KANK2_HUMAN
ID KANK2_HUMAN Reviewed; 851 AA.
AC Q63ZY3; B0I1P4; Q3KQZ3; Q6GUF5; Q9H8S4; Q9NUP0; Q9P210;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=KN motif and ankyrin repeat domain-containing protein 2;
DE AltName: Full=Ankyrin repeat domain-containing protein 25;
DE AltName: Full=Matrix-remodeling-associated protein 3;
DE AltName: Full=SRC-1-interacting protein;
DE Short=SIP;
DE Short=SRC-interacting protein;
DE Short=SRC1-interacting protein;
GN Name=KANK2; Synonyms=ANKRD25, KIAA1518, MXRA3, SIP;
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 2), FUNCTION, INTERACTION WITH NCOA1;
RP NCOA2 AND NCOA3, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND MUTAGENESIS OF
RP 510-SER--SER-512 AND SER-515.
RX PubMed=17476305; DOI=10.1038/sj.emboj.7601710;
RA Zhang Y., Zhang H., Liang J., Yu W., Shang Y.;
RT "SIP, a novel ankyrin repeat containing protein, sequesters steroid
RT receptor coactivators in the cytoplasm.";
RL EMBO J. 26:2645-2657(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Zhu Y., Kakinuma N., Wang Y., Kiyama R.;
RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Spleen;
RX PubMed=10819331; DOI=10.1093/dnares/7.2.143;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:143-150(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cervix, and Lung;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 386-841 (ISOFORM 3).
RC TISSUE=Ovary, and Placenta;
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19 AND SER-375, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17996375; DOI=10.1016/j.bbagen.2007.09.017;
RA Zhu Y., Kakinuma N., Wang Y., Kiyama R.;
RT "Kank proteins: a new family of ankyrin-repeat domain-containing
RT proteins.";
RL Biochim. Biophys. Acta 1780:128-133(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356 AND THR-472, AND
RP 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375, 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 [13]
RP TISSUE SPECIFICITY.
RX PubMed=20720434; DOI=10.1159/000320049;
RA Xu X., Patrakka J., Sistani L., Uhlen M., Jalanko H., Betsholtz C.,
RA Tryggvason K.;
RT "Expression of novel podocyte-associated proteins sult1b1 and ankrd25.";
RL Nephron Exp. Nephrol. 117:E39-E46(2011).
RN [14]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH AIFM1, AND REGION.
RX PubMed=22371500; DOI=10.1074/jbc.m111.334151;
RA Wang D., Liang J., Zhang Y., Gui B., Wang F., Yi X., Sun L., Yao Z.,
RA Shang Y.;
RT "Steroid receptor coactivator-interacting protein (SIP) inhibits caspase-
RT independent apoptosis by preventing apoptosis-inducing factor (AIF) from
RT being released from mitochondria.";
RL J. Biol. Chem. 287:12612-12621(2012).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356; SER-375 AND SER-540, AND
RP IDENTIFICATION BY 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 [16]
RP FUNCTION, INVOLVEMENT IN PPKWH, AND VARIANT PPKWH VAL-670.
RX PubMed=24671081; DOI=10.1136/jmedgenet-2014-102346;
RA Ramot Y., Molho-Pessach V., Meir T., Alper-Pinus R., Siam I., Tams S.,
RA Babay S., Zlotogorski A.;
RT "Mutation in KANK2, encoding a sequestering protein for steroid receptor
RT coactivators, causes keratoderma and woolly hair.";
RL J. Med. Genet. 51:388-394(2014).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92; SER-323; THR-329;
RP SER-375; SER-540 AND THR-552, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [18]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-105, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [19]
RP FUNCTION, INTERACTION WITH ARHGDIA, SUBCELLULAR LOCATION, INVOLVEMENT IN
RP NPHS16, VARIANTS NPHS16 GLY-181 AND PHE-676, AND CHARACTERIZATION OF
RP VARIANTS NPHS16 GLY-181 AND PHE-684.
RX PubMed=25961457; DOI=10.1172/jci79504;
RA Gee H.Y., Zhang F., Ashraf S., Kohl S., Sadowski C.E., Vega-Warner V.,
RA Zhou W., Lovric S., Fang H., Nettleton M., Zhu J.Y., Hoefele J.,
RA Weber L.T., Podracka L., Boor A., Fehrenbach H., Innis J.W., Washburn J.,
RA Levy S., Lifton R.P., Otto E.A., Han Z., Hildebrandt F.;
RT "KANK deficiency leads to podocyte dysfunction and nephrotic syndrome.";
RL J. Clin. Invest. 125:2375-2384(2015).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) OF 578-832.
RG Structural genomics consortium (SGC);
RT "Crystal structure of KANK2 ankyrin repeats.";
RL Submitted (DEC-2012) to the PDB data bank.
RN [21] {ECO:0007744|PDB:5YBV}
RP X-RAY CRYSTALLOGRAPHY (2.12 ANGSTROMS) OF 578-832 IN COMPLEX WITH KIF21A
RP PEPTIDE, INTERACTION WITH KIF21A, AND MUTAGENESIS OF TYR-702; ASP-803 AND
RP ASP-805.
RX PubMed=29183992; DOI=10.1074/jbc.m117.817494;
RA Guo Q., Liao S., Zhu Z., Li Y., Li F., Xu C.;
RT "Structural basis for the recognition of kinesin family member 21A (KIF21A)
RT by the ankyrin domains of KANK1 and KANK2 proteins.";
RL J. Biol. Chem. 293:557-566(2018).
