ZFP91_HUMAN
ID ZFP91_HUMAN Reviewed; 570 AA.
AC Q96JP5; A6NHC4; A8MSG7; Q86V47; Q96JP4; Q96QA3;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=E3 ubiquitin-protein ligase ZFP91;
DE EC=2.3.2.27;
DE AltName: Full=RING-type E3 ubiquitin transferase ZFP91;
DE AltName: Full=Zinc finger protein 757;
DE AltName: Full=Zinc finger protein 91 homolog;
DE Short=Zfp-91;
GN Name=ZFP91; Synonyms=ZNF757; ORFNames=FKSG11;
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 [MRNA] (ISOFORMS 1 AND 2), FUNCTION, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Leukocyte;
RX PubMed=12738986;
RA Unoki M., Okutsu J., Nakamura Y.;
RT "Identification of a novel human gene, ZFP91, involved in acute myelogenous
RT leukemia.";
RL Int. J. Oncol. 22:1217-1223(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ILE-37.
RC TISSUE=Testis;
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 [5]
RP PROTEIN SEQUENCE OF 2-23, CLEAVAGE OF INITIATOR METHIONINE, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 67-570 (ISOFORM 1), AND VARIANT GLY-207.
RA Wang Y.-G.;
RT "Identification of FKSG11, a novel gene related to breast cancer.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, INTERACTION WITH MAP3K14, AND MUTAGENESIS OF CYS-344 AND CYS-349.
RX PubMed=20682767; DOI=10.1074/jbc.m110.129551;
RA Jin X., Jin H.R., Jung H.S., Lee S.J., Lee J.H., Lee J.J.;
RT "An atypical E3 ligase zinc finger protein 91 stabilizes and activates NF-
RT kappaB-inducing kinase via Lys63-linked ubiquitination.";
RL J. Biol. Chem. 285:30539-30547(2010).
RN [8]
RP STRUCTURE BY NMR OF 370-456 IN COMPLEX WITH ZINC IONS.
RG Northeast structural genomics consortium (NESG);
RT "Solution structure of HR7784A.";
RL Submitted (JUL-2013) to the PDB data bank.
CC -!- FUNCTION: Atypical E3 ubiquitin-protein ligase that mediates 'Lys-63'-
CC linked ubiquitination of MAP3K14/NIK, leading to stabilize and activate
CC MAP3K14/NIK. It thereby acts as an activator of the non-canonical NF-
CC kappa-B2/NFKB2 pathway. May also play an important role in cell
CC proliferation and/or anti-apoptosis. {ECO:0000269|PubMed:12738986,
CC ECO:0000269|PubMed:20682767}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with MAP3K14/NIK. {ECO:0000269|PubMed:20682767,
CC ECO:0000269|Ref.8}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12738986}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96JP5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96JP5-2; Sequence=VSP_012686, VSP_012687;
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously, particularly at high level
CC in testis. Isoform 2 is testis specific.
CC -!- MISCELLANEOUS: In contrast to other E3 ubiquitin-protein ligase, does
CC not contain any domain (RING-type zinc finger or HECT domain) known to
CC mediate E3 ligase activity.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL09963.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB056107; BAB63373.1; -; mRNA.
DR EMBL; AB057443; BAB63374.1; -; mRNA.
DR EMBL; AP001350; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471076; EAW73811.1; -; Genomic_DNA.
DR EMBL; BC051743; AAH51743.1; -; mRNA.
DR EMBL; AF310246; AAL09963.1; ALT_FRAME; mRNA.
DR CCDS; CCDS31553.1; -. [Q96JP5-1]
DR RefSeq; NP_001183980.1; NM_001197051.1.
DR RefSeq; NP_444251.1; NM_053023.4. [Q96JP5-1]
DR PDB; 2M9A; NMR; -; A=370-456.
DR PDBsum; 2M9A; -.
DR AlphaFoldDB; Q96JP5; -.
DR SMR; Q96JP5; -.
DR BioGRID; 123322; 115.
DR CORUM; Q96JP5; -.
DR IntAct; Q96JP5; 31.
DR MINT; Q96JP5; -.
DR STRING; 9606.ENSP00000339030; -.
DR ChEMBL; CHEMBL4739701; -.
DR GlyGen; Q96JP5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96JP5; -.
DR PhosphoSitePlus; Q96JP5; -.
DR BioMuta; ZFP91; -.
DR DMDM; 60416377; -.
DR EPD; Q96JP5; -.
DR jPOST; Q96JP5; -.
DR MassIVE; Q96JP5; -.
DR MaxQB; Q96JP5; -.
DR PaxDb; Q96JP5; -.
DR PeptideAtlas; Q96JP5; -.
DR PRIDE; Q96JP5; -.
DR ProteomicsDB; 76999; -. [Q96JP5-1]
DR ProteomicsDB; 77000; -. [Q96JP5-2]
DR Antibodypedia; 14324; 202 antibodies from 24 providers.
DR DNASU; 80829; -.
DR Ensembl; ENST00000316059.7; ENSP00000339030.5; ENSG00000186660.15. [Q96JP5-1]
DR GeneID; 80829; -.
DR KEGG; hsa:80829; -.
DR MANE-Select; ENST00000316059.7; ENSP00000339030.5; NM_053023.5; NP_444251.1.
DR UCSC; uc001nmx.5; human. [Q96JP5-1]
DR CTD; 80829; -.
DR DisGeNET; 80829; -.
