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UBR7_MOUSE
ID   UBR7_MOUSE              Reviewed;         425 AA.
AC   Q8BU04; Q80UT9;
DT   24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Putative E3 ubiquitin-protein ligase UBR7;
DE            EC=2.3.2.27;
DE   AltName: Full=N-recognin-7;
DE   AltName: Full=RING-type E3 ubiquitin transferase UBR7;
GN   Name=Ubr7;
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 [LARGE SCALE MRNA].
RC   STRAIN=NOD; TISSUE=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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 141-425.
RC   STRAIN=129/Sv X 129/SvCp; TISSUE=Embryonic stem cell;
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   [3]
RP   IDENTIFICATION.
RX   PubMed=16055722; DOI=10.1128/mcb.25.16.7120-7136.2005;
RA   Tasaki T., Mulder L.C.F., Iwamatsu A., Lee M.J., Davydov I.V.,
RA   Varshavsky A., Muesing M., Kwon Y.T.;
RT   "A family of mammalian E3 ubiquitin ligases that contain the UBR box motif
RT   and recognize N-degrons.";
RL   Mol. Cell. Biol. 25:7120-7136(2005).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Spleen, and Testis;
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).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=24664117; DOI=10.1007/s00441-014-1808-x;
RA   Zimmerman S.W., Yi Y.J., Sutovsky M., van Leeuwen F.W., Conant G.,
RA   Sutovsky P.;
RT   "Identification and characterization of RING-finger ubiquitin ligase UBR7
RT   in mammalian spermatozoa.";
RL   Cell Tissue Res. 356:261-278(2014).
CC   -!- FUNCTION: E3 ubiquitin-protein ligase which is a component of the N-end
CC       rule pathway. Recognizes and binds to proteins bearing specific N-
CC       terminal residues that are destabilizing according to the N-end rule,
CC       leading to their ubiquitination and subsequent degradation.
CC       {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   -!- TISSUE SPECIFICITY: Expressed in testis and sperm (at protein level).
CC       {ECO:0000269|PubMed:24664117}.
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DR   EMBL; AK088208; BAC40212.1; -; mRNA.
DR   EMBL; BC051678; AAH51678.1; -; mRNA.
DR   CCDS; CCDS26124.1; -.
DR   RefSeq; NP_079942.1; NM_025666.2.
DR   AlphaFoldDB; Q8BU04; -.
DR   BioGRID; 211602; 1.
DR   STRING; 10090.ENSMUSP00000041247; -.
DR   iPTMnet; Q8BU04; -.
DR   PhosphoSitePlus; Q8BU04; -.
DR   EPD; Q8BU04; -.
DR   jPOST; Q8BU04; -.
DR   MaxQB; Q8BU04; -.
DR   PaxDb; Q8BU04; -.
DR   PRIDE; Q8BU04; -.
DR   ProteomicsDB; 298112; -.
DR   DNASU; 66622; -.
DR   Ensembl; ENSMUST00000046404; ENSMUSP00000041247; ENSMUSG00000041712.
DR   GeneID; 66622; -.
DR   KEGG; mmu:66622; -.
DR   UCSC; uc007ouo.1; mouse.
DR   CTD; 55148; -.
DR   MGI; MGI:1913872; Ubr7.
DR   VEuPathDB; HostDB:ENSMUSG00000041712; -.
DR   eggNOG; KOG2752; Eukaryota.
DR   GeneTree; ENSGT00390000017610; -.
DR   HOGENOM; CLU_025221_0_0_1; -.
DR   InParanoid; Q8BU04; -.
DR   OMA; GQPYFCR; -.
DR   OrthoDB; 1428122at2759; -.
DR   PhylomeDB; Q8BU04; -.
DR   TreeFam; TF105941; -.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 66622; 3 hits in 76 CRISPR screens.
DR   ChiTaRS; Ubr7; mouse.
DR   PRO; PR:Q8BU04; -.
DR   Proteomes; UP000000589; Chromosome 12.
DR   RNAct; Q8BU04; protein.
DR   Bgee; ENSMUSG00000041712; Expressed in saccule of membranous labyrinth and 261 other tissues.
DR   ExpressionAtlas; Q8BU04; baseline and differential.
DR   Genevisible; Q8BU04; MM.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR040204; UBR7.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR003126; Znf_UBR.
DR   PANTHER; PTHR13513; PTHR13513; 1.
DR   Pfam; PF02207; zf-UBR; 1.
DR   SMART; SM00396; ZnF_UBR1; 1.
DR   SUPFAM; SSF57903; SSF57903; 1.
DR   PROSITE; PS51157; ZF_UBR; 1.
PE   1: Evidence at protein level;
KW   Isopeptide bond; Metal-binding; Phosphoprotein; Reference proteome;
KW   Transferase; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN           1..425
FT                   /note="Putative E3 ubiquitin-protein ligase UBR7"
FT                   /id="PRO_0000089933"
FT   ZN_FING         44..116
FT                   /note="UBR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00508"
FT   ZN_FING         132..188
FT                   /note="PHD-type; atypical"
FT   REGION          212..269
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        236..253
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        254..269
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         264
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N806"
FT   CROSSLNK        225
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N806"
FT   CROSSLNK        252
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N806"
FT   CROSSLNK        274
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N806"
FT   CROSSLNK        398
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N806"
SQ   SEQUENCE   425 AA;  48065 MW;  59CACAA047B60321 CRC64;
     MAGAESPTEC QAELEPVVSL VDVLEEDEEL ENEACAVLGG SDSEKCSYSQ GSVGRQALYA
     CSTCTPEGEE PAGICLACSY ECHGSHKLFE LYTKRNFRCD CGNSKFKNLE CKLFPDKSKV
     NSCNKYNDNF FGLYCVCKRP YPDPEDEVPD EMIQCVVCED WFHGRHLGAI PPESGDFQEM
     VCQACMRRCS FLWAYAAQLA VTRISAEDDG LLPNATGMGD EDVSKPENGA PQDNGLKEDA
     PEHGRDSVNE VKAEQKNEPC SSSSSESDLQ TVFKKENIKT EPQSSCRLQE LQAKQFVKKD
     AATYWPLNWR SKLCTCQDCM KMYGELDVLF LTDECDTVLA YENKGKNDQA TDRRDPLMDT
     LSSMNRVQQV ELICEYNDLK TELKDYLKRF ADEGTVVKRE DIQQFFEEFQ SKKRRRVDGL
     QYYCS
 
 
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