CC -!- FUNCTION: Involved in transcription regulation by sequestering in the
CC cytoplasm nuclear receptor coactivators such as NCOA1, NCOA2 and NCOA3
CC (PubMed:17476305). Involved in regulation of caspase-independent
CC apoptosis by sequestering the proapoptotic factor AIFM1 in mitochondria
CC (PubMed:22371500). Pro-apoptotic stimuli can induce its proteasomal
CC degradation allowing the translocation of AIFM1 to the nucleus to
CC induce apoptosis (PubMed:22371500). Involved in the negative control of
CC vitamin D receptor signaling pathway (PubMed:24671081). Involved in
CC actin stress fibers formation through its interaction with ARHGDIA and
CC the regulation of the Rho signaling pathway (PubMed:17996375,
CC PubMed:25961457). May thereby play a role in cell adhesion and
CC migration, regulating for instance podocytes migration during
CC development of the kidney (PubMed:25961457). Through the Rho signaling
CC pathway may also regulate cell proliferation (By similarity).
CC {ECO:0000250|UniProtKB:Q8BX02, ECO:0000269|PubMed:17476305,
CC ECO:0000269|PubMed:17996375, ECO:0000269|PubMed:22371500,
CC ECO:0000269|PubMed:24671081, ECO:0000269|PubMed:25961457}.
CC -!- SUBUNIT: Interacts (non-phosphorylated form) with NCOA1; NCOA2 AND
CC NCOA3 (PubMed:17476305). Interacts with AIFM1 (PubMed:22371500).
CC Interacts with ARHGDIA; the interaction is direct and may regulate the
CC interaction of ARHGDIA with RHOA, RAC1 and CDC42 (PubMed:25961457).
CC Interacts (via ANK repeats 1-5) with KIF21A (via residues 1146-1167)
CC (PubMed:29183992). {ECO:0000269|PubMed:17476305,
CC ECO:0000269|PubMed:22371500, ECO:0000269|PubMed:25961457,
CC ECO:0000269|PubMed:29183992}.
CC -!- INTERACTION:
CC Q63ZY3; Q9P2A4: ABI3; NbExp=6; IntAct=EBI-2556193, EBI-742038;
CC Q63ZY3; Q9ULW3: ABT1; NbExp=3; IntAct=EBI-2556193, EBI-2602396;
CC Q63ZY3; Q8WTP8-2: AEN; NbExp=3; IntAct=EBI-2556193, EBI-12119298;
CC Q63ZY3; O95831: AIFM1; NbExp=2; IntAct=EBI-2556193, EBI-356440;
CC Q63ZY3; X5D778: ANKRD11; NbExp=3; IntAct=EBI-2556193, EBI-17183751;
CC Q63ZY3; P63010-2: AP2B1; NbExp=3; IntAct=EBI-2556193, EBI-11529439;
CC Q63ZY3; Q8N8R7: ARL14EP; NbExp=3; IntAct=EBI-2556193, EBI-2807994;
CC Q63ZY3; Q8WXK1: ASB15; NbExp=3; IntAct=EBI-2556193, EBI-12809012;
CC Q63ZY3; Q8N7W2-2: BEND7; NbExp=3; IntAct=EBI-2556193, EBI-10181188;
CC Q63ZY3; Q96CA5: BIRC7; NbExp=3; IntAct=EBI-2556193, EBI-517623;
CC Q63ZY3; Q9H2G9: BLZF1; NbExp=3; IntAct=EBI-2556193, EBI-2548012;
CC Q63ZY3; Q96GS4: BORCS6; NbExp=3; IntAct=EBI-2556193, EBI-10193358;
CC Q63ZY3; Q9H5F2: C11orf1; NbExp=3; IntAct=EBI-2556193, EBI-718615;
CC Q63ZY3; Q2NKX9: C2orf68; NbExp=3; IntAct=EBI-2556193, EBI-11603468;
CC Q63ZY3; A2RRN7: CADPS; NbExp=3; IntAct=EBI-2556193, EBI-10179719;
CC Q63ZY3; Q13555-5: CAMK2G; NbExp=3; IntAct=EBI-2556193, EBI-12020154;
CC Q63ZY3; P20807-4: CAPN3; NbExp=3; IntAct=EBI-2556193, EBI-11532021;
CC Q63ZY3; Q9BWT7: CARD10; NbExp=3; IntAct=EBI-2556193, EBI-3866279;
CC Q63ZY3; Q9H257-2: CARD9; NbExp=3; IntAct=EBI-2556193, EBI-11530605;
CC Q63ZY3; Q9HC52: CBX8; NbExp=3; IntAct=EBI-2556193, EBI-712912;
CC Q63ZY3; Q2TAC2-2: CCDC57; NbExp=3; IntAct=EBI-2556193, EBI-10961624;
CC Q63ZY3; A6NC98: CCDC88B; NbExp=3; IntAct=EBI-2556193, EBI-347573;
CC Q63ZY3; Q86Y33-5: CDC20B; NbExp=3; IntAct=EBI-2556193, EBI-11983537;
CC Q63ZY3; Q99459: CDC5L; NbExp=3; IntAct=EBI-2556193, EBI-374880;
CC Q63ZY3; Q07002: CDK18; NbExp=3; IntAct=EBI-2556193, EBI-746238;
CC Q63ZY3; Q8IVW4: CDKL3; NbExp=3; IntAct=EBI-2556193, EBI-3919850;
CC Q63ZY3; P40199: CEACAM6; NbExp=3; IntAct=EBI-2556193, EBI-4314501;
CC Q63ZY3; Q53EZ4: CEP55; NbExp=3; IntAct=EBI-2556193, EBI-747776;
CC Q63ZY3; Q96MT8-3: CEP63; NbExp=3; IntAct=EBI-2556193, EBI-11522539;