DR GeneCards; ZFP91; -.
DR HGNC; HGNC:14983; ZFP91.
DR HPA; ENSG00000186660; Low tissue specificity.
DR MIM; 619289; gene.
DR neXtProt; NX_Q96JP5; -.
DR OpenTargets; ENSG00000186660; -.
DR PharmGKB; PA37955; -.
DR VEuPathDB; HostDB:ENSG00000186660; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000156393; -.
DR HOGENOM; CLU_034557_0_0_1; -.
DR InParanoid; Q96JP5; -.
DR OMA; TYKPHLD; -.
DR PhylomeDB; Q96JP5; -.
DR TreeFam; TF332664; -.
DR PathwayCommons; Q96JP5; -.
DR SignaLink; Q96JP5; -.
DR SIGNOR; Q96JP5; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 80829; 27 hits in 1101 CRISPR screens.
DR ChiTaRS; ZFP91; human.
DR GeneWiki; ZFP91; -.
DR GenomeRNAi; 80829; -.
DR Pharos; Q96JP5; Tbio.
DR PRO; PR:Q96JP5; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q96JP5; protein.
DR Bgee; ENSG00000186660; Expressed in tibialis anterior and 195 other tissues.
DR ExpressionAtlas; Q96JP5; baseline and differential.
DR Genevisible; Q96JP5; HS.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR GO; GO:0007250; P:activation of NF-kappaB-inducing kinase activity; IDA:UniProtKB.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; IDA:UniProtKB.
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; 3.
DR SMART; SM00355; ZnF_C2H2; 5.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Direct protein sequencing;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.5"
FT CHAIN 2..570
FT /note="E3 ubiquitin-protein ligase ZFP91"
FT /id="PRO_0000047312"
FT ZN_FING 311..336
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 342..366
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 372..394
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 400..422
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 430..453
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..368
FT /note="Interaction with MAP3K14/NIK"
FT /evidence="ECO:0000269|PubMed:20682767"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..222
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..271
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..306
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62511"
FT MOD_RES 103
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62511"
FT VAR_SEQ 526..529
FT /note="VSLM -> SIHR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12738986"
FT /id="VSP_012686"
FT VAR_SEQ 530..570
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12738986"
FT /id="VSP_012687"
FT VARIANT 37
FT /note="V -> I (in dbSNP:rs17854702)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_032454"
FT VARIANT 207
FT /note="S -> G (in dbSNP:rs8373)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_021889"
FT MUTAGEN 344
FT /note="C->A: Abolishes ubiquitination of MAP3K14/NIK; when
FT associated with A-349."
FT /evidence="ECO:0000269|PubMed:20682767"
FT MUTAGEN 349
FT /note="C->A: Abolishes ubiquitination of MAP3K14/NIK; when
FT associated with A-344."
FT /evidence="ECO:0000269|PubMed:20682767"
FT CONFLICT 74
FT /note="A -> V (in Ref. 6; AAL09963)"
FT /evidence="ECO:0000305"
FT CONFLICT 206
FT /note="Missing (in Ref. 4; AAH51743)"
FT /evidence="ECO:0000305"
FT STRAND 381..383
FT /evidence="ECO:0007829|PDB:2M9A"
FT HELIX 384..390
FT /evidence="ECO:0007829|PDB:2M9A"
FT HELIX 391..393
FT /evidence="ECO:0007829|PDB:2M9A"
FT STRAND 395..397
FT /evidence="ECO:0007829|PDB:2M9A"
FT STRAND 408..411
FT /evidence="ECO:0007829|PDB:2M9A"
FT HELIX 412..423
FT /evidence="ECO:0007829|PDB:2M9A"
FT STRAND 426..429
FT /evidence="ECO:0007829|PDB:2M9A"
FT TURN 433..435
FT /evidence="ECO:0007829|PDB:2M9A"
FT HELIX 442..452
FT /evidence="ECO:0007829|PDB:2M9A"
SQ SEQUENCE 570 AA; 63445 MW; 476F4C21DD453522 CRC64;
MPGETEEPRP PEQQDQEGGE AAKAAPEEPQ QRPPEAVAAA PAGTTSSRVL RGGRDRGRAA
AAAAAAAVSR RRKAEYPRRR RSSPSARPPD VPGQQPQAAK SPSPVQGKKS PRLLCIEKVT
TDKDPKEEKE EEDDSALPQE VSIAASRPSR GWRSSRTSVS RHRDTENTRS SRSKTGSLQL
ICKSEPNTDQ LDYDVGEEHQ SPGGISSEEE EEEEEEMLIS EEEIPFKDDP RDETYKPHLE
RETPKPRRKS GKVKEEKEKK EIKVEVEVEV KEEENEIRED EEPPRKRGRR RKDDKSPRLP
KRRKKPPIQY VRCEMEGCGT VLAHPRYLQH HIKYQHLLKK KYVCPHPSCG RLFRLQKQLL
RHAKHHTDQR DYICEYCARA FKSSHNLAVH RMIHTGEKPL QCEICGFTCR QKASLNWHMK
KHDADSFYQF SCNICGKKFE KKDSVVAHKA KSHPEVLIAE ALAANAGALI TSTDILGTNP
ESLTQPSDGQ GLPLLPEPLG NSTSGECLLL EAEGMSKSYC SGTERVSLMA DGKIFVGSGS
SGGTEGLVMN SDILGATTEV LIEDSDSAGP
