ZN335_HUMAN
ID ZN335_HUMAN Reviewed; 1342 AA.
AC Q9H4Z2; B4DLG7; Q548D0; Q9H684;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Zinc finger protein 335;
DE AltName: Full=NRC-interacting factor 1;
DE Short=NIF-1;
GN Name=ZNF335;
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 1), FUNCTION, SUBCELLULAR LOCATION,
RP INTERACTION WITH NCOA6, AND TISSUE SPECIFICITY.
RC TISSUE=Teratocarcinoma;
RX PubMed=12215545; DOI=10.1128/mcb.22.19.6883-6894.2002;
RA Mahajan M.A., Murray A., Samuels H.H.;
RT "NRC-interacting factor 1 is a novel cotransducer that interacts with and
RT regulates the activity of the nuclear hormone receptor coactivator NRC.";
RL Mol. Cell. Biol. 22:6883-6894(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT THR-294.
RC TISSUE=Kidney epithelium, and Tongue;
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 GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [4]
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 [5]
RP FUNCTION, AND INTERACTION WITH CNOT6 AND CNOT9.
RX PubMed=18180299; DOI=10.1074/jbc.m706986200;
RA Garapaty S., Mahajan M.A., Samuels H.H.;
RT "Components of the CCR4-NOT complex function as nuclear hormone receptor
RT coactivators via association with the NRC-interacting Factor NIF-1.";
RL J. Biol. Chem. 283:6806-6816(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1153, 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 [7]
RP FUNCTION, IDENTIFICATION IN A NUCLEAR RECEPTOR HORMONE COMPLEX,
RP IDENTIFICATION IN A HISTONE METHYLATION COMPLEX, AND INTERACTION WITH
RP CCAR2; EMSY; RBBP5; ASH2L; WDR5; HCFC1 AND MKI67.
RX PubMed=19131338; DOI=10.1074/jbc.m805872200;
RA Garapaty S., Xu C.F., Trojer P., Mahajan M.A., Neubert T.A., Samuels H.H.;
RT "Identification and characterization of a novel nuclear protein complex
RT involved in nuclear hormone receptor-mediated gene regulation.";
RL J. Biol. Chem. 284:7542-7552(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-992 AND SER-1007, 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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [10]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1022, AND IDENTIFICATION BY MASS
RP 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).
RN [11]
RP VARIANT MCPH10 HIS-1111, CHARACTERIZATION OF VARIANT MCPH10 HIS-1111,
RP FUNCTION IN NEUROGENESIS, INTERACTION WITH ASCL2; CXXC1; KMT2A/MLL1; MKI67;
RP RBBP5; SETD1A AND WDR5, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=23178126; DOI=10.1016/j.cell.2012.10.043;
RA Yang Y.J., Baltus A.E., Mathew R.S., Murphy E.A., Evrony G.D.,
RA Gonzalez D.M., Wang E.P., Marshall-Walker C.A., Barry B.J., Murn J.,
RA Tatarakis A., Mahajan M.A., Samuels H.H., Shi Y., Golden J.A., Mahajnah M.,
RA Shenhav R., Walsh C.A.;
RT "Microcephaly gene links trithorax and REST/NRSF to control neural stem
RT cell proliferation and differentiation.";
RL Cell 151:1097-1112(2012).
CC -!- FUNCTION: Component or associated component of some histone
CC methyltransferase complexes may regulate transcription through
CC recruitment of those complexes on gene promoters (PubMed:19131338,
CC PubMed:23178126). Enhances ligand-dependent transcriptional activation
CC by nuclear hormone receptors (PubMed:12215545, PubMed:18180299,
CC PubMed:19131338). Plays an important role in neural progenitor cell
CC proliferation and self-renewal through the regulation of specific genes
CC involved brain development, including REST (PubMed:23178126). Also
CC controls the expression of genes involved in somatic development and
CC regulates, for instance, lymphoblast proliferation (PubMed:23178126).
CC {ECO:0000269|PubMed:12215545, ECO:0000269|PubMed:18180299,
CC ECO:0000269|PubMed:19131338, ECO:0000269|PubMed:23178126}.
CC -!- SUBUNIT: Interacts with NCOA6; may enhance ligand-dependent
CC transcriptional activation by nuclear hormone receptors
CC (PubMed:12215545). Interacts with CNOT6 (PubMed:18180299). Interacts
CC with CNOT9; the interaction is direct (PubMed:18180299). Component of a
CC nuclear receptor-mediated transcription complex composed of at least
CC ZNF335, CCAR2 and EMSY; the complex stimulates the transcription of
CC nuclear receptor target genes such as SOX9 and HOXA1 (PubMed:19131338).
CC Within the complex interacts with EMSY and interacts (via C-terminus)
CC with CCAR2 (PubMed:19131338). Interacts with members of histone
CC H3'Lys4'(H3K4) methyltransferase complexes ASCL2, CXXC1, KMT2A/MLL1,
CC RBBP5, SETD1A and WDR5 (PubMed:23178126). Component of a histone
CC methylation complex composed of at least ZNF335, RBBP5, ASH2L and WDR5;
CC the complex may have histone H3-specific methyltransferase activity,
CC however does not have specificity for 'Lys-4' of histone H3
CC (PubMed:19131338). Interacts with RBBP5 and WDR5 (PubMed:19131338).
CC Interacts with ASHL2 (PubMed:19131338). Components of this complex may
CC associate with components of the ZNF335-CCAR2-EMSY nuclear receptor-
CC mediated transcription complex to form a complex at least composed of
CC ZNF335, HCFC1, CCAR2, EMSY, MKI67, RBBP5, ASH2L and WDR5
CC (PubMed:19131338). Within this complex also interacts with HCFC1 and
CC MKI67 (PubMed:19131338). {ECO:0000269|PubMed:12215545,
CC ECO:0000269|PubMed:18180299, ECO:0000269|PubMed:19131338,
CC ECO:0000269|PubMed:23178126}.
CC -!- INTERACTION:
CC Q9H4Z2; Q8N163: CCAR2; NbExp=5; IntAct=EBI-2795590, EBI-355410;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12215545}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H4Z2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H4Z2-2; Sequence=VSP_035791, VSP_035792;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:12215545, ECO:0000269|PubMed:23178126}.
CC -!- DEVELOPMENTAL STAGE: Widely expressed in fetal tissues including fetal
CC brain. {ECO:0000269|PubMed:23178126}.
CC -!- DISEASE: Microcephaly 10, primary, autosomal recessive (MCPH10)
CC [MIM:615095]: A form of microcephaly, a disease defined as a head
CC circumference more than 3 standard deviations below the age-related
CC mean. Brain weight is markedly reduced and the cerebral cortex is
CC disproportionately small. MCPH10 is characterized by extremely small
CC head size and death usually by 1 year of age. Neuropathologic
CC examination shows severe loss of neurons as well as neuronal loss of
CC polarity and abnormal dendritic maturation.
CC {ECO:0000269|PubMed:23178126}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15379.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF395833; AAN09900.1; -; mRNA.
DR EMBL; AK026157; BAB15379.1; ALT_INIT; mRNA.
DR EMBL; AK296989; BAG59529.1; -; mRNA.
DR EMBL; AL162458; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS13389.1; -. [Q9H4Z2-1]
DR RefSeq; NP_071378.1; NM_022095.3. [Q9H4Z2-1]
DR AlphaFoldDB; Q9H4Z2; -.
DR BioGRID; 121994; 22.
DR CORUM; Q9H4Z2; -.
DR IntAct; Q9H4Z2; 21.
DR STRING; 9606.ENSP00000325326; -.
DR GlyGen; Q9H4Z2; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9H4Z2; -.
DR PhosphoSitePlus; Q9H4Z2; -.
DR BioMuta; ZNF335; -.
DR DMDM; 20141037; -.
DR EPD; Q9H4Z2; -.
DR jPOST; Q9H4Z2; -.
DR MassIVE; Q9H4Z2; -.
DR MaxQB; Q9H4Z2; -.
DR PaxDb; Q9H4Z2; -.
DR PeptideAtlas; Q9H4Z2; -.
DR PRIDE; Q9H4Z2; -.
DR ProteomicsDB; 80883; -. [Q9H4Z2-1]
DR ProteomicsDB; 80884; -. [Q9H4Z2-2]
DR Antibodypedia; 27906; 126 antibodies from 28 providers.
