ZN335_RAT
ID ZN335_RAT Reviewed; 1336 AA.
AC G3V893; Q8CIV9;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Zinc finger protein 335;
DE AltName: Full=NRC-interacting factor 1;
DE Short=NIF-1;
GN Name=Znf335; Synonyms=Zfp335;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 514-1336, AND INTERACTION WITH NCOA6.
RC STRAIN=Wistar Furth; TISSUE=Pituitary;
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 [3]
RP INTERACTION WITH 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-975, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(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 (By similarity).
CC Enhances ligand-dependent transcriptional activation by nuclear hormone
CC receptors (By similarity). Plays an important role in neural progenitor
CC cell proliferation and self-renewal through the regulation of specific
CC genes involved brain development, including REST (By similarity). Also
CC controls the expression of genes involved in somatic development and
CC regulates, for instance, lymphoblast proliferation (By similarity).
CC {ECO:0000250|UniProtKB:Q9H4Z2}.
CC -!- SUBUNIT: Interacts with NCOA6; may enhance ligand-dependent
CC transcriptional activation by nuclear hormone receptors (By
CC similarity). Interacts with CNOT6 (By similarity). Interacts with
CC 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 (By similarity).
CC Within the complex interacts with EMSY and interacts (via C-terminus)
CC with CCAR2 (By similarity). Interacts with members of histone
CC H3'Lys4'(H3K4) methyltransferase complexes ASCL2, CXXC1, KMT2A/MLL1,
CC RBBP5, SETD1A and WDR5 (By similarity). 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 (By
CC similarity). Interacts with RBBP5 and WDR5 (By similarity). Interacts
CC with ASHL2 (By similarity). Components of this complex may associate
CC with components of the ZNF335-CCAR2-EMSY nuclear receptor-mediated
CC transcription complex to form a complex at least composed of ZNF335,
CC HCFC1, CCAR2, EMSY, MKI67, RBBP5, ASH2L and WDR5 (By similarity).
CC Within this complex also interacts with HCFC1 and MKI67 (By
CC similarity). {ECO:0000250|UniProtKB:Q9H4Z2,
CC ECO:0000269|PubMed:18180299}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; CH474005; EDL96481.1; -; Genomic_DNA.
DR EMBL; AY079168; AAL86014.1; -; mRNA.
DR RefSeq; XP_008760786.1; XM_008762564.2.
DR RefSeq; XP_008773840.1; XM_008775618.2.
DR AlphaFoldDB; G3V893; -.
DR SMR; G3V893; -.
DR STRING; 10116.ENSRNOP00000023523; -.
DR iPTMnet; G3V893; -.
DR PhosphoSitePlus; G3V893; -.
DR PaxDb; G3V893; -.
DR PRIDE; G3V893; -.
DR Ensembl; ENSRNOT00000110042; ENSRNOP00000097203; ENSRNOG00000017290.
DR GeneID; 259270; -.
DR CTD; 329559; -.
DR RGD; 628751; Zfp335.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000158508; -.
DR HOGENOM; CLU_006340_0_0_1; -.
DR InParanoid; G3V893; -.
DR OrthoDB; 1318335at2759; -.
DR TreeFam; TF332472; -.
DR PRO; PR:G3V893; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Proteomes; UP000234681; Chromosome 3.
DR Genevisible; G3V893; RN.
DR GO; GO:0035097; C:histone methyltransferase complex; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; ISS:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR GO; GO:0007420; P:brain development; ISS:UniProtKB.
DR GO; GO:0048854; P:brain morphogenesis; ISO:RGD.
DR GO; GO:0021895; P:cerebral cortex neuron differentiation; ISO:RGD.
DR GO; GO:0080182; P:histone H3-K4 trimethylation; ISS:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0048812; P:neuron projection morphogenesis; ISS:UniProtKB.
DR GO; GO:0050671; P:positive regulation of lymphocyte proliferation; ISS:UniProtKB.
DR GO; GO:0002052; P:positive regulation of neuroblast proliferation; ISS:UniProtKB.
DR GO; GO:0050769; P:positive regulation of neurogenesis; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0040029; P:regulation of gene expression, epigenetic; ISS:UniProtKB.
DR GO; GO:0051569; P:regulation of histone H3-K4 methylation; ISO:RGD.
DR GO; GO:0050767; P:regulation of neurogenesis; ISO:RGD.
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; Developmental protein; DNA-binding; Isopeptide bond;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..1336
FT /note="Zinc finger protein 335"
FT /id="PRO_0000419260"
FT ZN_FING 247..270
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 1018..1040
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1046..1068
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1074..1096
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1102..1125
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 199..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 415..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 732..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 961..1013
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..329
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..392
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..766
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 978..995
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 975
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1006
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4Z2"
FT MOD_RES 1148
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4Z2"
FT CROSSLNK 1021
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H4Z2"
FT CONFLICT 723
FT /note="F -> I (in Ref. 2; AAL86014)"
FT /evidence="ECO:0000305"
FT CONFLICT 731
FT /note="E -> K (in Ref. 2; AAL86014)"
FT /evidence="ECO:0000305"
FT CONFLICT 760
FT /note="P -> S (in Ref. 2; AAL86014)"
FT /evidence="ECO:0000305"
FT CONFLICT 1295
FT /note="Missing (in Ref. 2; AAL86014)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1336 AA; 145536 MW; B0532FF562440206 CRC64;
MEENEVESSS DAAPRPGQPE EPSESGLGVG TSEAVSADST DAATAPGLTE ADDSGVGQSS
DSGSRSVEEV SESISTEPLP QGYLPDSSSV SRGPVAEVPG GPPALVHSSA LPDPSMLVSD
CTASSSDLGS AIDKIIESTI GPDLIQSCIT VTSGEEGGAE TTQYLILQGP DDGAPMASSM
STSTLANSLA AIEALADGPT STSTCLEPAE QPPGEPSSLA QPPAPVVEEL DLQGLEAMME
VVVVQQFKCK MCQYRSSTKA TLLRHMRERH FRPALAVAAA AAGKRGRVRK WGTSTKTTEE
EGPEEEEEDD DIVDAGAIDD LEEDSDYNPA EDEPRGRQLR LQRPTPSTLR PRRRPGRPRK
LPRLETSDLH DGIGEPLVSS QSTQSPPELQ DLEAPSSSDL RALGKVGRGL VETGVSQSDA
ENAAPSCQDE ADVPPRRRGR PSRRFLGKKY RKYYYKSPKP LLRPYLCRIC GSRFLSHEDL
RFHVNSHEAG DPQLFKCLQC SYRSRRWSSL KEHMFNHVGS KPYKCDECSY TSVYRKDVIR
HAAVHSQDRK KRPDPTPKLS SFPCPVCGRV YPMQKRLTQH MKTHSTEKPH MCDKCGKSFK
KRYTFKMHLL THIQAVANRR FKCEFCEFVC EDKKALLNHQ LSHVSDKPFK CSFCPYRTFR
EDFLLSHVAV KHTGAKPFAC EYCHFSTRHK KNLRLHVRCR HANSFEEWGR RHPEEPPSRR
RPFFSLQQIE ELKQQHSAAP GPPLSSAGPE APQEPAPFQP PETPPLLCPD ALGGATIIYQ
QGAEESTAMA TQTALDLLLN MSAQRELGAT ALQVAVVKSE DVEAELTSTA RQPSSEDTTP
RVVTLHVAES GSSVAAESQL GPSDLQQIAL PPGPFSGASY SVITAPPVEG RASASGPPYR
EEPPGEAAQA VVVNDTLKEA GTHYIMAADG TQLHHIELTA DGSISFPSPD TLAPGTKWPL
LQCGGPPRDG PEVLSPTKTH HTGGSQGSST PPPATSHALG LLVPHSPPSA AASSTKKFSC
KVCSEAFPSR AEMESHKRAH AGPAAFKCPD CPFSARQWPE VRAHMAQHSS LRPHQCNQCS
FASKNKKDLR RHMLTHTNEK PFSCHVCGQR FNRNGHLKFH IQRLHSIDGR KTGTSTARAP
AQTIILNSEE ETLATLHTAF QSNHGTLGTE RLQQALSQEH IIVAQEQTVA NQEEATYIQE
ITADGQTVQH LVTSDNQVQY IISQDGVQHL LPQEYVVVPD GHHIQVQEGQ ITHIQYEQGT
PFLQESQIQY VPVSPSQQLV TQAQLEAAAH SAVTAVADAA MAQAQGLFGT EEAVPEHIQQ
LQHQGIEYDV ITLSDD
