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TRI75_HUMAN
ID   TRI75_HUMAN             Reviewed;         468 AA.
AC   A6NK02;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 2.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Tripartite motif-containing protein 75 {ECO:0000305};
GN   Name=TRIM75 {ECO:0000312|HGNC:HGNC:32686}; Synonyms=TRIM75P;
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=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
CC   -!- FUNCTION: May play a role in female meiosis.
CC       {ECO:0000250|UniProtKB:Q3UWZ0}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle
CC       {ECO:0000250|UniProtKB:Q3UWZ0}.
CC   -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR   EMBL; AC108465; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A6NK02; -.
DR   SMR; A6NK02; -.
DR   iPTMnet; A6NK02; -.
DR   PhosphoSitePlus; A6NK02; -.
DR   BioMuta; TRIM75P; -.
DR   jPOST; A6NK02; -.
DR   MassIVE; A6NK02; -.
DR   PeptideAtlas; A6NK02; -.
DR   PRIDE; A6NK02; -.
DR   Antibodypedia; 82480; 1 antibodies from 1 providers.
DR   Ensembl; ENST00000503032.2; ENSP00000491320.1; ENSG00000250374.4.
DR   MANE-Select; ENST00000503032.3; ENSP00000491320.1; NM_001396070.1; NP_001382999.1.
DR   GeneCards; TRIM75P; -.
DR   HGNC; HGNC:32686; TRIM75.
DR   HPA; ENSG00000250374; Not detected.
DR   neXtProt; NX_A6NK02; -.
DR   OpenTargets; ENSG00000250374; -.
DR   VEuPathDB; HostDB:ENSG00000250374; -.
DR   GeneTree; ENSGT00940000162839; -.
DR   InParanoid; A6NK02; -.
DR   OMA; CVRFTKR; -.
DR   PhylomeDB; A6NK02; -.
DR   Pharos; A6NK02; Tdark.
DR   PRO; PR:A6NK02; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   RNAct; A6NK02; protein.
DR   Bgee; ENSG00000250374; Expressed in placenta and 5 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR   GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0007144; P:female meiosis I; ISS:UniProtKB.
DR   GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR   GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR   GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR   CDD; cd15829; SPRY_PRY_TRIM75; 1.
DR   Gene3D; 2.60.120.920; -; 1.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR001870; B30.2/SPRY.
DR   InterPro; IPR043136; B30.2/SPRY_sf.
DR   InterPro; IPR003879; Butyrophylin_SPRY.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR006574; PRY.
DR   InterPro; IPR035785; SPRY/PRY_TRIM75.
DR   InterPro; IPR003877; SPRY_dom.
DR   InterPro; IPR000315; Znf_B-box.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   Pfam; PF13765; PRY; 1.
DR   Pfam; PF00622; SPRY; 1.
DR   Pfam; PF00643; zf-B_box; 1.
DR   PRINTS; PR01407; BUTYPHLNCDUF.
DR   SMART; SM00336; BBOX; 1.
DR   SMART; SM00589; PRY; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00449; SPRY; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   PROSITE; PS50188; B302_SPRY; 1.
DR   PROSITE; PS50119; ZF_BBOX; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Cytoplasm; Cytoskeleton; Metal-binding; Reference proteome;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..468
FT                   /note="Tripartite motif-containing protein 75"
FT                   /id="PRO_0000331192"
FT   DOMAIN          276..468
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT   ZN_FING         16..57
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   ZN_FING         92..133
FT                   /note="B box-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   COILED          170..222
FT                   /evidence="ECO:0000255"
FT   BINDING         97
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         100
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         119
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         125
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
SQ   SEQUENCE   468 AA;  53678 MW;  793C2F1E8EEB2BF9 CRC64;
     MAVAAALTGL QAEAKCSICL DYLSDPVTIE CGHNFCRSCI QQSWLDLQEL FPCPVCRHQC
     QEGHFRSNTQ LGRMIEIAKL LQSTKSNKRK QEETTLCEKH NQPLSVFCKE DLMVLCPLCT
     QPPDHQGHHV RPIEKAAIHY RKRFCSYIQP LKKQLADLQK LISTQSKKPL ELREMVENQR
     QELSSEFEHL NQFLDREQQA VLSRLAEEEK DNQQKLSANI TAFSNYSATL KSQLSKVVEL
     SELSELELLS QIKIFYESEN ESSPSIFSIH LKRDGCSFPP QYSALQRIIK KFKVEIILDP
     ETAHPNLIVS EDKKRVRFTK RKQKVPGFPK RFTVKPVVLG FPYFHSGRHF WEIEVGDKSE
     WAIGICKDSL PTKARRPSSA QQECWRIELQ DDGYHAPGAF PTPLLLEVKA RAIGIFLDYE
     MGEISFYNMA EKSHICTFTD TFTGPLRPYF YVGPDSQPLR ICTGTVCE
 
 
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