| Tag | Content |
|---|
| CPLM ID | CPLM-000692 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Zinc finger protein 749 |
Protein Synonyms/Alias | |
Gene Name | ZNF749 |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 466 | IHTDAFSKRSDLIQH | acetylation | [1] |
|
Reference | [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M. Science. 2009 Aug 14;325(5942):834-40. [ PMID: 19608861] |
Functional Description | May be involved in transcriptional regulation. |
Sequence Annotation | DOMAIN 8 101 KRAB.
ZN_FING 152 174 C2H2-type 1; degenerate.
ZN_FING 196 218 C2H2-type 2; degenerate.
ZN_FING 224 246 C2H2-type 3; degenerate.
ZN_FING 252 274 C2H2-type 4; degenerate.
ZN_FING 298 320 C2H2-type 5.
ZN_FING 326 348 C2H2-type 6.
ZN_FING 354 376 C2H2-type 7.
ZN_FING 382 404 C2H2-type 8.
ZN_FING 410 432 C2H2-type 9.
ZN_FING 438 460 C2H2-type 10.
ZN_FING 483 505 C2H2-type 11.
ZN_FING 511 533 C2H2-type 12.
ZN_FING 556 578 C2H2-type 13; degenerate.
ZN_FING 584 606 C2H2-type 14.
ZN_FING 612 634 C2H2-type 15.
ZN_FING 640 662 C2H2-type 16.
ZN_FING 668 690 C2H2-type 17; atypical.
ZN_FING 696 718 C2H2-type 18.
ZN_FING 751 773 C2H2-type 19; degenerate.
MOD_RES 466 466 N6-acetyllysine.
MOD_RES 539 539 N6-acetyllysine. |
Keyword | Acetylation; Complete proteome; DNA-binding; Metal-binding; Nucleus; Polymorphism; Reference proteome; Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 778 AA |
Protein Sequence | MNLTEDCMVF EDVAIYFSQE EWGILNDAQR HLHSNVMLEN FALLSSVGCW HGAKDEEVPS 60
KQCVSVRVLQ VTIPKPALST LKAQPCKMCS SILKDILHLA EHDGTHPEQG LYTCAAEHDL 120
HQKEQIREKL TRSDEWRPSF VNHSAHVGER NFTCTQGGKD FTASSDLLQQ QVLNSGWKLY 180
RDTQDGEAFQ GEQNDFNSSQ GGKDFCHQHG LFEHQKTHNG ERPYEFSECG ELFRYNSNLI 240
KYQQNHAGER PYEGTEYGKT FIRKSNLVQH QKIHSEGFLS KRSDPIEHQE ILSRPTPYEC 300
TQCGKAFLTQ AHLVGHQKTH TGEQPYECNK CGKFFMYNSK LIRHQKVHTG ERRYECSECG 360
KLFMDSFTLG RHQRVHTGER PFECSICGKF FSHRSTLNMH QRVHAGKRLY KCSECGKAFS 420
LKHNVVQHLK IHTGERPYEC TECEKAFVRK SHLVQHQKIH TDAFSKRSDL IQHKRIDIRP 480
RPYTCSECGK AFLTQAHLVG HQKIHTGERP YECTQCAKAF VRKSHLVQHE KIHTDAFSKR 540
SDLIQHKRID LRPRPYVCSE CGKAFLTQAH LDGHQKIQTG ERRYECNECG KFFLDSYKLV 600
IHQRIHTGEK PYKCSKCGKF FRYRCTLSRH QKVHTGERPY ECSECGKFFR DSYKLIIHQR 660
VHTGEKPYEC SNCGKFLRYR STFIKHHKVC TGEKPHECSK CRELFRTKSS LIIHQQSHTG 720
ESPFKLRECG KDFNKCNTGQ RQKTHTGERS YECGESSKVF KYNSSLIKHQ IIHTGKRP 778 |
Gene Ontology | GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. GO:0003677; F:DNA binding; IEA:UniProtKB-KW. GO:0008270; F:zinc ion binding; IEA:InterPro. GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW. GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |