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 27-MAR-2024, entry version 210. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 44. 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; 9606-ENSP00000379368; -. DR PeptideAtlas; P13682; -. DR ProteomicsDB; 52959; -. DR Pumba; P13682; -. DR Antibodypedia; 12518; 262 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 AGR; HGNC:13099; -. 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; 4711909at2759; -. DR PhylomeDB; P13682; -. DR TreeFam; TF350849; -. DR PathwayCommons; P13682; -. DR SignaLink; P13682; -. DR BioGRID-ORCS; 7584; 10 hits in 1177 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 male germ line stem cell (sensu Vertebrata) in testis and 104 other cell types or tissues. DR ExpressionAtlas; P13682; baseline and differential. 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:0006355; P:regulation of DNA-templated transcription; TAS:ProtInc. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 11. DR InterPro; IPR036236; Znf_C2H2_sf. DR InterPro; IPR013087; Znf_C2H2_type. DR PANTHER; PTHR24393:SF168; FI01120P-RELATED; 1. DR PANTHER; PTHR24393; ZINC FINGER PROTEIN; 1. DR Pfam; PF00096; zf-C2H2; 11. DR SMART; SM00355; ZnF_C2H2; 11. DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 6. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 11. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 11. DR Genevisible; P13682; HS. 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 //