CC Q63ZY3; Q8NHQ1: CEP70; NbExp=6; IntAct=EBI-2556193, EBI-739624;
CC Q63ZY3; Q9NX63: CHCHD3; NbExp=3; IntAct=EBI-2556193, EBI-743375;
CC Q63ZY3; Q9UKJ5: CHIC2; NbExp=3; IntAct=EBI-2556193, EBI-741528;
CC Q63ZY3; Q9BW66: CINP; NbExp=3; IntAct=EBI-2556193, EBI-739784;
CC Q63ZY3; Q9Y2V7: COG6; NbExp=3; IntAct=EBI-2556193, EBI-3866319;
CC Q63ZY3; O43186: CRX; NbExp=3; IntAct=EBI-2556193, EBI-748171;
CC Q63ZY3; Q9NTM9: CUTC; NbExp=3; IntAct=EBI-2556193, EBI-714918;
CC Q63ZY3; Q2TBE0: CWF19L2; NbExp=3; IntAct=EBI-2556193, EBI-5453285;
CC Q63ZY3; Q9UIA0: CYTH4; NbExp=3; IntAct=EBI-2556193, EBI-11521003;
CC Q63ZY3; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-2556193, EBI-742054;
CC Q63ZY3; O95886: DLGAP3; NbExp=3; IntAct=EBI-2556193, EBI-1752541;
CC Q63ZY3; A0A0U1RQF7: DPEP2NB; NbExp=3; IntAct=EBI-2556193, EBI-18398199;
CC Q63ZY3; Q86UW9: DTX2; NbExp=3; IntAct=EBI-2556193, EBI-740376;
CC Q63ZY3; P63167: DYNLL1; NbExp=6; IntAct=EBI-2556193, EBI-349105;
CC Q63ZY3; Q96FJ2: DYNLL2; NbExp=3; IntAct=EBI-2556193, EBI-742371;
CC Q63ZY3; Q5JST6: EFHC2; NbExp=3; IntAct=EBI-2556193, EBI-2349927;
CC Q63ZY3; P06730: EIF4E; NbExp=7; IntAct=EBI-2556193, EBI-73440;
CC Q63ZY3; Q14241: ELOA; NbExp=3; IntAct=EBI-2556193, EBI-742350;
CC Q63ZY3; Q96B26: EXOSC8; NbExp=3; IntAct=EBI-2556193, EBI-371922;
CC Q63ZY3; Q3B820: FAM161A; NbExp=3; IntAct=EBI-2556193, EBI-719941;
CC Q63ZY3; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-2556193, EBI-6658203;
CC Q63ZY3; Q14192: FHL2; NbExp=6; IntAct=EBI-2556193, EBI-701903;
CC Q63ZY3; Q13643: FHL3; NbExp=3; IntAct=EBI-2556193, EBI-741101;
CC Q63ZY3; O75344: FKBP6; NbExp=3; IntAct=EBI-2556193, EBI-744771;
CC Q63ZY3; Q8TAE8: GADD45GIP1; NbExp=3; IntAct=EBI-2556193, EBI-372506;
CC Q63ZY3; Q8NHY3: GAS2L2; NbExp=3; IntAct=EBI-2556193, EBI-7960826;
CC Q63ZY3; P15976-2: GATA1; NbExp=3; IntAct=EBI-2556193, EBI-9090198;
CC Q63ZY3; P57678: GEMIN4; NbExp=3; IntAct=EBI-2556193, EBI-356700;
CC Q63ZY3; Q5VSY0: GKAP1; NbExp=5; IntAct=EBI-2556193, EBI-743722;
CC Q63ZY3; Q96IK5: GMCL1; NbExp=3; IntAct=EBI-2556193, EBI-2548508;
CC Q63ZY3; O75496: GMNN; NbExp=3; IntAct=EBI-2556193, EBI-371669;
CC Q63ZY3; Q9NVN8: GNL3L; NbExp=3; IntAct=EBI-2556193, EBI-746682;
CC Q63ZY3; Q08379: GOLGA2; NbExp=7; IntAct=EBI-2556193, EBI-618309;
CC Q63ZY3; Q9NYA3: GOLGA6A; NbExp=3; IntAct=EBI-2556193, EBI-11163335;
CC Q63ZY3; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-2556193, EBI-5916454;
CC Q63ZY3; O95872: GPANK1; NbExp=3; IntAct=EBI-2556193, EBI-751540;
CC Q63ZY3; Q92917: GPKOW; NbExp=3; IntAct=EBI-2556193, EBI-746309;
CC Q63ZY3; Q86YR5-3: GPSM1; NbExp=3; IntAct=EBI-2556193, EBI-10261098;
CC Q63ZY3; Q13322-4: GRB10; NbExp=3; IntAct=EBI-2556193, EBI-12353035;
CC Q63ZY3; P61296-2: HAND2; NbExp=3; IntAct=EBI-2556193, EBI-13086076;
CC Q63ZY3; Q9NSC5: HOMER3; NbExp=3; IntAct=EBI-2556193, EBI-748420;
CC Q63ZY3; O75031: HSF2BP; NbExp=3; IntAct=EBI-2556193, EBI-7116203;
CC Q63ZY3; Q16082: HSPB2; NbExp=3; IntAct=EBI-2556193, EBI-739395;
CC Q63ZY3; Q8IYA8: IHO1; NbExp=6; IntAct=EBI-2556193, EBI-8638439;
CC Q63ZY3; Q9UKT9: IKZF3; NbExp=3; IntAct=EBI-2556193, EBI-747204;
CC Q63ZY3; Q14005-2: IL16; NbExp=6; IntAct=EBI-2556193, EBI-17178971;
CC Q63ZY3; Q9C086: INO80B; NbExp=3; IntAct=EBI-2556193, EBI-715611;
CC Q63ZY3; Q9HAQ2: KIF9; NbExp=3; IntAct=EBI-2556193, EBI-8472129;
CC Q63ZY3; Q92845: KIFAP3; NbExp=3; IntAct=EBI-2556193, EBI-954040;
CC Q63ZY3; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-2556193, EBI-14069005;
CC Q63ZY3; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-2556193, EBI-3044087;
CC Q63ZY3; O76011: KRT34; NbExp=3; IntAct=EBI-2556193, EBI-1047093;
CC Q63ZY3; Q6A162: KRT40; NbExp=3; IntAct=EBI-2556193, EBI-10171697;