DR DNASU; 63925; -.
DR Ensembl; ENST00000322927.3; ENSP00000325326.2; ENSG00000198026.8. [Q9H4Z2-1]
DR GeneID; 63925; -.
DR KEGG; hsa:63925; -.
DR MANE-Select; ENST00000322927.3; ENSP00000325326.2; NM_022095.4; NP_071378.1.
DR UCSC; uc002xqw.4; human. [Q9H4Z2-1]
DR CTD; 63925; -.
DR DisGeNET; 63925; -.
DR GeneCards; ZNF335; -.
DR HGNC; HGNC:15807; ZNF335.
DR HPA; ENSG00000198026; Low tissue specificity.
DR MalaCards; ZNF335; -.
DR MIM; 610827; gene.
DR MIM; 615095; phenotype.
DR neXtProt; NX_Q9H4Z2; -.
DR OpenTargets; ENSG00000198026; -.
DR Orphanet; 329228; Microcephalic primordial dwarfism due to ZNF335 deficiency.
DR PharmGKB; PA38041; -.
DR VEuPathDB; HostDB:ENSG00000198026; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000158508; -.
DR HOGENOM; CLU_006340_0_0_1; -.
DR InParanoid; Q9H4Z2; -.
DR OMA; HKRAHVG; -.
DR PhylomeDB; Q9H4Z2; -.
DR TreeFam; TF332472; -.
DR PathwayCommons; Q9H4Z2; -.
DR Reactome; R-HSA-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis.
DR SignaLink; Q9H4Z2; -.
DR BioGRID-ORCS; 63925; 508 hits in 1108 CRISPR screens.
DR ChiTaRS; ZNF335; human.
DR GenomeRNAi; 63925; -.
DR Pharos; Q9H4Z2; Tbio.
DR PRO; PR:Q9H4Z2; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9H4Z2; protein.
DR Bgee; ENSG00000198026; Expressed in granulocyte and 125 other tissues.
DR Genevisible; Q9H4Z2; HS.
DR GO; GO:0035097; C:histone methyltransferase complex; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR GO; GO:0007420; P:brain development; IMP:UniProtKB.
DR GO; GO:0048854; P:brain morphogenesis; IEA:Ensembl.
DR GO; GO:0021895; P:cerebral cortex neuron differentiation; IEA:Ensembl.
DR GO; GO:0080182; P:histone H3-K4 trimethylation; IMP:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0048812; P:neuron projection morphogenesis; ISS:UniProtKB.
DR GO; GO:0050671; P:positive regulation of lymphocyte proliferation; IMP:UniProtKB.
DR GO; GO:0002052; P:positive regulation of neuroblast proliferation; ISS:UniProtKB.
DR GO; GO:0050769; P:positive regulation of neurogenesis; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0040029; P:regulation of gene expression, epigenetic; IMP:UniProtKB.
DR GO; GO:0051569; P:regulation of histone H3-K4 methylation; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR SMART; SM00355; ZnF_C2H2; 13.
