ZN335_MOUSE
ID ZN335_MOUSE Reviewed; 1337 AA.
AC A2A5K6; B2RXR9; Q3TZT1;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Zinc finger protein 335;
DE AltName: Full=NRC-interacting factor 1;
DE Short=NIF-1;
GN Name=Znf335; Synonyms=Zfp335;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD; TISSUE=Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
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 [4]
RP FUNCTION IN NEUROGENESIS, INTERACTION WITH RBBP5 AND WDR5, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
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 (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 (PubMed:23178126).
CC Also controls the expression of genes involved in somatic development
CC and regulates, for instance, lymphoblast proliferation (By similarity).
CC {ECO:0000250|UniProtKB:Q9H4Z2, ECO:0000269|PubMed:23178126}.
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 (By similarity). 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 (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 (By
CC similarity). Interacts with RBBP5 and WDR5 (PubMed:23178126). 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:23178126}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23178126}.
CC -!- TISSUE SPECIFICITY: Expressed at low levels in cerebral cortex,
CC hippocampus and cerebellum (at protein level).
CC {ECO:0000269|PubMed:23178126}.
CC -!- DEVELOPMENTAL STAGE: In brain, expression peaks at 13-15 dpc, during
CC cortical neurogenesis. At 8.5 dpc, expressed in forebrain and midbrain.
CC At 14.5 dpc, expressed in ventricular zone, subventricular zone and
CC cortical plate. {ECO:0000269|PubMed:23178126}.
CC -!- DISRUPTION PHENOTYPE: Loss leads to embryonic lethality as early as 7.5
CC dpc. Brain-specific conditional knockout produces a brain with an
CC essentially absent cortex lacking all cortical neurons.
CC {ECO:0000269|PubMed:23178126}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AK157577; BAE34126.1; -; mRNA.
DR EMBL; AL591495; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC151013; AAI51014.1; -; mRNA.
DR EMBL; BC157954; AAI57955.1; -; mRNA.
DR CCDS; CCDS38331.1; -.
DR RefSeq; NP_950192.2; NM_199027.2.
DR AlphaFoldDB; A2A5K6; -.
DR STRING; 10090.ENSMUSP00000038298; -.
DR iPTMnet; A2A5K6; -.
DR PhosphoSitePlus; A2A5K6; -.
DR EPD; A2A5K6; -.
DR MaxQB; A2A5K6; -.
DR PaxDb; A2A5K6; -.
DR PeptideAtlas; A2A5K6; -.
DR PRIDE; A2A5K6; -.
DR ProteomicsDB; 275283; -.
DR Antibodypedia; 27906; 126 antibodies from 28 providers.
DR Ensembl; ENSMUST00000041361; ENSMUSP00000038298; ENSMUSG00000039834.
DR GeneID; 329559; -.
DR KEGG; mmu:329559; -.
DR UCSC; uc008nwr.1; mouse.
DR CTD; 329559; -.
DR MGI; MGI:2682313; Zfp335.
DR VEuPathDB; HostDB:ENSMUSG00000039834; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000158508; -.
DR HOGENOM; CLU_006340_0_0_1; -.
DR InParanoid; A2A5K6; -.
DR OMA; HKRAHVG; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; A2A5K6; -.
DR TreeFam; TF332472; -.
DR BioGRID-ORCS; 329559; 7 hits in 75 CRISPR screens.
DR ChiTaRS; Zfp335; mouse.
DR PRO; PR:A2A5K6; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; A2A5K6; protein.
DR Bgee; ENSMUSG00000039834; Expressed in granulocyte and 203 other tissues.
DR ExpressionAtlas; A2A5K6; baseline and differential.
DR Genevisible; A2A5K6; MM.
DR GO; GO:0035097; C:histone methyltransferase complex; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA: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; IDA:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0007420; P:brain development; IMP:UniProtKB.
DR GO; GO:0048854; P:brain morphogenesis; IMP:MGI.
DR GO; GO:0021895; P:cerebral cortex neuron differentiation; IMP:MGI.
DR GO; GO:0080182; P:histone H3-K4 trimethylation; ISS:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0048812; P:neuron projection morphogenesis; IMP:UniProtKB.
DR GO; GO:0050671; P:positive regulation of lymphocyte proliferation; ISS:UniProtKB.
DR GO; GO:0002052; P:positive regulation of neuroblast proliferation; IMP:UniProtKB.
DR GO; GO:0050769; P:positive regulation of neurogenesis; ISO:MGI.
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; IDA:MGI.
DR GO; GO:0040029; P:regulation of gene expression, epigenetic; ISS:UniProtKB.
DR GO; GO:0051569; P:regulation of histone H3-K4 methylation; IDA:MGI.
DR GO; GO:0050767; P:regulation of neurogenesis; IMP:MGI.