CC Q63ZY3; O95678: KRT75; NbExp=3; IntAct=EBI-2556193, EBI-2949715;
CC Q63ZY3; O43790: KRT86; NbExp=3; IntAct=EBI-2556193, EBI-9996498;
CC Q63ZY3; Q96JM7-2: L3MBTL3; NbExp=3; IntAct=EBI-2556193, EBI-11985629;
CC Q63ZY3; P52954: LBX1; NbExp=3; IntAct=EBI-2556193, EBI-20141748;
CC Q63ZY3; Q96BZ8: LENG1; NbExp=3; IntAct=EBI-2556193, EBI-726510;
CC Q63ZY3; P48742: LHX1; NbExp=3; IntAct=EBI-2556193, EBI-11990598;
CC Q63ZY3; Q9UBR4-2: LHX3; NbExp=3; IntAct=EBI-2556193, EBI-12039345;
CC Q63ZY3; P25800: LMO1; NbExp=9; IntAct=EBI-2556193, EBI-8639312;
CC Q63ZY3; P25791: LMO2; NbExp=3; IntAct=EBI-2556193, EBI-739696;
CC Q63ZY3; P25791-3: LMO2; NbExp=3; IntAct=EBI-2556193, EBI-11959475;
CC Q63ZY3; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-2556193, EBI-11742507;
CC Q63ZY3; P61968: LMO4; NbExp=6; IntAct=EBI-2556193, EBI-2798728;
CC Q63ZY3; Q9Y250: LZTS1; NbExp=3; IntAct=EBI-2556193, EBI-1216080;
CC Q63ZY3; O15481: MAGEB4; NbExp=6; IntAct=EBI-2556193, EBI-751857;
CC Q63ZY3; P59942: MCCD1; NbExp=3; IntAct=EBI-2556193, EBI-11987923;
CC Q63ZY3; Q96EZ8: MCRS1; NbExp=3; IntAct=EBI-2556193, EBI-348259;
CC Q63ZY3; A0JLT2-2: MED19; NbExp=3; IntAct=EBI-2556193, EBI-13288755;
CC Q63ZY3; P50221: MEOX1; NbExp=3; IntAct=EBI-2556193, EBI-2864512;
CC Q63ZY3; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-2556193, EBI-16439278;
CC Q63ZY3; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-2556193, EBI-10172526;
CC Q63ZY3; Q8WV92: MITD1; NbExp=3; IntAct=EBI-2556193, EBI-2691489;
CC Q63ZY3; Q13064: MKRN3; NbExp=3; IntAct=EBI-2556193, EBI-2340269;
CC Q63ZY3; Q8NEH6: MNS1; NbExp=3; IntAct=EBI-2556193, EBI-743811;
CC Q63ZY3; Q9H8S9: MOB1A; NbExp=6; IntAct=EBI-2556193, EBI-748229;
CC Q63ZY3; Q70IA8: MOB3C; NbExp=3; IntAct=EBI-2556193, EBI-9679267;
CC Q63ZY3; Q6PF18: MORN3; NbExp=3; IntAct=EBI-2556193, EBI-9675802;
CC Q63ZY3; Q4VC12: MSS51; NbExp=3; IntAct=EBI-2556193, EBI-11599933;
CC Q63ZY3; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-2556193, EBI-11522433;
CC Q63ZY3; Q8TDC0: MYOZ3; NbExp=3; IntAct=EBI-2556193, EBI-5662487;
CC Q63ZY3; Q15788: NCOA1; NbExp=4; IntAct=EBI-2556193, EBI-455189;
CC Q63ZY3; Q7Z6G3-2: NECAB2; NbExp=3; IntAct=EBI-2556193, EBI-10172876;
CC Q63ZY3; P18615: NELFE; NbExp=3; IntAct=EBI-2556193, EBI-348444;
CC Q63ZY3; O43482: OIP5; NbExp=3; IntAct=EBI-2556193, EBI-536879;
CC Q63ZY3; P26367: PAX6; NbExp=3; IntAct=EBI-2556193, EBI-747278;
CC Q63ZY3; P61457: PCBD1; NbExp=3; IntAct=EBI-2556193, EBI-740475;
CC Q63ZY3; O76083-2: PDE9A; NbExp=3; IntAct=EBI-2556193, EBI-11524542;
CC Q63ZY3; Q9NR12: PDLIM7; NbExp=3; IntAct=EBI-2556193, EBI-350517;
CC Q63ZY3; O15212: PFDN6; NbExp=3; IntAct=EBI-2556193, EBI-356973;
CC Q63ZY3; Q4G0R1: PIBF1; NbExp=3; IntAct=EBI-2556193, EBI-14066006;
CC Q63ZY3; Q9UM63: PLAGL1; NbExp=3; IntAct=EBI-2556193, EBI-7233410;
CC Q63ZY3; Q9UPG8: PLAGL2; NbExp=3; IntAct=EBI-2556193, EBI-2876622;
CC Q63ZY3; Q9HB19: PLEKHA2; NbExp=3; IntAct=EBI-2556193, EBI-4401947;
CC Q63ZY3; Q96T60: PNKP; NbExp=3; IntAct=EBI-2556193, EBI-1045072;
CC Q63ZY3; P62140: PPP1CB; NbExp=3; IntAct=EBI-2556193, EBI-352350;
CC Q63ZY3; Q9GZV8: PRDM14; NbExp=3; IntAct=EBI-2556193, EBI-3957793;
CC Q63ZY3; Q9NQX0: PRDM6; NbExp=3; IntAct=EBI-2556193, EBI-11320284;
CC Q63ZY3; P31321: PRKAR1B; NbExp=3; IntAct=EBI-2556193, EBI-2805516;
CC Q63ZY3; O14744: PRMT5; NbExp=3; IntAct=EBI-2556193, EBI-351098;
CC Q63ZY3; Q99633: PRPF18; NbExp=3; IntAct=EBI-2556193, EBI-2798416;
CC Q63ZY3; Q8WWY3: PRPF31; NbExp=3; IntAct=EBI-2556193, EBI-1567797;
CC Q63ZY3; Q6MZQ0: PRR5L; NbExp=3; IntAct=EBI-2556193, EBI-1567866;
CC Q63ZY3; P28070: PSMB4; NbExp=3; IntAct=EBI-2556193, EBI-603350;
CC Q63ZY3; O43586: PSTPIP1; NbExp=3; IntAct=EBI-2556193, EBI-1050964;
CC Q63ZY3; Q7L804: RAB11FIP2; NbExp=3; IntAct=EBI-2556193, EBI-1049676;
CC Q63ZY3; Q15311: RALBP1; NbExp=3; IntAct=EBI-2556193, EBI-749285;
CC Q63ZY3; Q9BYM8: RBCK1; NbExp=3; IntAct=EBI-2556193, EBI-2340624;
CC Q63ZY3; Q15669: RHOH; NbExp=3; IntAct=EBI-2556193, EBI-1244971;
CC Q63ZY3; O76064: RNF8; NbExp=3; IntAct=EBI-2556193, EBI-373337;
CC Q63ZY3; Q6ZMJ2-2: SCARA5; NbExp=3; IntAct=EBI-2556193, EBI-12823227;
CC Q63ZY3; Q9BWG6: SCNM1; NbExp=6; IntAct=EBI-2556193, EBI-748391;
CC Q63ZY3; Q9UJW9: SERTAD3; NbExp=3; IntAct=EBI-2556193, EBI-748621;
CC Q63ZY3; O95295: SNAPIN; NbExp=3; IntAct=EBI-2556193, EBI-296723;
CC Q63ZY3; Q13573: SNW1; NbExp=3; IntAct=EBI-2556193, EBI-632715;
CC Q63ZY3; O60504: SORBS3; NbExp=3; IntAct=EBI-2556193, EBI-741237;
CC Q63ZY3; Q8WUK8: STAC; NbExp=3; IntAct=EBI-2556193, EBI-10276615;
CC Q63ZY3; Q99469: STAC; NbExp=3; IntAct=EBI-2556193, EBI-2652799;
CC Q63ZY3; Q5T7P8-2: SYT6; NbExp=6; IntAct=EBI-2556193, EBI-10246152;
CC Q63ZY3; Q86VP1: TAX1BP1; NbExp=3; IntAct=EBI-2556193, EBI-529518;
CC Q63ZY3; Q8IYF3-3: TEX11; NbExp=3; IntAct=EBI-2556193, EBI-11523345;
CC Q63ZY3; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-2556193, EBI-1105213;
CC Q63ZY3; O43548: TGM5; NbExp=3; IntAct=EBI-2556193, EBI-12027348;
CC Q63ZY3; Q9NVV9: THAP1; NbExp=3; IntAct=EBI-2556193, EBI-741515;
CC Q63ZY3; Q8TBB0: THAP6; NbExp=3; IntAct=EBI-2556193, EBI-3925505;
CC Q63ZY3; Q96CG3: TIFA; NbExp=3; IntAct=EBI-2556193, EBI-740711;
CC Q63ZY3; Q08117: TLE5; NbExp=3; IntAct=EBI-2556193, EBI-717810;
CC Q63ZY3; Q08117-2: TLE5; NbExp=6; IntAct=EBI-2556193, EBI-11741437;
CC Q63ZY3; O95985: TOP3B; NbExp=3; IntAct=EBI-2556193, EBI-373403;
CC Q63ZY3; Q13077: TRAF1; NbExp=3; IntAct=EBI-2556193, EBI-359224;
CC Q63ZY3; Q12933: TRAF2; NbExp=3; IntAct=EBI-2556193, EBI-355744;
CC Q63ZY3; Q9BUZ4: TRAF4; NbExp=3; IntAct=EBI-2556193, EBI-3650647;
CC Q63ZY3; Q96RU7: TRIB3; NbExp=5; IntAct=EBI-2556193, EBI-492476;
CC Q63ZY3; Q9UPQ4-2: TRIM35; NbExp=3; IntAct=EBI-2556193, EBI-17716262;
CC Q63ZY3; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-2556193, EBI-2130429;
CC Q63ZY3; Q9BZW7: TSGA10; NbExp=3; IntAct=EBI-2556193, EBI-744794;
CC Q63ZY3; Q3SY00: TSGA10IP; NbExp=3; IntAct=EBI-2556193, EBI-10241197;
CC Q63ZY3; Q8N831: TSPYL6; NbExp=3; IntAct=EBI-2556193, EBI-12023322;
CC Q63ZY3; P40222: TXLNA; NbExp=6; IntAct=EBI-2556193, EBI-359793;
CC Q63ZY3; Q5T6F2: UBAP2; NbExp=3; IntAct=EBI-2556193, EBI-2514383;
CC Q63ZY3; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-2556193, EBI-739895;
CC Q63ZY3; Q5TAP6: UTP14C; NbExp=3; IntAct=EBI-2556193, EBI-11737646;
CC Q63ZY3; Q2NL98: VMAC; NbExp=3; IntAct=EBI-2556193, EBI-2803134;
CC Q63ZY3; Q8N1B4: VPS52; NbExp=3; IntAct=EBI-2556193, EBI-2799833;
CC Q63ZY3; Q2TAL6: VWC2; NbExp=3; IntAct=EBI-2556193, EBI-11957238;
CC Q63ZY3; Q9UPY6-2: WASF3; NbExp=3; IntAct=EBI-2556193, EBI-12026286;
CC Q63ZY3; B2RXF5: ZBTB42; NbExp=3; IntAct=EBI-2556193, EBI-12287587;
CC Q63ZY3; Q9NU63-3: ZFP57; NbExp=3; IntAct=EBI-2556193, EBI-12879708;
CC Q63ZY3; Q96NC0: ZMAT2; NbExp=3; IntAct=EBI-2556193, EBI-2682299;
CC Q63ZY3; Q9H0C1: ZMYND12; NbExp=3; IntAct=EBI-2556193, EBI-12030590;
CC Q63ZY3; Q9UDV6: ZNF212; NbExp=3; IntAct=EBI-2556193, EBI-1640204;
CC Q63ZY3; Q96IQ9: ZNF414; NbExp=3; IntAct=EBI-2556193, EBI-744257;
CC Q63ZY3; Q8TAU3: ZNF417; NbExp=3; IntAct=EBI-2556193, EBI-740727;
CC Q63ZY3; Q96ME7: ZNF512; NbExp=3; IntAct=EBI-2556193, EBI-10986895;
CC Q63ZY3; Q5T619: ZNF648; NbExp=3; IntAct=EBI-2556193, EBI-11985915;
CC Q63ZY3; Q6NX45: ZNF774; NbExp=3; IntAct=EBI-2556193, EBI-10251462;
CC Q63ZY3; Q8NCA9: ZNF784; NbExp=3; IntAct=EBI-2556193, EBI-7138303;
CC Q63ZY3; O43257: ZNHIT1; NbExp=3; IntAct=EBI-2556193, EBI-347522;