DR SUPFAM; SSF57667; SSF57667; 7.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 13.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Developmental protein; Disease variant;
KW DNA-binding; Intellectual disability; Isopeptide bond; Metal-binding;
KW Nucleus; Phosphoprotein; Primary microcephaly; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..1342
FT /note="Zinc finger protein 335"
FT /id="PRO_0000047538"
FT ZN_FING 245..268
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 465..487
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 495..517
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 523..545
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 562..584
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 590..612
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 621..643
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 649..672
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 678..701
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1019..1041
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1047..1069
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1075..1097
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1103..1126
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 732..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 964..1013
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1041..1342
FT /note="Involved in the interaction with CCAR2"
FT /evidence="ECO:0000269|PubMed:19131338"
FT COMPBIAS 53..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..325
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 740..754
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 981..996
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 976
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:G3V893"
FT MOD_RES 992
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1007
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1153
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT CROSSLNK 1022
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..155
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_035791"
FT VAR_SEQ 156..173
FT /note="EDGGAETTRYLILQGPDD -> MATSSMPESERNVATKAS (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_035792"
FT VARIANT 65
FT /note="R -> C (in dbSNP:rs6130982)"
FT /id="VAR_047560"
FT VARIANT 101
FT /note="G -> S (in dbSNP:rs6094231)"
FT /id="VAR_047561"
FT VARIANT 294
FT /note="S -> T (in dbSNP:rs6032606)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_024211"
FT VARIANT 603
FT /note="Y -> H (in dbSNP:rs16990961)"
FT /id="VAR_047562"
FT VARIANT 1111
FT /note="R -> H (in MCPH10; hypomorphic mutation; may cause
FT altered transcript but some full-length protein is still
FT formed; dbSNP:rs397514642)"
FT /evidence="ECO:0000269|PubMed:23178126"
FT /id="VAR_069469"
FT CONFLICT 227
FT /note="E -> G (in Ref. 2; BAG59529)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1342 AA; 144893 MW; 6D230DEE0B3AE670 CRC64;
MEENEVESSS DAAPGPGRPE EPSESGLGVG TSEAVSADSS DAAAAPGQAE ADDSGVGQSS
DRGSRSQEEV SESSSSADPL PNSYLPDSSS VSHGPVAGVT GGPPALVHSS ALPDPNMLVS
DCTASSSDLG SAIDKIIEST IGPDLIQNCI TVTSAEDGGA ETTRYLILQG PDDGAPMTSP
MSSSTLAHSL AAIEALADGP TSTSTCLEAQ GGPSSPVQLP PASGAEEPDL QSLEAMMEVV
VVQQFKCKMC QYRSSTKATL LRHMRERHFR PVAAAAAAAG KKGRLRKWST STKSQEEEGP
EEEDDDDIVD AGAIDDLEED SDYNPAEDEP RGRQLRLQRP TPSTPRPRRR PGRPRKLPRL
EISDLPDGVE GEPLVSSQSG QSPPEPQDPE APSSSGPGHL VAMGKVSRTP VEAGVSQSDA
ENAAPSCPDE HDTLPRRRGR PSRRFLGKKY RKYYYKSPKP LLRPFLCRIC GSRFLSHEDL
RFHVNSHEAG DPQLFKCLQC SYRSRRWSSL KEHMFNHVGS KPYKCDECSY TSVYRKDVIR
HAAVHSRDRK KRPDPTPKLS SFPCPVCGRV YPMQKRLTQH MKTHSTEKPH MCDKCGKSFK
KRYTFKMHLL THIQAVANRR FKCEFCEFVC EDKKALLNHQ LSHVSDKPFK CSFCPYRTFR
EDFLLSHVAV KHTGAKPFAC EYCHFSTRHK KNLRLHVRCR HASSFEEWGR RHPEEPPSRR
RPFFSLQQIE ELKQQHSAAP GPPPSSPGPP EIPPEATTFQ SSEAPSLLCS DTLGGATIIY
QQGAEESTAM ATQTALDLLL NMSAQRELGG TALQVAVVKS EDVEAGLASP GGQPSPEGAT
PQVVTLHVAE PGGGAAAESQ LGPPDLPQIT LAPGPFGGTG YSVITAPPME EGTSAPGTPY
SEEPAGEAAQ AVVVSDTLKE AGTHYIMATD GTQLHHIELT ADGSISFPSP DALASGAKWP
LLQCGGLPRD GPEPPSPAKT HCVGDSQSSA SSPPATSKAL GLAVPPSPPS AATAASKKFS
CKICAEAFPG RAEMESHKRA HAGPGAFKCP DCPFSARQWP EVRAHMAQHS SLRPHQCSQC
SFASKNKKDL RRHMLTHTKE KPFACHLCGQ RFNRNGHLKF HIQRLHSPDG RKSGTPTARA
PTQTPTQTII LNSDDETLAT LHTALQSSHG VLGPERLQQA LSQEHIIVAQ EQTVTNQEEA
AYIQEITTAD GQTVQHLVTS DNQVQYIISQ DGVQHLLPQE YVVVPEGHHI QVQEGQITHI
QYEQGAPFLQ ESQIQYVPVS PGQQLVTQAQ LEAAAHSAVT AVADAAMAQA QGLFGTDETV
PEHIQQLQHQ GIEYDVITLA DD
