR ProteomicsDB; 85022; -. [Q9ULH0-3]
DR ProteomicsDB; 85023; -. [Q9ULH0-4]
DR ProteomicsDB; 85024; -. [Q9ULH0-5]
DR Antibodypedia; 6605; 283 antibodies from 32 providers.
DR DNASU; 57498; -.
DR Ensembl; ENST00000256707.8; ENSP00000256707.4; ENSG00000134313.17. [Q9ULH0-1]
DR Ensembl; ENST00000319688.5; ENSP00000319947.5; ENSG00000134313.17. [Q9ULH0-3]
DR Ensembl; ENST00000473731.5; ENSP00000418974.1; ENSG00000134313.17. [Q9ULH0-4]
DR Ensembl; ENST00000685097.1; ENSP00000510510.1; ENSG00000134313.17. [Q9ULH0-2]
DR GeneID; 57498; -.
DR KEGG; hsa:57498; -.
DR MANE-Select; ENST00000256707.8; ENSP00000256707.4; NM_020738.4; NP_065789.1.
DR UCSC; uc002qzc.2; human. [Q9ULH0-1]
DR CTD; 57498; -.
DR DisGeNET; 57498; -.
DR GeneCards; KIDINS220; -.
DR HGNC; HGNC:29508; KIDINS220.
DR HPA; ENSG00000134313; Low tissue specificity.
DR MalaCards; KIDINS220; -.
DR MIM; 615759; gene.
DR MIM; 617296; phenotype.
DR MIM; 619501; phenotype.
DR neXtProt; NX_Q9ULH0; -.
DR OpenTargets; ENSG00000134313; -.
DR Orphanet; 521390; Spastic paraplegia-intellectual disability-nystagmus-obesity syndrome.
DR PharmGKB; PA164721911; -.
DR VEuPathDB; HostDB:ENSG00000134313; -.
DR eggNOG; KOG0502; Eukaryota.
DR GeneTree; ENSGT00940000156714; -.
DR HOGENOM; CLU_001438_0_0_1; -.
DR InParanoid; Q9ULH0; -.
DR OMA; EENWPTC; -.
DR OrthoDB; 58543at2759; -.
DR PhylomeDB; Q9ULH0; -.
DR TreeFam; TF344032; -.
DR PathwayCommons; Q9ULH0; -.
DR Reactome; R-HSA-170984; ARMS-mediated activation.
DR Reactome; R-HSA-9696270; RND2 GTPase cycle.
DR Reactome; R-HSA-9696273; RND1 GTPase cycle.
DR SignaLink; Q9ULH0; -.
DR SIGNOR; Q9ULH0; -.
DR BioGRID-ORCS; 57498; 45 hits in 1083 CRISPR screens.
DR ChiTaRS; KIDINS220; human.
DR GeneWiki; KIDINS220; -.
DR GenomeRNAi; 57498; -.
DR Pharos; Q9ULH0; Tbio.
DR PRO; PR:Q9ULH0; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9ULH0; protein.
DR Bgee; ENSG00000134313; Expressed in middle frontal gyrus and 204 other tissues.
DR ExpressionAtlas; Q9ULH0; baseline and differential.
DR Genevisible; Q9ULH0; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005770; C:late endosome; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR GO; GO:0030165; F:PDZ domain binding; ISS:UniProtKB.
DR GO; GO:0019887; F:protein kinase regulator activity; IBA:GO_Central.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0048813; P:dendrite morphogenesis; IEA:Ensembl.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0038180; P:nerve growth factor signaling pathway; ISS:UniProtKB.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISS:UniProtKB.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 1.25.40.20; -; 3.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR011646; KAP_P-loop.
DR InterPro; IPR013761; SAM/pointed_sf.
DR Pfam; PF12796; Ank_2; 3.
DR Pfam; PF13637; Ank_4; 2.
DR Pfam; PF07693; KAP_NTPase; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 11.
DR SUPFAM; SSF47769; SSF47769; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 10.