CC Q63ZY3; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-2556193, EBI-527853;
CC Q63ZY3-2; O95831: AIFM1; NbExp=4; IntAct=EBI-6244894, EBI-356440;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17476305,
CC ECO:0000269|PubMed:17996375, ECO:0000269|PubMed:22371500,
CC ECO:0000269|PubMed:25961457}. Mitochondrion
CC {ECO:0000269|PubMed:22371500}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q63ZY3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q63ZY3-2; Sequence=VSP_019427;
CC Name=3;
CC IsoId=Q63ZY3-3; Sequence=VSP_019428, VSP_019429;
CC -!- TISSUE SPECIFICITY: Strongly expressed in cervix, colon, heart, kidney
CC and lung. Expressed in kidney glomerular podocytes and mesangial cells
CC (at protein level). {ECO:0000269|PubMed:17996375,
CC ECO:0000269|PubMed:20720434}.
CC -!- PTM: Phosphorylated by casein kinase II upon estrogen stimulation
CC (PubMed:17476305). Phosphorylation induces the release by KANK2 of
CC NCOA1 and its translocation to the nucleus where NCOA1 can activate
CC gene transcription (PubMed:17476305). {ECO:0000269|PubMed:17476305}.
CC -!- DISEASE: Palmoplantar keratoderma and woolly hair (PPKWH) [MIM:616099]:
CC A disorder characterized by abnormal thickening of the skin on the
CC palms and soles, in association with woolly scalp hair. Affected
CC individuals manifest a variable degree of striate palmoplantar
CC keratoderma, generally more severe on the soles. Leukonychia is more
CC pronounced on the fingernails than toenails. Scalp hair, body hair,
CC eyebrows, and eyelashes are sparse. The fifth toes show variable
CC degrees of pseudoainhum, ranging from external rotation to a deep
CC sulcus at the digitoplantar fold, accompanied by a bulbous appearance
CC of the distal toe. {ECO:0000269|PubMed:24671081}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- DISEASE: Nephrotic syndrome 16 (NPHS16) [MIM:617783]: A form of
CC nephrotic syndrome, a renal disease clinically characterized by severe
CC proteinuria, resulting in complications such as hypoalbuminemia,
CC hyperlipidemia and edema. Kidney biopsies show non-specific histologic
CC changes such as focal segmental glomerulosclerosis and diffuse
CC mesangial proliferation. Some affected individuals have an inherited
CC steroid-resistant form that progresses to end-stage renal failure.
CC NPHS16 inheritance is autosomal recessive.
CC {ECO:0000269|PubMed:25961457}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA92081.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA96042.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB14531.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY639929; AAT57879.1; -; mRNA.
DR EMBL; AB284125; BAG06864.1; -; mRNA.
DR EMBL; AB040951; BAA96042.2; ALT_INIT; mRNA.
DR EMBL; CH471106; EAW84177.1; -; Genomic_DNA.
DR EMBL; BC082762; AAH82762.1; -; mRNA.
DR EMBL; BC098105; AAH98105.1; -; mRNA.
DR EMBL; BC098286; AAH98286.1; -; mRNA.
DR EMBL; BC098312; AAH98312.1; -; mRNA.
DR EMBL; BC105989; AAI05990.1; -; mRNA.
DR EMBL; AK002094; BAA92081.1; ALT_INIT; mRNA.
DR EMBL; AK023332; BAB14531.1; ALT_INIT; mRNA.
DR CCDS; CCDS12255.1; -. [Q63ZY3-1]
DR CCDS; CCDS54219.1; -. [Q63ZY3-2]
DR RefSeq; NP_001129663.1; NM_001136191.2. [Q63ZY3-1]
DR RefSeq; NP_001316380.1; NM_001329451.1. [Q63ZY3-1]
DR RefSeq; NP_056308.3; NM_015493.6. [Q63ZY3-2]
DR PDB; 4HBD; X-ray; 1.72 A; A=578-832.
DR PDB; 5YBV; X-ray; 2.12 A; A/B=578-832.
DR PDB; 6TMD; X-ray; 1.50 A; A=583-832.
DR PDBsum; 4HBD; -.
DR PDBsum; 5YBV; -.
DR PDBsum; 6TMD; -.
DR AlphaFoldDB; Q63ZY3; -.
DR SMR; Q63ZY3; -.
DR BioGRID; 117449; 291.
DR ELM; Q63ZY3; -.
DR IntAct; Q63ZY3; 237.
DR MINT; Q63ZY3; -.
DR STRING; 9606.ENSP00000468002; -.
DR GlyGen; Q63ZY3; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q63ZY3; -.
DR MetOSite; Q63ZY3; -.
DR PhosphoSitePlus; Q63ZY3; -.
DR BioMuta; KANK2; -.
DR DMDM; 74757262; -.
DR EPD; Q63ZY3; -.
DR jPOST; Q63ZY3; -.
DR MassIVE; Q63ZY3; -.
DR MaxQB; Q63ZY3; -.
DR PaxDb; Q63ZY3; -.
DR PeptideAtlas; Q63ZY3; -.
DR PRIDE; Q63ZY3; -.
DR ProteomicsDB; 65901; -. [Q63ZY3-1]
DR ProteomicsDB; 65902; -. [Q63ZY3-2]
DR ProteomicsDB; 65903; -. [Q63ZY3-3]
DR Antibodypedia; 2885; 199 antibodies from 28 providers.
DR DNASU; 25959; -.
DR Ensembl; ENST00000586659.6; ENSP00000465650.1; ENSG00000197256.11. [Q63ZY3-1]
DR Ensembl; ENST00000589359.5; ENSP00000468002.1; ENSG00000197256.11. [Q63ZY3-2]
DR Ensembl; ENST00000589894.1; ENSP00000467029.1; ENSG00000197256.11. [Q63ZY3-3]
DR GeneID; 25959; -.
DR KEGG; hsa:25959; -.
DR MANE-Select; ENST00000586659.6; ENSP00000465650.1; NM_001136191.3; NP_001129663.1.
DR UCSC; uc002mqo.5; human. [Q63ZY3-1]
DR CTD; 25959; -.
DR DisGeNET; 25959; -.
DR GeneCards; KANK2; -.
DR HGNC; HGNC:29300; KANK2.
DR HPA; ENSG00000197256; Low tissue specificity.
DR MalaCards; KANK2; -.
DR MIM; 614610; gene.
DR MIM; 616099; phenotype.
DR MIM; 617783; phenotype.
DR neXtProt; NX_Q63ZY3; -.
DR OpenTargets; ENSG00000197256; -.
DR Orphanet; 420686; Woolly hair-palmoplantar keratoderma syndrome.
DR PharmGKB; PA162392581; -.
DR VEuPathDB; HostDB:ENSG00000197256; -.
DR eggNOG; KOG0514; Eukaryota.
DR GeneTree; ENSGT00940000161012; -.
DR HOGENOM; CLU_004269_2_0_1; -.
DR InParanoid; Q63ZY3; -.
DR OMA; HQRSLQF; -.
DR OrthoDB; 98668at2759; -.
DR PhylomeDB; Q63ZY3; -.
DR TreeFam; TF324499; -.
DR PathwayCommons; Q63ZY3; -.
DR SignaLink; Q63ZY3; -.
DR BioGRID-ORCS; 25959; 14 hits in 1079 CRISPR screens.
DR ChiTaRS; KANK2; human.
DR GeneWiki; ANKRD25; -.
DR GenomeRNAi; 25959; -.
DR Pharos; Q63ZY3; Tbio.
DR PRO; PR:Q63ZY3; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q63ZY3; protein.
DR Bgee; ENSG00000197256; Expressed in saphenous vein and 194 other tissues.
DR ExpressionAtlas; Q63ZY3; baseline and differential.
DR Genevisible; Q63ZY3; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0072073; P:kidney epithelium development; IMP:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IDA:UniProtKB.
DR GO; GO:0033147; P:negative regulation of intracellular estrogen receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0043069; P:negative regulation of programmed cell death; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0070563; P:negative regulation of vitamin D receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0090521; P:podocyte cell migration; IMP:UniProtKB.
DR GO; GO:0035023; P:regulation of Rho protein signal transduction; IMP:UniProtKB.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR021939; KN_motif.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF12075; KN_motif; 1.
DR SMART; SM00248; ANK; 5.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ANK repeat; Apoptosis; Coiled coil;
KW Cytoplasm; Disease variant; Methylation; Mitochondrion;
KW Palmoplantar keratoderma; Phosphoprotein; Reference proteome; Repeat;
KW Transcription; Transcription regulation.
FT CHAIN 1..851
FT /note="KN motif and ankyrin repeat domain-containing
FT protein 2"
FT /id="PRO_0000240840"
FT REPEAT 614..651
FT /note="ANK 0; degenerate"
FT /evidence="ECO:0000269|PubMed:29183992"
FT REPEAT 666..696
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 700..733
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT REPEAT 738..767
FT /note="ANK 3"
FT /evidence="ECO:0000255"
FT REPEAT 771..801
FT /note="ANK 4"
FT /evidence="ECO:0000255"
FT REPEAT 805..835
FT /note="ANK 5"
FT /evidence="ECO:0000255"
FT REGION 1..72
FT /note="Interaction with AIFM1"
FT /evidence="ECO:0000269|PubMed:22371500"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 139..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 669..835
FT /note="Interaction with NCOA1"
FT /evidence="ECO:0000269|PubMed:17476305"
FT COILED 183..234
FT /evidence="ECO:0000255"
FT COILED 282..312
FT /evidence="ECO:0000255"
FT COMPBIAS 10..30
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..462
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..580
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BX02"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BX02"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BX02"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 105
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 168
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8BX02"
FT MOD_RES 323
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 329
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 356
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 375
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 472
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 540
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 552
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 472
FT /note="T -> TAPPLSSPP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17476305"
FT /id="VSP_019427"
FT VAR_SEQ 835..841
FT /note="FAPMSDD -> VSLNPAG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_019428"
FT VAR_SEQ 842..851
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_019429"
FT VARIANT 118
FT /note="G -> S (in dbSNP:rs755237)"
FT /id="VAR_048304"
FT VARIANT 181
FT /note="S -> G (in NPHS16; increased interaction with
FT ARHGDIA; loss of function in regulation of the Rho
FT signaling pathway; no effect on cytoplasmic localization;
FT loss of function in podocytes migration;
FT dbSNP:rs1555820663)"
FT /evidence="ECO:0000269|PubMed:25961457"
FT /id="VAR_080959"
FT VARIANT 401
FT /note="M -> T (in dbSNP:rs17616661)"
FT /id="VAR_048305"
FT VARIANT 670
FT /note="A -> V (in PPKWH; dbSNP:rs606231303)"
FT /evidence="ECO:0000269|PubMed:24671081"
FT /id="VAR_072431"
FT VARIANT 676
FT /note="S -> F (in NPHS16; loss of function in regulation of
FT the Rho signaling pathway; no effect on cytoplasmic
FT localization; decreased function in podocytes migration;
FT dbSNP:rs1555816634)"
FT /evidence="ECO:0000269|PubMed:25961457"
FT /id="VAR_080960"
FT MUTAGEN 510..512
FT /note="SSS->AAA: Impairs phosphorylation; when associated
FT with A-515."
