ZNF35_HUMAN
ID ZNF35_HUMAN Reviewed; 527 AA.
AC P13682; B2RBU6; Q53Y54; Q96D01;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 4.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Zinc finger protein 35;
DE AltName: Full=Zinc finger protein HF.10;
GN Name=ZNF35;
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].
RC TISSUE=Placenta;
RX PubMed=3380682; DOI=10.1093/nar/16.10.4227;
RA Pannuti A., Lanfrancone L., Pascucci A., Pelicci P.-G., la Mantia G.,
RA Lania L.;
RT "Isolation of cDNAs encoding finger proteins and measurement of the
RT corresponding mRNA levels during myeloid terminal differentiation.";
RL Nucleic Acids Res. 16:4227-4237(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1572646; DOI=10.1016/0888-7543(92)90301-8;
RA Lanfrancone L., Pengue G., Pandolfi P.P., Salcini A.E., Giacomucci A.,
RA Longo L., Donti E., de Luca P., la Mantia G., Pelicci P.-G., Lania L.;
RT "Structural and functional organization of the HF.10 human zinc finger gene
RT (ZNF35) located on chromosome 3p21-p22.";
RL Genomics 12:720-728(1992).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 9-527.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-20; LYS-21; LYS-99; LYS-117;
RP LYS-125; LYS-144; LYS-158; LYS-189; LYS-214 AND LYS-276, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: May be involved in transcriptional regulation. Involved in
CC cell differentiation and/or proliferation.
CC -!- INTERACTION:
CC P13682; Q8N5M1: ATPAF2; NbExp=3; IntAct=EBI-11041653, EBI-1166928;
CC P13682; Q01850: CDR2; NbExp=3; IntAct=EBI-11041653, EBI-1181367;
CC P13682; Q86X02: CDR2L; NbExp=3; IntAct=EBI-11041653, EBI-11063830;
CC P13682; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-11041653, EBI-739624;
CC P13682; Q2TBE0: CWF19L2; NbExp=3; IntAct=EBI-11041653, EBI-5453285;
CC P13682; Q96G04: EEF2KMT; NbExp=3; IntAct=EBI-11041653, EBI-747840;
CC P13682; Q8IYI6: EXOC8; NbExp=3; IntAct=EBI-11041653, EBI-742102;
CC P13682; A1L4K1: FSD2; NbExp=3; IntAct=EBI-11041653, EBI-5661036;
CC P13682; P57678: GEMIN4; NbExp=3; IntAct=EBI-11041653, EBI-356700;
CC P13682; Q08379: GOLGA2; NbExp=3; IntAct=EBI-11041653, EBI-618309;
CC P13682; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-11041653, EBI-5916454;
CC P13682; Q4V328: GRIPAP1; NbExp=3; IntAct=EBI-11041653, EBI-717919;
CC P13682; Q9NSC5: HOMER3; NbExp=3; IntAct=EBI-11041653, EBI-748420;
CC P13682; Q9UJC3: HOOK1; NbExp=3; IntAct=EBI-11041653, EBI-746704;
CC P13682; Q96ED9-2: HOOK2; NbExp=3; IntAct=EBI-11041653, EBI-10961706;
CC P13682; Q9Y250: LZTS1; NbExp=3; IntAct=EBI-11041653, EBI-1216080;
CC P13682; Q9NYL2-2: MAP3K20; NbExp=3; IntAct=EBI-11041653, EBI-10255081;
CC P13682; P23508: MCC; NbExp=3; IntAct=EBI-11041653, EBI-307531;
CC P13682; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-11041653, EBI-11522433;
CC P13682; Q99836: MYD88; NbExp=3; IntAct=EBI-11041653, EBI-447677;
CC P13682; Q9GZM8: NDEL1; NbExp=3; IntAct=EBI-11041653, EBI-928842;
CC P13682; Q4G0R1: PIBF1; NbExp=3; IntAct=EBI-11041653, EBI-14066006;
CC P13682; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-11041653, EBI-79165;
CC P13682; Q8ND90: PNMA1; NbExp=3; IntAct=EBI-11041653, EBI-302345;
CC P13682; P31321: PRKAR1B; NbExp=3; IntAct=EBI-11041653, EBI-2805516;
CC P13682; Q12933: TRAF2; NbExp=3; IntAct=EBI-11041653, EBI-355744;
CC P13682; P13994: YJU2B; NbExp=3; IntAct=EBI-11041653, EBI-716093;
CC P13682; Q96BR9: ZBTB8A; NbExp=3; IntAct=EBI-11041653, EBI-742740;
CC P13682; Q8N5A5-2: ZGPAT; NbExp=3; IntAct=EBI-11041653, EBI-10183064;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA85451.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAG37343.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA30268.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X07289; CAA30268.1; ALT_INIT; mRNA.
DR EMBL; L35269; AAA85451.1; ALT_INIT; Genomic_DNA.
DR EMBL; M76702; AAA85451.1; JOINED; Genomic_DNA.
DR EMBL; M76703; AAA85451.1; JOINED; Genomic_DNA.
DR EMBL; AK314821; BAG37343.1; ALT_INIT; mRNA.
DR EMBL; AC099669; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC013597; AAH13597.2; -; mRNA.