PE 1: Evidence at protein level;
KW Alternative splicing; ANK repeat; Disease variant; Endosome;
KW Hereditary spastic paraplegia; Intellectual disability; Membrane;
KW Neurodegeneration; Neurogenesis; Obesity; Phosphoprotein;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix.
FT CHAIN 1..1771
FT /note="Kinase D-interacting substrate of 220 kDa"
FT /id="PRO_0000322119"
FT TOPO_DOM 1..499
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 500..520
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 521..524
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 525..545
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 546..659
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 660..680
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 681..685
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 686..706
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 707..1771
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 4..33
FT /note="ANK 1"
FT REPEAT 37..66
FT /note="ANK 2"
FT REPEAT 70..99
FT /note="ANK 3"
FT REPEAT 103..132
FT /note="ANK 4"
FT REPEAT 136..165
FT /note="ANK 5"
FT REPEAT 169..198
FT /note="ANK 6"
FT REPEAT 202..231
FT /note="ANK 7"
FT REPEAT 235..264
FT /note="ANK 8"
FT REPEAT 268..297
FT /note="ANK 9"
FT REPEAT 301..330
FT /note="ANK 10"
FT REPEAT 334..363
FT /note="ANK 11"
FT REPEAT 367..396
FT /note="ANK 12"
FT DOMAIN 440..953
FT /note="KAP NTPase"
FT REGION 1089..1092
FT /note="Mediates interaction with CRKL"
FT /evidence="ECO:0000250|UniProtKB:Q9EQG6"
FT REGION 1182..1202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1285..1310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1344..1368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1397..1564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1578..1633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1713..1771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1766..1771
FT /note="PDZ-binding"
FT /evidence="ECO:0000250|UniProtKB:Q9EQG6"
FT COMPBIAS 1345..1368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1397..1430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1431..1454
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1489..1507
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1531..1564
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1588..1602
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1603..1626
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1713..1745
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 882
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 885
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 914
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 918
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 1163
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1296
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1352
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1359
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1361
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1362
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1365
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1521
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1526
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1555
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 1574
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1623
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1633
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1679
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1681
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1684
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..1228
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_031861"
FT VAR_SEQ 1..42
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031862"
FT VAR_SEQ 135
FT /note="L -> LQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_031863"
FT VAR_SEQ 1005..1030
FT /note="ISKNIPTTKDVEPLLEIDGDIRNFEV -> CCGADSCDRDRIGISKSVLVAM
FT LMES (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_031864"
FT VAR_SEQ 1031..1771
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_031865"
FT VAR_SEQ 1138..1194
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031866"
FT VAR_SEQ 1177..1195
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_031867"
FT VARIANT 538
FT /note="I -> T (in dbSNP:rs2289229)"
FT /id="VAR_048285"
FT VARIANT 713..715
FT /note="Missing (in VENARG)"
FT /evidence="ECO:0000269|PubMed:33205811"
FT /id="VAR_086218"
FT VARIANT 1307
FT /note="R -> H (in dbSNP:rs2304591)"
FT /id="VAR_039399"
FT VARIANT 1350..1771
FT /note="Missing (in SINO; no effect on protein abundance)"
FT /evidence="ECO:0000269|PubMed:27005418"
FT /id="VAR_077995"
FT VARIANT 1366..1771
FT /note="Missing (in SINO; no effect on protein abundance; no
FT effect on subcellular localization)"
FT /evidence="ECO:0000269|PubMed:27005418"
FT /id="VAR_077996"
FT VARIANT 1608
FT /note="Q -> H (in dbSNP:rs1044280)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005"
FT /id="VAR_039400"
FT CONFLICT 1335
FT /note="T -> P (in Ref. 4; CAE45935)"
FT /evidence="ECO:0000305"
FT CONFLICT 1613
FT /note="N -> D (in Ref. 3; BAB14285)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1771 AA; 196542 MW; FD1F99DB88B6996D CRC64;
MSVLISQSVI NYVEEENIPA LKALLEKCKD VDERNECGQT PLMIAAEQGN LEIVKELIKN
GANCNLEDLD NWTALISASK EGHVHIVEEL LKCGVNLEHR DMGGWTALMW ACYKGRTDVV
ELLLSHGANP SVTGLYSVYP IIWAAGRGHA DIVHLLLQNG AKVNCSDKYG TTPLVWAARK
GHLECVKHLL AMGADVDQEG ANSMTALIVA VKGGYTQSVK EILKRNPNVN LTDKDGNTAL
MIASKEGHTE IVQDLLDAGT YVNIPDRSGD TVLIGAVRGG HVEIVRALLQ KYADIDIRGQ
DNKTALYWAV EKGNATMVRD ILQCNPDTEI CTKDGETPLI KATKMRNIEV VELLLDKGAK
VSAVDKKGDT PLHIAIRGRS RKLAELLLRN PKDGRLLYRP NKAGETPYNI DCSHQKSILT
QIFGARHLSP TETDGDMLGY DLYSSALADI LSEPTMQPPI CVGLYAQWGS GKSFLLKKLE
DEMKTFAGQQ IEPLFQFSWL IVFLTLLLCG GLGLLFAFTV HPNLGIAVSL SFLALLYIFF
IVIYFGGRRE GESWNWAWVL STRLARHIGY LELLLKLMFV NPPELPEQTT KALPVRFLFT
DYNRLSSVGG ETSLAEMIAT LSDACEREFG FLATRLFRVF KTEDTQGKKK WKKTCCLPSF
VIFLFIIGCI ISGITLLAIF RVDPKHLTVN AVLISIASVV GLAFVLNCRT WWQVLDSLLN
SQRKRLHNAA SKLHKLKSEG FMKVLKCEVE LMARMAKTID SFTQNQTRLV VIIDGLDACE
QDKVLQMLDT VRVLFSKGPF IAIFASDPHI IIKAINQNLN SVLRDSNING HDYMRNIVHL
PVFLNSRGLS NARKFLVTSA TNGDVPCSDT TGIQEDADRR VSQNSLGEMT KLGSKTALNR
RDTYRRRQMQ RTITRQMSFD LTKLLVTEDW FSDISPQTMR RLLNIVSVTG RLLRANQISF
NWDRLASWIN LTEQWPYRTS WLILYLEETE GIPDQMTLKT IYERISKNIP TTKDVEPLLE
IDGDIRNFEV FLSSRTPVLV ARDVKVFLPC TVNLDPKLRE IIADVRAARE QISIGGLAYP
PLPLHEGPPR APSGYSQPPS VCSSTSFNGP FAGGVVSPQP HSSYYSGMTG PQHPFYNRPF
FAPYLYTPRY YPGGSQHLIS RPSVKTSLPR DQNNGLEVIK EDAAEGLSSP TDSSRGSGPA
PGPVVLLNSL NVDAVCEKLK QIEGLDQSML PQYCTTIKKA NINGRVLAQC NIDELKKEMN
MNFGDWHLFR STVLEMRNAE SHVVPEDPRF LSESSSGPAP HGEPARRASH NELPHTELSS
QTPYTLNFSF EELNTLGLDE GAPRHSNLSW QSQTRRTPSL SSLNSQDSSI EISKLTDKVQ
AEYRDAYREY IAQMSQLEGG PGSTTISGRS SPHSTYYMGQ SSSGGSIHSN LEQEKGKDSE
PKPDDGRKSF LMKRGDVIDY SSSGVSTNDA SPLDPITEED EKSDQSGSKL LPGKKSSERS
SLFQTDLKLK GSGLRYQKLP SDEDESGTEE SDNTPLLKDD KDRKAEGKVE RVPKSPEHSA
EPIRTFIKAK EYLSDALLDK KDSSDSGVRS SESSPNHSLH NEVADDSQLE KANLIELEDD
SHSGKRGIPH SLSGLQDPII ARMSICSEDK KSPSECSLIA SSPEENWPAC QKAYNLNRTP
STVTLNNNSA PANRANQNFD EMEGIRETSQ VILRPSSSPN PTTIQNENLK SMTHKRSQRS
SYTRLSKDPP ELHAAASSES TGFGEERESI L