FT /evidence="ECO:0000269|PubMed:17476305"
FT MUTAGEN 515
FT /note="S->A: Impairs phosphorylation; when associated with
FT 510-A--A-512."
FT /evidence="ECO:0000269|PubMed:17476305"
FT MUTAGEN 702
FT /note="Y->A: 4-fold decrease in binding to KIF21A."
FT /evidence="ECO:0000269|PubMed:29183992"
FT MUTAGEN 702
FT /note="Y->L: 33-fold decrease in binding to KIF21A."
FT /evidence="ECO:0000269|PubMed:29183992"
FT MUTAGEN 803
FT /note="D->A: 26-fold decrease in binding to KIF21A."
FT /evidence="ECO:0000269|PubMed:29183992"
FT MUTAGEN 805
FT /note="D->A: 20-fold decrease in binding to KIF21A."
FT /evidence="ECO:0000269|PubMed:29183992"
FT CONFLICT 525
FT /note="D -> N (in Ref. 3; BAA96042)"
FT /evidence="ECO:0000305"
FT HELIX 592..606
FT /evidence="ECO:0007829|PDB:6TMD"
FT HELIX 608..610
FT /evidence="ECO:0007829|PDB:5YBV"
FT HELIX 613..626
FT /evidence="ECO:0007829|PDB:6TMD"
FT HELIX 628..631
FT /evidence="ECO:0007829|PDB:6TMD"
FT STRAND 632..635
FT /evidence="ECO:0007829|PDB:5YBV"
FT HELIX 638..649
FT /evidence="ECO:0007829|PDB:6TMD"
FT HELIX 653..660
FT /evidence="ECO:0007829|PDB:6TMD"
FT HELIX 670..676
FT /evidence="ECO:0007829|PDB:6TMD"
FT HELIX 680..688
FT /evidence="ECO:0007829|PDB:6TMD"
FT HELIX 704..707
FT /evidence="ECO:0007829|PDB:6TMD"
FT HELIX 708..710
FT /evidence="ECO:0007829|PDB:6TMD"
FT HELIX 716..728
FT /evidence="ECO:0007829|PDB:6TMD"
FT TURN 736..739
FT /evidence="ECO:0007829|PDB:6TMD"
FT HELIX 742..748
FT /evidence="ECO:0007829|PDB:6TMD"
FT HELIX 752..760
FT /evidence="ECO:0007829|PDB:6TMD"
FT HELIX 775..782
FT /evidence="ECO:0007829|PDB:6TMD"
FT HELIX 785..792
FT /evidence="ECO:0007829|PDB:6TMD"
FT HELIX 809..815
FT /evidence="ECO:0007829|PDB:6TMD"
FT HELIX 819..828
FT /evidence="ECO:0007829|PDB:6TMD"
SQ SEQUENCE 851 AA; 91174 MW; C14CD8B937A7B6E8 CRC64;
MAQVLHVPAP FPGTPGPASP PAFPAKDPDP PYSVETPYGY RLDLDFLKYV DDIEKGHTLR
RVAVQRRPRL SSLPRGPGSW WTSTESLCSN ASGDSRHSAY SYCGRGFYPQ YGALETRGGF
NPRVERTLLD ARRRLEDQAA TPTGLGSLTP SAAGSTASLV GVGLPPPTPR SSGLSTPVPP
SAGHLAHVRE QMAGALRKLR QLEEQVKLIP VLQVKLSVLQ EEKRQLTVQL KSQKFLGHPT
AGRGRSELCL DLPDPPEDPV ALETRSVGTW VRERDLGMPD GEAALAAKVA VLETQLKKAL
QELQAAQARQ ADPQPQAWPP PDSPVRVDTV RVVEGPREVE VVASTAAGAP AQRAQSLEPY
GTGLRALAMP GRPESPPVFR SQEVVETMCP VPAAATSNVH MVKKISITER SCDGAAGLPE
VPAESSSSPP GSEVASLTQP EKSTGRVPTQ EPTHREPTRQ AASQESEEAG GTGGPPAGVR
SIMKRKEEVA DPTAHRRSLQ FVGVNGGYES SSEDSSTAEN ISDNDSTENE APEPRERVPS
VAEAPQLRPA GTAAAKTSRQ ECQLSRESQH IPTAEGASGS NTEEEIRMEL SPDLISACLA
LEKYLDNPNA LTERELKVAY TTVLQEWLRL ACRSDAHPEL VRRHLVTFRA MSARLLDYVV
NIADSNGNTA LHYSVSHANF PVVQQLLDSG VCKVDKQNRA GYSPIMLTAL ATLKTQDDIE
TVLQLFRLGN INAKASQAGQ TALMLAVSHG RVDVVKALLA CEADVNVQDD DGSTALMCAC
EHGHKEIAGL LLAVPSCDIS LTDRDGSTAL MVALDAGQSE IASMLYSRMN IKCSFAPMSD
DESPTSSSAE E
