KANK3_HUMAN
ID KANK3_HUMAN Reviewed; 821 AA.
AC Q6NY19; Q6NZI1; Q6ZQR3; Q8IUV2;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 29-SEP-2021, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=KN motif and ankyrin repeat domain-containing protein 3 {ECO:0000305};
DE AltName: Full=Ankyrin repeat domain-containing protein 47;
GN Name=KANK3 {ECO:0000312|HGNC:HGNC:24796}; Synonyms=ANKRD47;
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 2), AND VARIANTS TYR-288
RP AND THR-485.
RC TISSUE=Mammary gland;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Placenta;
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 [3]
RP POSSIBLE FUNCTION, 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152; SER-167; SER-168;
RP SER-177; SER-271 AND SER-293, 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).
CC -!- FUNCTION: May be involved in the control of cytoskeleton formation by
CC regulating actin polymerization.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=2;
CC IsoId=Q6NY19-2; Sequence=Displayed;
CC Name=1;
CC IsoId=Q6NY19-1; Sequence=VSP_061119;
CC -!- TISSUE SPECIFICITY: Strongly expressed in breast, liver, lung, skeletal
CC muscle and kidney. {ECO:0000269|PubMed:17996375}.
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DR EMBL; AK128815; BAC87620.1; -; mRNA.
DR EMBL; BC035849; AAH35849.1; -; mRNA.
DR EMBL; BC066124; AAH66124.1; -; mRNA.
DR EMBL; BC066775; AAH66775.1; -; mRNA.
DR CCDS; CCDS12199.1; -. [Q6NY19-2]
DR RefSeq; NP_940873.2; NM_198471.2. [Q6NY19-2]
DR RefSeq; XP_006722781.1; XM_006722718.3. [Q6NY19-2]
DR RefSeq; XP_011526186.1; XM_011527884.2. [Q6NY19-2]
DR AlphaFoldDB; Q6NY19; -.
DR SMR; Q6NY19; -.
DR BioGRID; 129185; 5.
DR IntAct; Q6NY19; 1.
DR STRING; 9606.ENSP00000328923; -.
DR iPTMnet; Q6NY19; -.
DR PhosphoSitePlus; Q6NY19; -.
DR BioMuta; KANK3; -.
DR DMDM; 74749039; -.
DR EPD; Q6NY19; -.
DR jPOST; Q6NY19; -.
DR MassIVE; Q6NY19; -.
DR PaxDb; Q6NY19; -.
DR PeptideAtlas; Q6NY19; -.
DR PRIDE; Q6NY19; -.
DR ProteomicsDB; 66779; -. [Q6NY19-1]
DR ProteomicsDB; 66780; -. [Q6NY19-2]
DR Antibodypedia; 42728; 56 antibodies from 17 providers.
DR DNASU; 256949; -.
DR Ensembl; ENST00000330915.7; ENSP00000328923.2; ENSG00000186994.12. [Q6NY19-2]
DR Ensembl; ENST00000593649.5; ENSP00000470728.1; ENSG00000186994.12. [Q6NY19-1]
DR GeneID; 256949; -.
DR KEGG; hsa:256949; -.
DR MANE-Select; ENST00000330915.7; ENSP00000328923.2; NM_198471.3; NP_940873.2.
DR UCSC; uc010dwa.3; human. [Q6NY19-2]
DR CTD; 256949; -.
DR DisGeNET; 256949; -.
DR GeneCards; KANK3; -.
DR HGNC; HGNC:24796; KANK3.
DR HPA; ENSG00000186994; Low tissue specificity.
DR MIM; 614611; gene.
DR neXtProt; NX_Q6NY19; -.
DR OpenTargets; ENSG00000186994; -.
DR PharmGKB; PA162392612; -.
DR VEuPathDB; HostDB:ENSG00000186994; -.
DR eggNOG; KOG0514; Eukaryota.
DR GeneTree; ENSGT00940000161178; -.
DR HOGENOM; CLU_004269_2_0_1; -.
DR InParanoid; Q6NY19; -.
DR OMA; SDAWVTE; -.
DR OrthoDB; 98668at2759; -.
DR PhylomeDB; Q6NY19; -.
DR TreeFam; TF324499; -.
DR PathwayCommons; Q6NY19; -.
