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RB-associated KRAB zinc finger protein (RB-associated KRAB repressor) (hRBaK) (Zinc finger protein 769)

 RBAK_HUMAN              Reviewed;         714 AA.
Q9NYW8; A6NDF2; A8KAK4; B2RN44; B9EGS1; F8W6M7;
05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
22-NOV-2017, entry version 145.
RecName: Full=RB-associated KRAB zinc finger protein;
AltName: Full=RB-associated KRAB repressor;
Short=hRBaK;
AltName: Full=Zinc finger protein 769;
Name=RBAK; Synonyms=ZNF769;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH
RB1, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=10702291; DOI=10.1074/jbc.275.10.7212;
Skapek S.X., Jansen D., Wei T.-F., McDermott T., Huang W., Olson E.N.,
Lee E.Y.-H.P.;
"Cloning and characterization of a novel Kruppel-associated box family
transcriptional repressor that interacts with the retinoblastoma gene
product, RB.";
J. Biol. Chem. 275:7212-7223(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
PubMed=8889548; DOI=10.1101/gr.6.9.791;
Bonaldo M.F., Lennon G., Soares M.B.;
"Normalization and subtraction: two approaches to facilitate gene
discovery.";
Genome Res. 6:791-806(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Uterus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
FUNCTION, AND INTERACTION WITH AR.
PubMed=14664718; DOI=10.1677/jme.0.0310583;
Hofman K., Swinnen J.V., Claessens F., Verhoeven G., Heyns W.;
"The retinoblastoma protein-associated transcription repressor RBaK
interacts with the androgen receptor and enhances its transcriptional
activity.";
J. Mol. Endocrinol. 31:583-596(2003).
[8]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-534, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[9]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-534, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[10]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-97; LYS-259; LYS-315;
LYS-357; LYS-534 AND LYS-537, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
-!- FUNCTION: May repress E2F-dependent transcription. May promote AR-
dependent transcription. {ECO:0000269|PubMed:10702291,
ECO:0000269|PubMed:14664718}.
-!- SUBUNIT: Interacts with AR and RB1. May also interact with other
nuclear hormone receptors such as NR3C1/GR.
{ECO:0000269|PubMed:10702291, ECO:0000269|PubMed:14664718}.
-!- INTERACTION:
O95995:GAS8; NbExp=4; IntAct=EBI-1210429, EBI-1052570;
Q5T619:ZNF648; NbExp=4; IntAct=EBI-1210429, EBI-11985915;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10702291}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9NYW8-1; Sequence=Displayed;
Name=2;
IsoId=Q9NYW8-2; Sequence=VSP_044805, VSP_044806;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in bone, brain, heart, kidney,
liver, lung, pancreas and placenta. {ECO:0000269|PubMed:10702291}.
-!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
family. {ECO:0000305}.
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EMBL; AF226869; AAF43389.1; -; mRNA.
EMBL; BM929719; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AK293069; BAF85758.1; -; mRNA.
EMBL; AC092032; AAQ93364.1; -; Genomic_DNA.
EMBL; AC008167; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471144; EAW87321.1; -; Genomic_DNA.
EMBL; BC136675; AAI36676.1; -; mRNA.
EMBL; BC136676; AAI36677.1; -; mRNA.
CCDS; CCDS5337.1; -. [Q9NYW8-1]
RefSeq; NP_001191385.1; NM_001204456.1. [Q9NYW8-1]
RefSeq; NP_066986.1; NM_021163.3. [Q9NYW8-1]
UniGene; Hs.396178; -.
ProteinModelPortal; Q9NYW8; -.
SMR; Q9NYW8; -.
BioGrid; 121759; 14.
DIP; DIP-39336N; -.
IntAct; Q9NYW8; 30.
STRING; 9606.ENSP00000275423; -.
iPTMnet; Q9NYW8; -.
PhosphoSitePlus; Q9NYW8; -.
BioMuta; RBAK; -.
DMDM; 74761820; -.
EPD; Q9NYW8; -.
MaxQB; Q9NYW8; -.
PaxDb; Q9NYW8; -.
PeptideAtlas; Q9NYW8; -.
PRIDE; Q9NYW8; -.
Ensembl; ENST00000353796; ENSP00000275423; ENSG00000146587. [Q9NYW8-1]
Ensembl; ENST00000396912; ENSP00000380120; ENSG00000146587. [Q9NYW8-1]
GeneID; 57786; -.
KEGG; hsa:57786; -.
UCSC; uc003sns.1; human. [Q9NYW8-1]
CTD; 57786; -.
DisGeNET; 57786; -.
EuPathDB; HostDB:ENSG00000146587.17; -.
GeneCards; RBAK; -.
HGNC; HGNC:17680; RBAK.
HPA; HPA071231; -.
MIM; 608191; gene.
neXtProt; NX_Q9NYW8; -.
OpenTargets; ENSG00000146587; -.
PharmGKB; PA162400745; -.
eggNOG; KOG1721; Eukaryota.
eggNOG; COG5048; LUCA.
GeneTree; ENSGT00900000140826; -.
GeneTree; ENSGT00900000141000; -.
HOGENOM; HOG000234617; -.
HOVERGEN; HBG018163; -.
InParanoid; Q9NYW8; -.
KO; K09228; -.
OMA; LTIHYRS; -.
OrthoDB; EOG091G02KC; -.
PhylomeDB; Q9NYW8; -.
TreeFam; TF350803; -.
GenomeRNAi; 57786; -.
PRO; PR:Q9NYW8; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000146587; -.
CleanEx; HS_RBAK; -.
Genevisible; Q9NYW8; HS.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; TAS:UniProtKB.
GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
GO; GO:0008270; F:zinc ion binding; NAS:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; TAS:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd07765; KRAB_A-box; 1.
Gene3D; 3.30.40.10; -; 4.
InterPro; IPR001909; KRAB.
InterPro; IPR036051; KRAB_dom_sf.
InterPro; IPR036236; Znf_C2H2_sf.
InterPro; IPR013087; Znf_C2H2_type.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
Pfam; PF01352; KRAB; 1.
SMART; SM00349; KRAB; 1.
SMART; SM00355; ZnF_C2H2; 16.
SUPFAM; SSF109640; SSF109640; 1.
SUPFAM; SSF57667; SSF57667; 10.
PROSITE; PS50805; KRAB; 1.
PROSITE; PS00028; ZINC_FINGER_C2H2_1; 14.
PROSITE; PS50157; ZINC_FINGER_C2H2_2; 15.
1: Evidence at protein level;
Activator; Alternative splicing; Complete proteome; Isopeptide bond;
Metal-binding; Nucleus; Polymorphism; Reference proteome; Repeat;
Repressor; Transcription; Transcription regulation; Ubl conjugation;
Zinc; Zinc-finger.
CHAIN 1 714 RB-associated KRAB zinc finger protein.
/FTId=PRO_0000316976.
DOMAIN 8 79 KRAB. {ECO:0000255|PROSITE-
ProRule:PRU00119}.
ZN_FING 261 283 C2H2-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 289 311 C2H2-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 317 339 C2H2-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 345 367 C2H2-type 4. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 373 395 C2H2-type 5. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 401 423 C2H2-type 6. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 429 451 C2H2-type 7. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 457 479 C2H2-type 8. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 485 505 C2H2-type 9. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 511 533 C2H2-type 10; degenerate.
{ECO:0000255|PROSITE-ProRule:PRU00042}.
ZN_FING 539 561 C2H2-type 11. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 567 589 C2H2-type 12. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 595 617 C2H2-type 13. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 623 645 C2H2-type 14. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 651 673 C2H2-type 15. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 679 701 C2H2-type 16. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
REGION 171 260 Required for interaction with RB1.
{ECO:0000269|PubMed:10702291}.
REGION 417 714 Interaction with AR.
{ECO:0000269|PubMed:14664718}.
CROSSLNK 97 97 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 259 259 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 315 315 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 357 357 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 534 534 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 537 537 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 80 113 EAWRVDDLIERIQENEDKHSRQAACINSKTLTEE -> AAL
PAGHVAPAVAAAAAAPGRPGPHRQSRSPPGC (in
isoform 2). {ECO:0000303|PubMed:8889548}.
/FTId=VSP_044805.
VAR_SEQ 114 714 Missing (in isoform 2).
{ECO:0000303|PubMed:8889548}.
/FTId=VSP_044806.
VARIANT 229 229 G -> E (in dbSNP:rs35352738).
/FTId=VAR_038438.
CONFLICT 273 273 K -> E (in Ref. 3; BAF85758).
{ECO:0000305}.
SEQUENCE 714 AA; 82995 MW; 36D90A6206118F8B CRC64;
MNTLQGPVSF KDVAVDFTQE EWQQLDPDEK ITYRDVMLEN YSHLVSVGYD TTKPNVIIKL
EQGEEPWIMG GEFPCQHSPE AWRVDDLIER IQENEDKHSR QAACINSKTL TEEKENTFSQ
IYMETSLVPS SIIAHNCVSC GKNLESISQL ISSDGSYART KPDECNECGK TYHGEKMCEF
NQNGDTYSHN EENILQKISI LEKPFEYNEC MEALDNEAVF IAHKRAYIGE KPYEWNDSGP
DFIQMSNFNA YQRSQMEMKP FECSECGKSF CKKSKFIIHQ RAHTGEKPYE CNVCGKSFSQ
KGTLTVHRRS HLEEKPYKCN ECGKTFCQKL HLTQHLRTHS GEKPYECSEC GKTFCQKTHL
TLHQRNHSGE RPYPCNECGK SFSRKSALSD HQRTHTGEKL YKCNECGKSY YRKSTLITHQ
RTHTGEKPYQ CSECGKFFSR VSYLTIHYRS HLEEKPYECN ECGKTFNLNS AFIRHRKVHT
EEKSHECSEC GKFSQLYLTD HHTAHLEEKP YECNECGKTF LVNSAFDGHQ PLPKGEKSYE
CNVCGKLFNE LSYYTEHYRS HSEEKPYGCS ECGKTFSHNS SLFRHQRVHT GEKPYECYEC
GKFFSQKSYL TIHHRIHSGE KPYECSKCGK VFSRMSNLTV HYRSHSGEKP YECNECGKVF
SQKSYLTVHY RTHSGEKPYE CNECGKKFHH RSAFNSHQRI HRRGNMNVLD VENL


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EIAAB47504 Homo sapiens,Human,KIAA1962,Zinc finger protein 483,Zinc finger protein with KRAB and SCAN domains 16,ZKSCAN16,ZNF483
EIAAB47297 Homo sapiens,Human,Zinc finger protein 197,Zinc finger protein with KRAB and SCAN domains 9,ZKSCAN9,ZNF166,ZNF197,ZnF20
EIAAB47196 Homo sapiens,Human,KIAA1015,ZFP95,Zfp-95,Zinc finger protein 95 homolog,Zinc finger protein with KRAB and SCAN domains 5,ZKSCAN5
EIAAB47192 Homo sapiens,Human,Zinc finger protein 694,Zinc finger protein with KRAB and SCAN domains 2,ZKSCAN2,ZNF694
EIAAB47516 Homo sapiens,Human,Zinc finger protein 496,Zinc finger protein with KRAB and SCAN domains 17,ZKSCAN17,ZNF496
EIAAB47294 Homo sapiens,Human,LD5-1,Zinc finger protein 192,Zinc finger protein with KRAB and SCAN domains 8,ZKSCAN8,ZNF192


 

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