ANKZ1_HUMAN
ID ANKZ1_HUMAN Reviewed; 726 AA.
AC Q9H8Y5; Q9NVZ4;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Ankyrin repeat and zinc finger domain-containing protein 1;
DE AltName: Full=Zinc finger protein 744;
GN Name=ANKZF1; Synonyms=ZNF744;
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].
RA Zhao Y., Li Y., Yuan W., Wu X., Liu M.;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon, and Eye;
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 [4]
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-675, AND IDENTIFICATION BY
RP 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 [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258; SER-398; SER-533 AND
RP THR-607, AND IDENTIFICATION BY 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 [10]
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 [11]
RP INTERACTION WITH VCP, VIM MOTI, AND MUTAGENESIS OF 661-ARG-ARG-662.
RX PubMed=21896481; DOI=10.1074/jbc.m111.274472;
RA Stapf C., Cartwright E., Bycroft M., Hofmann K., Buchberger A.;
RT "The general definition of the p97/valosin-containing protein (VCP)-
RT interacting motif (VIM) delineates a new family of p97 cofactors.";
RL J. Biol. Chem. 286:38670-38678(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-398, AND IDENTIFICATION BY
RP 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-361; SER-533; THR-607;
RP SER-675 AND SER-680, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [14]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH VPC, VARIANTS
RP 32-VAL--GLN-87 DEL; LYS-152; GLN-585 AND PRO-638, AND CHARACTERIZATION OF
RP VARIANTS LYS-152 AND GLN-585.
RX PubMed=28302725; DOI=10.1074/jbc.m116.772038;
RA van Haaften-Visser D.Y., Harakalova M., Mocholi E., van Montfrans J.M.,
RA Elkadri A., Rieter E., Fiedler K., van Hasselt P.M., Triffaux E.M.M.,
RA van Haelst M.M., Nijman I.J., Kloosterman W.P., Nieuwenhuis E.E.S.,
RA Muise A.M., Cuppen E., Houwen R.H.J., Coffer P.J.;
RT "Ankyrin repeat and zinc-finger domain-containing 1 mutations are
RT associated with infantile-onset inflammatory bowel disease.";
RL J. Biol. Chem. 292:7904-7920(2017).
CC -!- FUNCTION: Plays a role in the cellular response to hydrogen peroxide
CC and in the maintenance of mitochondrial integrity under conditions of
CC cellular stress (PubMed:28302725). Involved in the endoplasmic
CC reticulum (ER)-associated degradation (ERAD) pathway (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:28302725}.
CC -!- SUBUNIT: Interacts (via VIM motif) with VCP.
CC {ECO:0000269|PubMed:21896481, ECO:0000269|PubMed:28302725}.
CC -!- INTERACTION:
CC Q9H8Y5; Q9Q2G4: ORF; Xeno; NbExp=2; IntAct=EBI-724848, EBI-6248094;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:28302725}.
CC Note=Translocates to the mitochondria upon exposure to hydrogen
CC peroxide. {ECO:0000269|PubMed:28302725}.
CC -!- SIMILARITY: Belongs to the ANKZF1/VMS1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABD65410.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAA91596.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; DQ412564; ABD65410.1; ALT_FRAME; mRNA.
DR EMBL; AK001277; BAA91596.1; ALT_FRAME; mRNA.
DR EMBL; AK023206; BAB14462.1; -; mRNA.
DR EMBL; BC000238; AAH00238.1; -; mRNA.
DR EMBL; BC008948; AAH08948.1; -; mRNA.
DR CCDS; CCDS42821.1; -.
DR RefSeq; NP_001035869.1; NM_001042410.1.
DR RefSeq; NP_060559.2; NM_018089.2.
DR AlphaFoldDB; Q9H8Y5; -.
DR BioGRID; 120443; 23.
DR IntAct; Q9H8Y5; 13.
DR MINT; Q9H8Y5; -.
DR STRING; 9606.ENSP00000321617; -.
DR GlyGen; Q9H8Y5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9H8Y5; -.
DR MetOSite; Q9H8Y5; -.
DR PhosphoSitePlus; Q9H8Y5; -.
DR SwissPalm; Q9H8Y5; -.
DR BioMuta; ANKZF1; -.
DR DMDM; 74761542; -.
DR EPD; Q9H8Y5; -.
DR jPOST; Q9H8Y5; -.
DR MassIVE; Q9H8Y5; -.
DR MaxQB; Q9H8Y5; -.
DR PaxDb; Q9H8Y5; -.
DR PeptideAtlas; Q9H8Y5; -.
DR PRIDE; Q9H8Y5; -.
DR ProteomicsDB; 81256; -.
DR ABCD; Q9H8Y5; 5 sequenced antibodies.
DR Antibodypedia; 34312; 138 antibodies from 26 providers.
DR DNASU; 55139; -.
DR Ensembl; ENST00000323348.10; ENSP00000321617.5; ENSG00000163516.14.
DR Ensembl; ENST00000410034.7; ENSP00000386337.3; ENSG00000163516.14.
DR GeneID; 55139; -.
DR KEGG; hsa:55139; -.
DR MANE-Select; ENST00000323348.10; ENSP00000321617.5; NM_018089.3; NP_060559.2.
DR UCSC; uc002vkg.3; human.
DR CTD; 55139; -.
DR DisGeNET; 55139; -.
DR GeneCards; ANKZF1; -.
DR HGNC; HGNC:25527; ANKZF1.
DR HPA; ENSG00000163516; Low tissue specificity.
DR MIM; 617541; gene.
DR neXtProt; NX_Q9H8Y5; -.
DR OpenTargets; ENSG00000163516; -.
DR PharmGKB; PA143485305; -.
DR VEuPathDB; HostDB:ENSG00000163516; -.
DR eggNOG; KOG2505; Eukaryota.
DR GeneTree; ENSGT00390000005911; -.
DR InParanoid; Q9H8Y5; -.
DR OMA; GESKWDW; -.
DR OrthoDB; 1495271at2759; -.
DR PhylomeDB; Q9H8Y5; -.
DR TreeFam; TF313431; -.
DR BRENDA; 3.1.1.29; 2681.
DR PathwayCommons; Q9H8Y5; -.
DR SignaLink; Q9H8Y5; -.
DR BioGRID-ORCS; 55139; 13 hits in 1079 CRISPR screens.
DR ChiTaRS; ANKZF1; human.
DR GeneWiki; ANKZF1; -.
DR GenomeRNAi; 55139; -.
DR Pharos; Q9H8Y5; Tbio.
DR PRO; PR:Q9H8Y5; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9H8Y5; protein.
DR Bgee; ENSG00000163516; Expressed in right uterine tube and 134 other tissues.
DR ExpressionAtlas; Q9H8Y5; baseline and differential.
DR Genevisible; Q9H8Y5; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IMP:UniProtKB.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR041540; VATC.
DR InterPro; IPR041175; VLRF1/Vms1.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF18826; bVLRF1; 1.
DR Pfam; PF18716; VATC; 1.
DR SMART; SM00248; ANK; 2.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 1: Evidence at protein level;
KW ANK repeat; Coiled coil; Cytoplasm; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..726
FT /note="Ankyrin repeat and zinc finger domain-containing
FT protein 1"
FT /id="PRO_0000247278"
FT REPEAT 493..526
FT /note="ANK 1"
FT REPEAT 534..563
FT /note="ANK 2"
FT ZN_FING 72..96
FT /note="C2H2-type"
FT REGION 40..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 120..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 436..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 588..656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 654..666
FT /note="VCP/p97-interacting motif (VIM)"
FT /evidence="ECO:0000269|PubMed:21896481"
FT COILED 609..659
FT /evidence="ECO:0000255"
FT COMPBIAS 454..474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..656
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 258
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 361
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 398
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 533
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 607
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 675
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 680
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 32..87
FT /note="Missing (found in a patient with infantile-onset
FT inflammatory bowel disease; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:28302725"
FT /id="VAR_079136"
FT VARIANT 152
FT /note="E -> K (found in a patient with infantile-onset
FT inflammatory bowel disease; unknown pathological
FT significance; decreased function in cellular response to
FT hydrogen peroxide; does not affect protein abundance; does
FT not affect interaction with VCP; dbSNP:rs149382949)"
FT /evidence="ECO:0000269|PubMed:28302725"
FT /id="VAR_079137"
FT VARIANT 569
FT /note="R -> W (in dbSNP:rs2293076)"
FT /id="VAR_048269"
FT VARIANT 585
FT /note="R -> Q (found in a patient with infantile-onset
FT inflammatory bowel disease; unknown pathological
FT significance; decreased function in cellular response to
FT hydrogen peroxide; decreased protein abundance; does not
FT affect interaction with VCP; dbSNP:rs189875478)"
FT /evidence="ECO:0000269|PubMed:28302725"
FT /id="VAR_079138"
FT VARIANT 638
FT /note="Q -> P"
FT /evidence="ECO:0000269|PubMed:28302725"
FT /id="VAR_079139"
FT VARIANT 676
FT /note="P -> L (in dbSNP:rs2293079)"
FT /id="VAR_048270"
FT MUTAGEN 661..662
FT /note="AA->LL: Abolishes interaction with VCP."
FT /evidence="ECO:0000269|PubMed:21896481"
SQ SEQUENCE 726 AA; 80927 MW; 44F7930A530F1355 CRC64;
MSPAPDAAPA PASISLFDLS ADAPVFQGLS LVSHAPGEAL ARAPRTSCSG SGERESPERK
LLQGPMDISE KLFCSTCDQT FQNHQEQREH YKLDWHRFNL KQRLKDKPLL SALDFEKQSS
TGDLSSISGS EDSDSASEED LQTLDRERAT FEKLSRPPGF YPHRVLFQNA QGQFLYAYRC
VLGPHQDPPE EAELLLQNLQ SRGPRDCVVL MAAAGHFAGA IFQGREVVTH KTFHRYTVRA
KRGTAQGLRD ARGGPSHSAG ANLRRYNEAT LYKDVRDLLA GPSWAKALEE AGTILLRAPR
SGRSLFFGGK GAPLQRGDPR LWDIPLATRR PTFQELQRVL HKLTTLHVYE EDPREAVRLH
SPQTHWKTVR EERKKPTEEE IRKICRDEKE ALGQNEESPK QGSGSEGEDG FQVELELVEL
TVGTLDLCES EVLPKRRRRK RNKKEKSRDQ EAGAHRTLLQ QTQEEEPSTQ SSQAVAAPLG
PLLDEAKAPG QPELWNALLA ACRAGDVGVL KLQLAPSPAD PRVLSLLSAP LGSGGFTLLH
AAAAAGRGSV VRLLLEAGAD PTVQDSRARP PYTVAADKST RNEFRRFMEK NPDAYDYNKA
QVPGPLTPEM EARQATRKRE QKAARRQREE QQQRQQEQEE REREEQRRFA ALSDREKRAL
AAERRLAAQL GAPTSPIPDS AIVNTRRCWS CGASLQGLTP FHYLDFSFCS TRCLQDHRRQ
AGRPSS