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..1337
FT /note="Zinc finger protein 335"
FT /id="PRO_0000419259"
FT ZN_FING 248..271
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 466..488
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 496..518
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 524..546
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 563..585
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 591..613
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 622..644
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 650..673
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 679..702
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..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 278..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 733..767
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 963..999
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..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..330
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 743..765
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 979..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 1007
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4Z2"
FT MOD_RES 1149
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4Z2"
FT CROSSLNK 1022
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H4Z2"
FT CONFLICT 309
FT /note="E -> EE (in Ref. 1; BAE34126 and 3; AAI57955/
FT AAI51014)"
FT /evidence="ECO:0000305"
FT CONFLICT 400
FT /note="G -> D (in Ref. 1; BAE34126 and 3; AAI57955/
FT AAI51014)"
FT /evidence="ECO:0000305"
FT CONFLICT 490
FT /note="A -> V (in Ref. 1; BAE34126)"
FT /evidence="ECO:0000305"
FT CONFLICT 526
FT /note="C -> G (in Ref. 1; BAE34126)"
FT /evidence="ECO:0000305"
FT CONFLICT 712
FT /note="R -> C (in Ref. 1; BAE34126)"
FT /evidence="ECO:0000305"
FT CONFLICT 856
FT /note="A -> E (in Ref. 1; BAE34126 and 3; AAI57955/
FT AAI51014)"
FT /evidence="ECO:0000305"
FT CONFLICT 949
FT /note="S -> G (in Ref. 1; BAE34126)"
FT /evidence="ECO:0000305"
FT CONFLICT 1135
FT /note="T -> I (in Ref. 1; BAE34126 and 3; AAI57955/
FT AAI51014)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1337 AA; 145603 MW; 48E6D13B3C16F2BB CRC64;
MEENEVESSS DAAPRPGQPE EPSESGLGVC TSEAVSADSS DAATVPGLTE ADDSGVGQSS
DGGNHSVEEV SESISTDPLP HGCLPDSSSV SRGPVAEMPG GPPALVHSSV LPDPSMLVSD
CTASSSDLGS AIDKIIESTI GPDLIQSCIT VTSGEEGGAE TTQYLILQGP DDGAPMASSM
STSTLANSLA AIEALADGPT STSACLEPPE EPQGDPSSVA QQPPAPVTEE LDLQSLEAMM
EVVVVQQFKC KMCQYRSSTK ATLLRHMRER HFRPALAAAA AATGKRGRVR KWGTSTKTTE
EDRPEEEEED DDIVDAGAID DLEEDSDYNP AEDEPRGRQL RLQRPTPSTP RPRRRPGRPR
KLPRLETSDL HDGVGQPLVS SQSTQSPPEL QDLEAPSSSG LRALGKVGRG LVESGVSQSD
AENAAPSCQD EADAPPRRRG RPSRRFLGKK YRKYYYKSPK PLLRPYLCRI CGSRFLSHED
LRFHVNSHEA GDPQLFRCLQ CSYRSRRWSS LKEHMFNHVG SKPYKCDECS YTSVYRKDVI
RHAAVHSQDR KKRPDPTPKL SSFPCPVCGR VYPMQKRLTQ HMKTHSTEKP HMCDKCGKSF
KKRYTFKMHL LTHIQAVANR RFKCEFCEFV CEDKKALLNH QLSHVSDKPF KCSFCPYRTF
REDFLLSHVA VKHTGAKPFA CEYCHFSTRH KKNLRLHVRC RHANSFEEWG RRHPEEPPSR
RRPFFSLQQI EELKQQHSTA PGPPLSSPGP EAPQEPAPFQ SPETPPLLCP DALGGTTIIY
QQGAEESTAV ATQTALDLLL NMSAQRELGA TALQVAVVKS EGIEAELTST GGQPSPEDTT
PRVVTLHMAE SGSSVAAESQ LGPSDLQQIA LPSGPFGGAS YSVITAPPVE GRTSASGPPY
REEPPGEAAQ AVVVSDTLKE AGTHYIMAAD GTQLHHIELT ADGSISFPSP DTLAPGTKWP
LLQCGGPPRD GSEVLSPTKT HHMGGSQGSS TPPPAASHTL GLVVPQSPPS AAASSTKKFS
CKVCSEAFPS RAEMESHKRA HAGPAAFKCP DCPFSARQWP EVRAHMAQHS SLRPHQCNQC
SFASKNKKDL RRHMLTHTNE KPFSCHVCGQ RFNRNGHLKF HIQRLHSIDG RKTGTSTARA
PAQTIILNSE EETLATLHTA FQSSHGVLGT ERLQQALSQE HIIVAQEQTV TNQEEATYIQ
EITADGQTVQ HLVTSDNQVQ YIISQDGVQH LLPQEYVVVP DGHHIQVQEG QITHIQYEQG
TPFLQESQIQ YVPVSPSQQL VTQAQLEAAA HSAVTAVADA AMAQAQGLFG TEEAVPEQIH
QLQHQGIEYD VITLSDD
