ZN749_HUMAN
ID ZN749_HUMAN Reviewed; 778 AA.
AC O43361;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Zinc finger protein 749;
GN Name=ZNF749;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-692.
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 ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-466 AND LYS-539, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [4]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-761 AND LYS-768, AND
RP IDENTIFICATION 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.
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=AAB97932.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC004076; AAB97932.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AK122794; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS33132.2; -.
DR RefSeq; NP_001018855.2; NM_001023561.3.
DR RefSeq; NP_001308882.1; NM_001321953.1.
DR RefSeq; NP_001308883.1; NM_001321954.1.
DR RefSeq; XP_016882291.1; XM_017026802.1.
DR AlphaFoldDB; O43361; -.
DR SMR; O43361; -.
DR BioGRID; 132749; 3.
DR STRING; 9606.ENSP00000333980; -.
DR GlyGen; O43361; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O43361; -.
DR PhosphoSitePlus; O43361; -.
DR BioMuta; ZNF749; -.
DR EPD; O43361; -.
DR jPOST; O43361; -.
DR MassIVE; O43361; -.
DR MaxQB; O43361; -.
DR PaxDb; O43361; -.
DR PeptideAtlas; O43361; -.
DR PRIDE; O43361; -.
DR ProteomicsDB; 48910; -.
DR Antibodypedia; 51139; 46 antibodies from 8 providers.
DR DNASU; 388567; -.
DR Ensembl; ENST00000334181.5; ENSP00000333980.4; ENSG00000186230.7.
DR GeneID; 388567; -.
DR KEGG; hsa:388567; -.
DR MANE-Select; ENST00000334181.5; ENSP00000333980.4; NM_001023561.4; NP_001018855.2.
DR UCSC; uc002qoq.3; human.
DR CTD; 388567; -.
DR GeneCards; ZNF749; -.
DR HGNC; HGNC:32783; ZNF749.
DR HPA; ENSG00000186230; Low tissue specificity.
DR neXtProt; NX_O43361; -.
DR VEuPathDB; HostDB:ENSG00000186230; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000164862; -.
DR HOGENOM; CLU_002678_17_1_1; -.
DR InParanoid; O43361; -.
DR OMA; PIEHQEI; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; O43361; -.
DR TreeFam; TF339848; -.
DR PathwayCommons; O43361; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; O43361; -.
DR BioGRID-ORCS; 388567; 8 hits in 1101 CRISPR screens.
DR GenomeRNAi; 388567; -.
DR Pharos; O43361; Tdark.
DR PRO; PR:O43361; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; O43361; protein.
DR Bgee; ENSG00000186230; Expressed in mucosa of transverse colon and 97 other tissues.
DR ExpressionAtlas; O43361; baseline and differential.
DR Genevisible; O43361; HS.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor 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:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd07765; KRAB_A-box; 1.
DR InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF00096; zf-C2H2; 10.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 16.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 11.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 13.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 17.
PE 1: Evidence at protein level;
KW Acetylation; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..778
FT /note="Zinc finger protein 749"
FT /id="PRO_0000274397"
FT DOMAIN 8..101
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 152..174
FT /note="C2H2-type 1; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 196..218
FT /note="C2H2-type 2; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 224..246
FT /note="C2H2-type 3; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 252..274
FT /note="C2H2-type 4; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 298..320
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 326..348
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 354..376
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 382..404
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 410..432
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 438..460
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 483..505
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 511..533
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 556..578
FT /note="C2H2-type 13; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 584..606
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 612..634
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 640..662
FT /note="C2H2-type 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 668..690
FT /note="C2H2-type 17; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 696..718
FT /note="C2H2-type 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 751..773
FT /note="C2H2-type 19; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT MOD_RES 466
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 539
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT CROSSLNK 761
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 768
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 243
FT /note="Q -> R (in dbSNP:rs12986235)"
FT /id="VAR_030278"
FT VARIANT 405
FT /note="A -> T (in dbSNP:rs2240038)"
FT /id="VAR_030279"
FT VARIANT 771
FT /note="I -> R (in dbSNP:rs7246856)"
FT /id="VAR_030280"
FT CONFLICT 177
FT /note="Missing (in Ref. 2; AK122794)"
FT /evidence="ECO:0000305"
FT CONFLICT 679
FT /note="Y -> C (in Ref. 2; AK122794)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 778 AA; 90364 MW; FB08226F2E47856B CRC64;
MNLTEDCMVF EDVAIYFSQE EWGILNDAQR HLHSNVMLEN FALLSSVGCW HGAKDEEVPS
KQCVSVRVLQ VTIPKPALST LKAQPCKMCS SILKDILHLA EHDGTHPEQG LYTCAAEHDL
HQKEQIREKL TRSDEWRPSF VNHSAHVGER NFTCTQGGKD FTASSDLLQQ QVLNSGWKLY
RDTQDGEAFQ GEQNDFNSSQ GGKDFCHQHG LFEHQKTHNG ERPYEFSECG ELFRYNSNLI
KYQQNHAGER PYEGTEYGKT FIRKSNLVQH QKIHSEGFLS KRSDPIEHQE ILSRPTPYEC
TQCGKAFLTQ AHLVGHQKTH TGEQPYECNK CGKFFMYNSK LIRHQKVHTG ERRYECSECG
KLFMDSFTLG RHQRVHTGER PFECSICGKF FSHRSTLNMH QRVHAGKRLY KCSECGKAFS
LKHNVVQHLK IHTGERPYEC TECEKAFVRK SHLVQHQKIH TDAFSKRSDL IQHKRIDIRP
RPYTCSECGK AFLTQAHLVG HQKIHTGERP YECTQCAKAF VRKSHLVQHE KIHTDAFSKR
SDLIQHKRID LRPRPYVCSE CGKAFLTQAH LDGHQKIQTG ERRYECNECG KFFLDSYKLV
IHQRIHTGEK PYKCSKCGKF FRYRCTLSRH QKVHTGERPY ECSECGKFFR DSYKLIIHQR
VHTGEKPYEC SNCGKFLRYR STFIKHHKVC TGEKPHECSK CRELFRTKSS LIIHQQSHTG
ESPFKLRECG KDFNKCNTGQ RQKTHTGERS YECGESSKVF KYNSSLIKHQ IIHTGKRP