DR EMBL; BT006962; AAP35608.1; -; mRNA.
DR CCDS; CCDS2718.2; -.
DR PIR; A38073; A38073.
DR RefSeq; NP_003411.3; NM_003420.3.
DR RefSeq; XP_016862618.1; XM_017007129.1.
DR RefSeq; XP_016862619.1; XM_017007130.1.
DR RefSeq; XP_016862620.1; XM_017007131.1.
DR AlphaFoldDB; P13682; -.
DR SMR; P13682; -.
DR BioGRID; 113412; 43.
DR IntAct; P13682; 38.
DR STRING; 9606.ENSP00000379368; -.
DR iPTMnet; P13682; -.
DR PhosphoSitePlus; P13682; -.
DR BioMuta; ZNF35; -.
DR DMDM; 300669709; -.
DR EPD; P13682; -.
DR jPOST; P13682; -.
DR MassIVE; P13682; -.
DR MaxQB; P13682; -.
DR PaxDb; P13682; -.
DR PeptideAtlas; P13682; -.
DR PRIDE; P13682; -.
DR ProteomicsDB; 52959; -.
DR Antibodypedia; 12518; 227 antibodies from 23 providers.
DR DNASU; 7584; -.
DR Ensembl; ENST00000396056.7; ENSP00000379368.2; ENSG00000169981.11.
DR Ensembl; ENST00000625394.3; ENSP00000486354.1; ENSG00000281306.3.
DR GeneID; 7584; -.
DR KEGG; hsa:7584; -.
DR MANE-Select; ENST00000396056.7; ENSP00000379368.2; NM_003420.4; NP_003411.3.
DR UCSC; uc003cnq.4; human.
DR CTD; 7584; -.
DR DisGeNET; 7584; -.
DR GeneCards; ZNF35; -.
DR HGNC; HGNC:13099; ZNF35.
DR HPA; ENSG00000169981; Low tissue specificity.
DR MIM; 194533; gene.
DR neXtProt; NX_P13682; -.
DR OpenTargets; ENSG00000169981; -.
DR PharmGKB; PA37674; -.
DR VEuPathDB; HostDB:ENSG00000169981; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162289; -.
DR HOGENOM; CLU_002678_47_0_1; -.
DR InParanoid; P13682; -.
DR OMA; VNDCHLP; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; P13682; -.
DR TreeFam; TF350849; -.
DR PathwayCommons; P13682; -.
DR SignaLink; P13682; -.
DR BioGRID-ORCS; 7584; 10 hits in 1099 CRISPR screens.
DR ChiTaRS; ZNF35; human.
DR GeneWiki; ZNF35; -.
DR GenomeRNAi; 7584; -.
DR Pharos; P13682; Tbio.
DR PRO; PR:P13682; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P13682; protein.
DR Bgee; ENSG00000169981; Expressed in corpus callosum and 103 other tissues.
DR ExpressionAtlas; P13682; baseline and differential.
DR Genevisible; P13682; HS.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0071300; P:cellular response to retinoic acid; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:ProtInc.
DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 11.
DR SMART; SM00355; ZnF_C2H2; 11.
DR SUPFAM; SSF57667; SSF57667; 6.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 11.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 11.
PE 1: Evidence at protein level;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..527
FT /note="Zinc finger protein 35"
FT /id="PRO_0000047366"
FT ZN_FING 222..244
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 250..272
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 278..300
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 306..328
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 334..356
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 362..384
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 390..412
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 418..440
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 446..468
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 474..496
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 502..524
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 9..221
FT /note="Globular domain"
FT REGION 16..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 20
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 21
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 99
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 117
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 125
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 144
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 158
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 189
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 214
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 276
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CONFLICT 413..440
FT /note="Missing (in Ref. 1; CAA30268)"
FT /evidence="ECO:0000305"
FT CONFLICT 432
FT /note="C -> S (in Ref. 2; AAA85451)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 527 AA; 59089 MW; 9E7099A290ED938B CRC64;
MTAELREAMA LAPWGPVKVK KEEEEEENFP GQASSQQVHS ENIKVWAPVQ GLQTGLDGSE
EEEKGQNISW DMAVVLKATQ EAPAASTLGS YSLPGTLAKS EILETHGTMN FLGAETKNLQ
LLVPKTEICE EAEKPLIISE RIQKADPQGP ELGEACEKGN MLKRQRIKRE KKDFRQVIVN
DCHLPESFKE EENQKCKKSG GKYSLNSGAV KNPKTQLGQK PFTCSVCGKG FSQSANLVVH
QRIHTGEKPF ECHECGKAFI QSANLVVHQR IHTGQKPYVC SKCGKAFTQS SNLTVHQKIH
SLEKTFKCNE CEKAFSYSSQ LARHQKVHIT EKCYECNECG KTFTRSSNLI VHQRIHTGEK
PFACNDCGKA FTQSANLIVH QRSHTGEKPY ECKECGKAFS CFSHLIVHQR IHTAEKPYDC
SECGKAFSQL SCLIVHQRIH SGDLPYVCNE CGKAFTCSSY LLIHQRIHNG EKPYTCNECG
KAFRQRSSLT VHQRTHTGEK PYECEKCGAA FISNSHLMRH HRTHLVE