DR SignaLink; Q6NY19; -.
DR BioGRID-ORCS; 256949; 13 hits in 1070 CRISPR screens.
DR ChiTaRS; KANK3; human.
DR GenomeRNAi; 256949; -.
DR Pharos; Q6NY19; Tdark.
DR PRO; PR:Q6NY19; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q6NY19; protein.
DR Bgee; ENSG00000186994; Expressed in vena cava and 165 other tissues.
DR ExpressionAtlas; Q6NY19; baseline and differential.
DR Genevisible; Q6NY19; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0030837; P:negative regulation of actin filament polymerization; IBA:GO_Central.
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; 1.
DR Pfam; PF13857; Ank_5; 1.
DR Pfam; PF12075; KN_motif; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 4.
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 Alternative splicing; ANK repeat; Coiled coil; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..821
FT /note="KN motif and ankyrin repeat domain-containing
FT protein 3"
FT /id="PRO_0000244582"
FT REPEAT 622..652
FT /note="ANK 1"
FT REPEAT 656..690
FT /note="ANK 2"
FT REPEAT 695..724
FT /note="ANK 3"
FT REPEAT 728..758
FT /note="ANK 4"
FT REPEAT 762..785
FT /note="ANK 5"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 58..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 784..821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 181..230
FT /evidence="ECO:0000255"
FT COILED 367..404
FT /evidence="ECO:0000255"
FT COMPBIAS 128..146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..266
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 787..808
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 152
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1P7"
FT MOD_RES 164
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1P7"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 168
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 271
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1P7"
FT MOD_RES 293
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 795..821
FT /note="SESPPGSQTATPGEGECGDNGENPQVQ -> AGVQRHNLSSLQPPPPRFKKF
FT SCLSLPSSWDYNSCEPSRLAQLTIF (in isoform 1)"
FT /id="VSP_061119"
FT VARIANT 288
FT /note="D -> Y (in dbSNP:rs890850)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_026909"
FT VARIANT 359
FT /note="R -> H (in dbSNP:rs890853)"
FT /id="VAR_026910"
FT VARIANT 485
FT /note="A -> T (in dbSNP:rs2913955)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_026911"
SQ SEQUENCE 821 AA; 85893 MW; 66CCB7F5B1B251F5 CRC64;
MAKFALNQNL PDLGGPRLCP VPAAGGARSP SSPYSVETPY GFHLDLDFLK YIEELERGPA
ARRAPGPPTS RRPRAPRPGL AGARSPGAWT SSESLASDDG GAPGILSQGA PSGLLMQPLS
PRAPVRNPRV EHTLRETSRR LELAQTHERA PSPGRGVPRS PRGSGRSSPA PNLAPASPGP
AQLQLVREQM AAALRRLREL EDQARTLPEL QEQVRALRAE KARLLAGRAQ PEPDGEAETR
PDKLAQLRRL TERLATSERG GRARASPRAD SPDGLAAGRS EGALQVLDGE VGSLDGTPQT
REVAAEAVPE TREAGAQAVP ETREAGVEAA PETVEADAWV TEALLGLPAA AERELELLRA
SLEHQRGVSE LLRGRLRELE EAREAAEEAA AGARAQLREA TTQTPWSCAE KAAQTESPAE
APSLTQESSP GSMDGDRAVA PAGILKSIMK KRDGTPGAQP SSGPKSLQFV GVLNGEYESS
SSEDASDSDG DSENGGAEPP GSSSGSGDDS GGGSDSGTPG PPSGGDIRDP EPEAEAEPQQ
VAQGRCELSP RLREACVALQ RQLSRPRGVA SDGGAVRLVA QEWFRVSSQR RSQAEPVARM
LEGVRRLGPE LLAHVVNLAD GNGNTALHYS VSHGNLAIAS LLLDTGACEV NRQNRAGYSA
LMLAALTSVR QEEEDMAVVQ RLFCMGDVNA KASQTGQTAL MLAISHGRQD MVATLLACGA
DVNAQDADGA TALMCASEYG RLDTVRLLLT QPGCDPAILD NEGTSALAIA LEAEQDEVAA
LLHAHLSSGQ PDTQSESPPG SQTATPGEGE CGDNGENPQV Q
