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   05-OCT-2010, entry version 78.
DE   RecName: Full=E3 ubiquitin-protein ligase ZFP91;
DE            EC=6.3.2.-;
DE   AltName: Full=Zinc finger protein 91 homolog;
DE            Short=Zfp-91;
GN   Name=ZFP91; ORFNames=FKSG11;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, AND
RP   SUBCELLULAR LOCATION.
RC   TISSUE=Leukocyte;
RX   MEDLINE=22623614; PubMed=12738986;
RA   Unoki M., Okutsu J., Nakamura Y.;
RT   "Identification of a novel human gene, ZFP91, involved in acute
RT   myelogenous 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.,
RA   Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA   FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA   Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA   Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA   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.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   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
RP   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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 2-23, CLEAVAGE OF INITIATOR METHIONINE, LACK OF
RP   N-TERMINAL ACETYLATION, AND 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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=15302935; DOI=10.1073/pnas.0404720101;
RA   Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,
RA   Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
RT   "Large-scale characterization of HeLa cell nuclear phosphoproteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82 AND SER-83, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling networks.";
RL   Cell 127:635-648(2006).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-395, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RA   Colinge J., Superti-Furga G., Bennett K.L.;
RL   Submitted (OCT-2008) to UniProtKB.
RN   [11]
RP   FUNCTION, INTERACTION WITH MAP3K14, AND MUTAGENESIS OF CYS-344 AND
RP   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
RT   NF-{kappa}B-inducing kinase via K63-linked ubiquitination.";
RL   J. Biol. Chem. 0:0-0(2010).
CC   -!- FUNCTION: Atypical E3 ubiquitin-protein ligase that mediates 'Lys-
CC       63'-linked ubiquitination of MAP3K14/NIK, leading to stabilize and
CC       activate MAP3K14/NIK. It thereby acts as an activator of the non-
CC       canonical NF-kappa-B2/NFKB2 pathway. May also play an important
CC       role in cell proliferation and/or anti-apoptosis.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with MAP3K14/NIK.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
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
CC       level in testis. Isoform 2 is testis specific.
CC   -!- MISCELLANEOUS: In contrast to other E3 ubiquitin-protein ligase,
CC       does not contain any domain (RING-type zinc finger or HECT domain)
CC       known to mediate E3 ligase activity.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family.
CC   -!- SIMILARITY: Contains 5 C2H2-type zinc fingers.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL09963.1; Type=Frameshift; Positions=72, 80;
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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   IPI; IPI00172474; -.
DR   IPI; IPI00477661; -.
DR   RefSeq; NP_444251.1; -.
DR   UniGene; Hs.524920; -.
DR   ProteinModelPortal; Q96JP5; -.
DR   SMR; Q96JP5; 311-381, 314-453, 395-459.
DR   IntAct; Q96JP5; 2.
DR   STRING; Q96JP5; -.
DR   PhosphoSite; Q96JP5; -.
DR   PRIDE; Q96JP5; -.
DR   Ensembl; ENST00000316059; ENSP00000339030; ENSG00000186660.
DR   GeneID; 80829; -.
DR   KEGG; hsa:80829; -.
DR   UCSC; uc001nmx.2; human.
DR   UCSC; uc001nmz.2; human.
DR   CTD; 80829; -.
DR   GeneCards; GC11P058347; -.
DR   HGNC; HGNC:14983; ZFP91.
DR   HPA; CAB025417; -.
DR   HPA; HPA024037; -.
DR   PharmGKB; PA37955; -.
DR   eggNOG; prNOG10456; -.
DR   HOGENOM; HBG282653; -.
DR   HOVERGEN; HBG055547; -.
DR   InParanoid; Q96JP5; -.
DR   OMA; VAEEHQS; -.
DR   OrthoDB; EOG9QZB56; -.
DR   NextBio; 100936; -.
DR   ArrayExpress; Q96JP5; -.
DR   Bgee; Q96JP5; -.
DR   CleanEx; HS_ZFP91; -.
DR   Genevestigator; Q96JP5; -.
DR   GermOnline; ENSG00000186660; Homo sapiens.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004842; F:ubiquitin-protein ligase activity; IDA:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0007250; P:activation of NF-kappaB-inducing kinase act...; IDA:UniProtKB.
DR   GO; GO:0070534; P:protein K63-linked ubiquitination; IDA:UniProtKB.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   SMART; SM00355; ZnF_C2H2; 5.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE   1: Evidence at protein level;
KW   Alternative splicing; Complete proteome; Direct protein sequencing;
KW   Ligase; Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Repeat;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    570       E3 ubiquitin-protein ligase ZFP91.
FT                                /FTId=PRO_0000047312.
FT   ZN_FING     311    336       C2H2-type 1.
FT   ZN_FING     342    366       C2H2-type 2.
FT   ZN_FING     372    394       C2H2-type 3.
FT   ZN_FING     400    422       C2H2-type 4.
FT   ZN_FING     430    453       C2H2-type 5.
FT   REGION      338    368       Interaction with MAP3K14/NIK.
FT   COMPBIAS     21     67       Ala-rich.
FT   COMPBIAS     48     81       Arg-rich.
FT   COMPBIAS    197    282       Glu-rich.
FT   MOD_RES      82     82       Phosphoserine.
FT   MOD_RES      83     83       Phosphoserine.
FT   MOD_RES     103    103       Phosphoserine.
FT   MOD_RES     395    395       Phosphothreonine.
FT   VAR_SEQ     526    529       VSLM -> SIHR (in isoform 2).
FT                                /FTId=VSP_012686.
FT   VAR_SEQ     530    570       Missing (in isoform 2).
FT                                /FTId=VSP_012687.
FT   VARIANT      37     37       V -> I (in dbSNP:rs17854702).
FT                                /FTId=VAR_032454.
FT   VARIANT     207    207       S -> G (in dbSNP:rs8373).
FT                                /FTId=VAR_021889.
FT   MUTAGEN     344    344       C->A: Abolishes ubiquitination of
FT                                MAP3K14/NIK; when associated with A-349.
FT   MUTAGEN     349    349       C->A: Abolishes ubiquitination of
FT                                MAP3K14/NIK; when associated with A-344.
FT   CONFLICT     74     74       A -> V (in Ref. 6; AAL09963).
FT   CONFLICT    206    206       Missing (in Ref. 4; AAH51743).
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
//