ZFP91_MOUSE
ID ZFP91_MOUSE Reviewed; 572 AA.
AC Q62511; Q3TEQ3; Q3UH61; Q62509; Q6P219; Q6PG06; Q8BPY3; Q8C2B4; Q8CDZ3;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 3.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=E3 ubiquitin-protein ligase ZFP91;
DE EC=2.3.2.27;
DE AltName: Full=Penta Zf protein;
DE AltName: Full=RING-type E3 ubiquitin transferase ZFP91;
DE AltName: Full=Zinc finger protein 91 homolog;
DE Short=Zfp-91;
DE AltName: Full=Zinc finger protein PZF;
GN Name=Zfp91; Synonyms=Pzf;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Brain, and Testis;
RX PubMed=7835706; DOI=10.1016/0378-1119(94)00717-7;
RA Saotome Y., Winter C.G., Hirsh D.;
RT "A widely expressed novel C2H2 zinc-finger protein with multiple consensus
RT phosphorylation sites is conserved in mouse and man.";
RL Gene 152:233-238(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Eye, Head, Placenta, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 252-572.
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, Colon, and Embryo;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86 AND SER-106, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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:0000250}.
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:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q62511-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q62511-2; Sequence=VSP_025759, VSP_025760;
CC -!- TISSUE SPECIFICITY: Found in all the examined tissues including brain,
CC heart, kidney, lung, liver, spleen, thymus, skeletal muscle, ovary and
CC testis. {ECO:0000269|PubMed:7835706}.
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=BAC26394.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC34808.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC40660.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U05342; AAA81911.1; -; mRNA.
DR EMBL; U05343; AAA81913.1; -; mRNA.
DR EMBL; AK029319; BAC26394.1; ALT_FRAME; mRNA.
DR EMBL; AK051904; BAC34808.1; ALT_INIT; mRNA.
DR EMBL; AK088933; BAC40660.1; ALT_FRAME; mRNA.
DR EMBL; AK147502; BAE27956.1; -; mRNA.
DR EMBL; AK147560; BAE27996.1; -; mRNA.
DR EMBL; AK169477; BAE41195.1; -; mRNA.
DR EMBL; BC057323; AAH57323.1; -; mRNA.
DR EMBL; BC064766; AAH64766.1; -; mRNA.
DR EMBL; BC083000; AAH83000.1; -; mRNA.
DR CCDS; CCDS37927.1; -. [Q62511-1]
DR PIR; I48722; I48722.
DR PIR; I48724; I48724.
DR RefSeq; NP_443735.2; NM_053009.3. [Q62511-1]
DR AlphaFoldDB; Q62511; -.
DR SMR; Q62511; -.
DR BioGRID; 225146; 2.
DR STRING; 10090.ENSMUSP00000037971; -.
DR iPTMnet; Q62511; -.
DR PhosphoSitePlus; Q62511; -.
DR jPOST; Q62511; -.
DR MaxQB; Q62511; -.
DR PaxDb; Q62511; -.
DR PeptideAtlas; Q62511; -.
DR PRIDE; Q62511; -.
DR ProteomicsDB; 275363; -. [Q62511-1]
DR ProteomicsDB; 275364; -. [Q62511-2]
DR DNASU; 109910; -.
DR Ensembl; ENSMUST00000038627; ENSMUSP00000037971; ENSMUSG00000024695. [Q62511-1]
DR GeneID; 109910; -.
DR KEGG; mmu:109910; -.
DR UCSC; uc008gup.2; mouse. [Q62511-1]
DR CTD; 80829; -.
DR MGI; MGI:104854; Zfp91.
DR VEuPathDB; HostDB:ENSMUSG00000024695; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000156393; -.
DR HOGENOM; CLU_034557_0_0_1; -.
DR InParanoid; Q62511; -.
DR OMA; TYKPHLD; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q62511; -.
DR TreeFam; TF332664; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 109910; 4 hits in 73 CRISPR screens.
DR PRO; PR:Q62511; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q62511; protein.
DR Bgee; ENSMUSG00000024695; Expressed in ascending aorta and 262 other tissues.
DR Genevisible; Q62511; MM.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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; ISS:UniProtKB.
DR GO; GO:0007250; P:activation of NF-kappaB-inducing kinase activity; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; 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 Alternative splicing; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..572
FT /note="E3 ubiquitin-protein ligase ZFP91"
FT /id="PRO_0000047313"
FT ZN_FING 313..338
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 344..368
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 374..396
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 402..424
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 432..455
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..370
FT /note="Interaction with MAP3K14/NIK"
FT /evidence="ECO:0000250"
FT COMPBIAS 118..138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..224
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..273
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..308
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..111
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7835706"
FT /id="VSP_025759"
FT VAR_SEQ 112..128
FT /note="KSPRLQCIEKLTTDKDP -> MKTKKECEEDD (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7835706"
FT /id="VSP_025760"
FT CONFLICT 104
FT /note="P -> A (in Ref. 2; BAE41195)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="E -> Q (in Ref. 2; BAC40660)"
FT /evidence="ECO:0000305"
FT CONFLICT 256
FT /note="K -> T (in Ref. 1; AAA81911/AAA81913)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="K -> R (in Ref. 2; BAC40660)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="Q -> E (in Ref. 1; AAA81911)"
FT /evidence="ECO:0000305"
FT CONFLICT 466
FT /note="A -> V (in Ref. 1; AAA81911/AAA81913)"
FT /evidence="ECO:0000305"
FT CONFLICT 498
FT /note="P -> T (in Ref. 2; BAC26394)"
FT /evidence="ECO:0000305"
FT CONFLICT 528..529
FT /note="VS -> LI (in Ref. 1; AAA81911)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 572 AA; 63389 MW; C57D976BA1DC07F4 CRC64;
MPGETEEPRS PEQQDQEGGP AAAADAASEE LRPGAAAAPA APAETASSRV LRGGRDRGRT
AAAAAAAAAA VSRRRKAEYP RRRRSSPSNR PPDGPGHQPA AAKPPSPAQG KKSPRLQCIE
KLTTDKDPKE EKEDDSVLPQ EVSITTTRAS RSWRSSSRTS ISRLRDSENT RSSRSKTGSL
QLVCKTEPIT DQLDYDVPEE HQSPGGISSD EEEEEEEEML ISEEEIPFKD DPRDETYKPH
LERETPKPRR KSGKVKEEKE KKEIKVEVEV EVKEEENEIR EDEEPPRKRG RRRKDDKSPR
LPKRRKKPPI QYVRCEMEGC GTVLAHPRYL QHHIKYQHLL KKKYVCPHPS CGRLFRLQKQ
LLRHAKHHTD QRDYICEYCA RAFKSSHNLA VHRMIHTGEK PLQCEICGFT CRQKASLNWH
MKKHDADSFY QFSCNICGKK FEKKDSVVAH KAKSHPEVLI AEALAANAGA LITSTDILGT
NPEPLTQPAD GQGLPLLPEP LGNSTAGECL LLEAEGMSKS YCSGTERVSL MADGKIFVGS
GSSGGTEGLV MNSDILGATT EVLIEDTDST GP
