ZN629_MOUSE
ID ZN629_MOUSE Reviewed; 867 AA.
AC Q6A085; Q8BG88; Q8BIR0;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Zinc finger protein 629;
GN Name=Znf629; Synonyms=Kiaa0326, Zfp629;
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 TISSUE=Pancreatic islet;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Diencephalon, and Forelimb;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Eye;
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).
CC -!- FUNCTION: May be involved in transcriptional regulation.
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=BAD32211.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK172933; BAD32211.1; ALT_INIT; mRNA.
DR EMBL; AK031161; BAC27286.1; -; mRNA.
DR EMBL; AK034484; BAC28725.1; -; mRNA.
DR EMBL; BC035547; AAH35547.1; -; mRNA.
DR EMBL; BC067053; AAH67053.1; -; mRNA.
DR CCDS; CCDS21873.1; -.
DR RefSeq; NP_796200.1; NM_177226.5.
DR RefSeq; XP_006508016.1; XM_006507953.3.
DR RefSeq; XP_011240135.1; XM_011241833.2.
DR AlphaFoldDB; Q6A085; -.
DR SMR; Q6A085; -.
DR STRING; 10090.ENSMUSP00000053760; -.
DR iPTMnet; Q6A085; -.
DR PhosphoSitePlus; Q6A085; -.
DR EPD; Q6A085; -.
DR MaxQB; Q6A085; -.
DR PaxDb; Q6A085; -.
DR PeptideAtlas; Q6A085; -.
DR PRIDE; Q6A085; -.
DR ProteomicsDB; 275021; -.
DR Antibodypedia; 7095; 12 antibodies from 7 providers.
DR DNASU; 320683; -.
DR Ensembl; ENSMUST00000058038; ENSMUSP00000053760; ENSMUSG00000045639.
DR Ensembl; ENSMUST00000084564; ENSMUSP00000081612; ENSMUSG00000045639.
DR Ensembl; ENSMUST00000122066; ENSMUSP00000113903; ENSMUSG00000045639.
DR GeneID; 320683; -.
DR KEGG; mmu:320683; -.
DR UCSC; uc009jwh.1; mouse.
DR CTD; 320683; -.
DR MGI; MGI:2444524; Zfp629.
DR VEuPathDB; HostDB:ENSMUSG00000045639; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000161909; -.
DR HOGENOM; CLU_014070_0_0_1; -.
DR InParanoid; Q6A085; -.
DR OMA; FKMPEGQ; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q6A085; -.
DR TreeFam; TF350847; -.
DR BioGRID-ORCS; 320683; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Zfp629; mouse.
DR PRO; PR:Q6A085; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q6A085; protein.
DR Bgee; ENSMUSG00000045639; Expressed in dorsal pancreas and 224 other tissues.
DR ExpressionAtlas; Q6A085; baseline and differential.
DR Genevisible; Q6A085; MM.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IBA:GO_Central.
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:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 14.
DR SMART; SM00355; ZnF_C2H2; 19.
DR SUPFAM; SSF57667; SSF57667; 12.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 19.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 19.
PE 2: Evidence at transcript level;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..867
FT /note="Zinc finger protein 629"
FT /id="PRO_0000280427"
FT ZN_FING 149..171
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 177..199
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 205..227
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 233..255
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 261..283
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 289..311
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 317..339
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 345..367
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 373..395
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 401..423
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 429..451
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 457..479
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 485..507
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 513..535
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 568..590
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 661..683
FT /note="C2H2-type 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 713..735
FT /note="C2H2-type 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 766..788
FT /note="C2H2-type 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 840..862
FT /note="C2H2-type 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 596..656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 786..839
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 798..824
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UEG4"
FT CROSSLNK 250
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UEG4"
FT CROSSLNK 687
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UEG4"
FT CROSSLNK 748
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UEG4"
FT CROSSLNK 838
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UEG4"
FT CONFLICT 319
FT /note="C -> Y (in Ref. 2; BAC27286)"
FT /evidence="ECO:0000305"
FT CONFLICT 385
FT /note="S -> R (in Ref. 2; BAC27286)"
FT /evidence="ECO:0000305"
FT CONFLICT 545
FT /note="A -> D (in Ref. 2; BAC27286)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 867 AA; 96033 MW; B53C48A5D8D9D92C CRC64;
MEPETVLWGP DLQGPEESQN EAHRGAGSGN EEESPQQESS GEEIILGDPA QSPESKDPSE
MPLESPSQDA SAPQDSPTPL GSSPLDHQTP MDPSAPEVVP SPSEWTKACE TNWQWGTLTP
WNSTPVVTAS EPSLRELVQG RPSGAEKPYI CNECGKSFSQ WSKLLRHQRI HTGERPNTCS
ECGKSFTQSS HLVQHQRTHT GEKPYKCPDC GKCFSWSSNL VQHQRTHTGE KPYKCTECEK
AFTQSTNLIK HQRSHTGEKP YKCGECRRAF YRSSDLIQHQ ATHTGEKPYK CPECGKRFGQ
NHNLLKHQKI HAGEKPYRCT ECGKSFIQSS ELTQHQRTHT GEKPYECLEC GKSFGHSSTL
IKHQRTHLRE DPFKCPVCGK TFTLSATLLR HQRTHTGERP YKCPECGKSF SVSSNLINHQ
RIHRGERPYI CADCGKSFIM SSTLIRHQRI HTGEKPYKCS DCGKSFIRSS HLIQHRRTHT
GEKPYKCPEC GKSFSQSSNL ITHVRTHMDE NLFVCSDCGK AFLEAQELEQ HRVIHERGKT
PARRAQGDSL LGFGDPALMT PPPGAKPHKC LVCGKGFNDE GIFMQHQRIH IGENPYKNAD
GLITHPAPKP QQLRPSRLPF GGNSHPGASE SRADPPGQPS KVPESQEGSG QRPGQPSPKC
YVCSHCGESF LDRAVLLQHQ LTHGNEKPFL FPECRTGRGE GAGPSPFLNA KPFKCPECKK
SFGLSSELLQ HQKVHAGGKS QKSSELGKSS SVLLEHLRSP LGARPYSCSD CGASFLDRLA
LTRHQETHTH ERASTPEDTP SESATLSTNQ EDEGEASTPP KSSSHGEEES PKTVSEKKPF
LCPECGDGFT EVATLLLHRS CHPGVSL
