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PRAM9_HUMAN
ID   PRAM9_HUMAN             Reviewed;         478 AA.
AC   P0DUQ2; B2RPE1; Q08EQ1; Q5VWM5;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   29-SEP-2021, sequence version 1.
DT   03-AUG-2022, entry version 4.
DE   RecName: Full=PRAME family member 9 {ECO:0000305};
GN   Name=PRAMEF9 {ECO:0000303|PubMed:26138980, ECO:0000312|HGNC:HGNC:27996};
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 [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [2]
RP   FUNCTION, PATHWAY, AND IDENTIFICATION IN A CRL2 E3 UBIQUITIN-PROTEIN LIGASE
RP   COMPLEX.
RX   PubMed=26138980; DOI=10.1126/science.aab0515;
RA   Lin H.C., Ho S.C., Chen Y.Y., Khoo K.H., Hsu P.H., Yen H.C.;
RT   "SELENOPROTEINS. CRL2 aids elimination of truncated selenoproteins produced
RT   by failed UGA/Sec decoding.";
RL   Science 349:91-95(2015).
CC   -!- FUNCTION: Substrate-recognition component of a Cul2-RING (CRL2) E3
CC       ubiquitin-protein ligase complex, which mediates ubiquitination of
CC       target proteins, leading to their degradation (PubMed:26138980). The
CC       CRL2(PRAMEF9) complex mediates ubiquitination and degradation of
CC       truncated MSRB1/SEPX1 selenoproteins produced by failed UGA/Sec
CC       decoding (PubMed:26138980). {ECO:0000269|PubMed:26138980}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000269|PubMed:26138980}.
CC   -!- SUBUNIT: Component of a CRL2 E3 ubiquitin-protein ligase complex, also
CC       named ECS (Elongin BC-CUL2/5-SOCS-box protein) complex, composed of
CC       CUL2, Elongin BC (ELOB and ELOC), RBX1 and substrate-specific adapter
CC       PRAMEF9. {ECO:0000269|PubMed:26138980}.
CC   -!- SIMILARITY: Belongs to the PRAME family. {ECO:0000305}.
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DR   EMBL; BX470067; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_001091846.1; NM_001098376.2.
DR   iPTMnet; Q5VWM5; -.
DR   PeptideAtlas; P0DUQ2; -.
DR   GeneID; 653619; -.
DR   KEGG; hsa:653619; -.
DR   MANE-Select; ENST00000376152.2; ENSP00000365322.1; NM_001098376.3; NP_001091846.1.
DR   CTD; 653619; -.
DR   HGNC; HGNC:27996; PRAMEF9.
DR   neXtProt; NX_P0DUQ2; -.
DR   OpenTargets; ENSG00000204501; -.
DR   GeneTree; ENSGT01030000234531; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   Bgee; ENSG00000204501; Expressed in liver and 3 other tissues.
DR   Genevisible; Q5VWM5; HS.
DR   GO; GO:0031462; C:Cul2-RING ubiquitin ligase complex; IDA:UniProtKB.
DR   GO; GO:1990756; F:ubiquitin ligase-substrate adaptor activity; IDA:UniProtKB.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IEA:InterPro.
DR   GO; GO:0045596; P:negative regulation of cell differentiation; IEA:InterPro.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:InterPro.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:InterPro.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.80.10.10; -; 1.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR026271; PRAME_family.
DR   PIRSF; PIRSF038286; PRAME; 1.
PE   1: Evidence at protein level;
KW   Leucine-rich repeat; Reference proteome; Repeat; Ubl conjugation pathway.
FT   CHAIN           1..478
FT                   /note="PRAME family member 9"
FT                   /id="PRO_0000156983"
FT   REPEAT          99..126
FT                   /note="LRR 1; degenerate"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UWY1"
FT   REPEAT          181..205
FT                   /note="LRR 2; degenerate"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UWY1"
FT   REPEAT          206..232
FT                   /note="LRR 3; degenerate"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UWY1"
FT   REPEAT          233..268
FT                   /note="LRR 4; degenerate"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UWY1"
FT   REPEAT          269..294
FT                   /note="LRR 5"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UWY1"
FT   REPEAT          295..326
FT                   /note="LRR 6"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UWY1"
FT   REPEAT          327..347
FT                   /note="LRR 7"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UWY1"
FT   REPEAT          351..378
FT                   /note="LRR 8"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UWY1"
FT   REPEAT          379..403
FT                   /note="LRR 9"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UWY1"
SQ   SEQUENCE   478 AA;  55420 MW;  01C7079F4D65BF10 CRC64;
     MKMSIRTPPR LLELAGRSLL RDQALAMSTL EELPTELFPP LFMEAFSRRR CEALKLMVQA
     WPFRRLPLRP LIKMPCLEAF QAVLDGLDAL LTQGVRPRRW KLQVLDLQDV CENFWMVWSE
     AMAHGCFLNA KRNKKPVQDC PRMRGRQPLT VFVELWLKNR TLDEYLTYLL LWVKQRKDLL
     HLCCKKLKIL GMPFRNIRSI LKMVNLDCIQ EVEVNCKWVL PILTQFTPYL GHMRNLQKLV
     LSHMDVSRYV SPEQKKEIVT QFTTQFLKLR CLQKLYMNSV SFLEGHLDQL LSCLKTSLKV
     LTITNCVLLE SDLKHLSQCP SISQLKTLDL SGIRLTNYSL VPLQILLEKV AATLEYLDLD
     DCGIIDSQVN AILPALSRCF ELNTFSFCGN PICMATLENL LSHTIILKNL CVELYPAPRE
     SYGADGTLCW SRFAQIRAEL MNRVRDLRHP KRILFCTDYC PDCGNRSFYD LEADQYCC
 
 
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