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Database: UniProt
Entry: O75382
LinkDB: O75382
Original site: O75382 
ID   TRIM3_HUMAN             Reviewed;         744 AA.
AC   O75382; B7Z5E6; F5H2Q8; Q4V9L4; Q9C038; Q9C039;
DT   06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 2.
DT   01-OCT-2014, entry version 137.
DE   RecName: Full=Tripartite motif-containing protein 3;
DE   AltName: Full=Brain-expressed RING finger protein;
DE   AltName: Full=RING finger protein 22;
DE   AltName: Full=RING finger protein 97;
GN   Name=TRIM3; Synonyms=BERP, RNF22, RNF97;
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] (ISOFORM ALPHA).
RC   TISSUE=Brain;
RX   PubMed=11170753; DOI=10.1006/geno.2000.6452;
RA   El-Husseini A.E.-D., Fretier P., Vincent S.R.;
RT   "Cloning and characterization of a gene (RNF22) encoding a novel brain
RT   expressed ring finger protein (BERP) that maps to human chromosome
RT   11p15.5.";
RL   Genomics 71:363-367(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA; BETA AND GAMMA).
RX   PubMed=11331580; DOI=10.1093/emboj/20.9.2140;
RA   Reymond A., Meroni G., Fantozzi A., Merla G., Cairo S., Luzi L.,
RA   Riganelli D., Zanaria E., Messali S., Cainarca S., Guffanti A.,
RA   Minucci S., Pelicci P.G., Ballabio A.;
RT   "The tripartite motif family identifies cell compartments.";
RL   EMBO J. 20:2140-2151(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS ALPHA AND 4).
RC   TISSUE=Brain;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
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   [5]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
RC   TISSUE=Cervix;
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   [7]
RP   IDENTIFICATION IN THE CART COMPLEX, AND SUBCELLULAR LOCATION.
RX   PubMed=15772161; DOI=10.1091/mbc.E04-11-1014;
RA   Yan Q., Sun W., Kujala P., Lotfi Y., Vida T.A., Bean A.J.;
RT   "CART: an Hrs/actinin-4/BERP/myosin V protein complex required for
RT   efficient receptor recycling.";
RL   Mol. Biol. Cell 16:2470-2482(2005).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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   [9]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS], AND CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [10]
RP   INTERACTION WITH ZFYVE28.
RX   PubMed=19460345; DOI=10.1016/j.devcel.2009.03.015;
RA   Mosesson Y., Chetrit D., Schley L., Berghoff J., Ziv T., Carvalho S.,
RA   Milanezi F., Admon A., Schmitt F., Ehrlich M., Yarden Y.;
RT   "Monoubiquitinylation regulates endosomal localization of Lst2, a
RT   negative regulator of EGF receptor signaling.";
RL   Dev. Cell 16:687-698(2009).
CC   -!- FUNCTION: Probably involved in vesicular trafficking via its
CC       association with the CART complex. The CART complex is necessary
CC       for efficient transferrin receptor recycling but not for EGFR
CC       degradation.
CC   -!- SUBUNIT: Associates with myosin-Vb (MYO5B) and alpha-actinin-4
CC       (ACTN4) (By similarity). Component of the CART complex, at least
CC       composed of ACTN4, HGS/HRS, MYO5B and TRIM3. Interacts with
CC       ZFYVE28/LST2. {ECO:0000250, ECO:0000269|PubMed:15772161,
CC       ECO:0000269|PubMed:19460345}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Early endosome
CC       {ECO:0000269|PubMed:15772161}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=Alpha;
CC         IsoId=O75382-1; Sequence=Displayed;
CC       Name=Beta;
CC         IsoId=O75382-2; Sequence=VSP_005758;
CC       Name=Gamma;
CC         IsoId=O75382-3; Sequence=VSP_005759;
CC       Name=4;
CC         IsoId=O75382-4; Sequence=VSP_044780, VSP_044781;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Expressed in brain, heart, uterus and testis.
CC   -!- DOMAIN: The interaction with MYO5B is dependent upon its NHL
CC       repeats, which form a beta-propeller (NHL) domain containing six
CC       blades. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 B box-type zinc finger.
CC       {ECO:0000255|PROSITE-ProRule:PRU00024}.
CC   -!- SIMILARITY: Contains 1 filamin repeat. {ECO:0000255|PROSITE-
CC       ProRule:PRU00087}.
CC   -!- SIMILARITY: Contains 6 NHL repeats. {ECO:0000255|PROSITE-
CC       ProRule:PRU00504}.
CC   -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC       {ECO:0000255|PROSITE-ProRule:PRU00175}.
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DR   EMBL; AF045239; AAC24809.1; -; mRNA.
DR   EMBL; AF220020; AAG53474.1; -; mRNA.
DR   EMBL; AF220021; AAG53475.1; -; mRNA.
DR   EMBL; AF220022; AAG53476.1; -; mRNA.
DR   EMBL; AK291396; BAF84085.1; -; mRNA.
DR   EMBL; AK298843; BAH12882.1; -; mRNA.
DR   EMBL; AC084337; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471064; EAW68709.1; -; Genomic_DNA.
DR   EMBL; BC096827; AAH96827.1; -; mRNA.
DR   CCDS; CCDS58115.1; -. [O75382-4]
DR   CCDS; CCDS7764.1; -. [O75382-1]
DR   RefSeq; NP_001234935.1; NM_001248006.1. [O75382-1]
DR   RefSeq; NP_001234936.1; NM_001248007.1. [O75382-4]
DR   RefSeq; NP_006449.2; NM_006458.3. [O75382-1]
DR   RefSeq; NP_150594.2; NM_033278.3. [O75382-1]
DR   UniGene; Hs.591992; -.
DR   ProteinModelPortal; O75382; -.
DR   SMR; O75382; 18-63, 290-420, 475-744.
DR   BioGrid; 115858; 10.
DR   IntAct; O75382; 3.
DR   STRING; 9606.ENSP00000340797; -.
DR   PhosphoSite; O75382; -.
DR   MaxQB; O75382; -.
DR   PaxDb; O75382; -.
DR   PRIDE; O75382; -.
DR   Ensembl; ENST00000345851; ENSP00000340797; ENSG00000110171. [O75382-1]
DR   Ensembl; ENST00000359518; ENSP00000352508; ENSG00000110171. [O75382-1]
DR   Ensembl; ENST00000525074; ENSP00000433102; ENSG00000110171. [O75382-1]
DR   Ensembl; ENST00000536344; ENSP00000445460; ENSG00000110171. [O75382-4]
DR   GeneID; 10612; -.
DR   KEGG; hsa:10612; -.
DR   UCSC; uc001mdh.3; human. [O75382-1]
DR   CTD; 10612; -.
DR   GeneCards; GC11M006469; -.
DR   HGNC; HGNC:10064; TRIM3.
DR   HPA; HPA043396; -.
DR   HPA; HPA048233; -.
DR   MIM; 605493; gene.
DR   neXtProt; NX_O75382; -.
DR   PharmGKB; PA35534; -.
DR   eggNOG; COG3391; -.
DR   HOGENOM; HOG000220817; -.
DR   HOVERGEN; HBG054843; -.
DR   InParanoid; O75382; -.
DR   KO; K11997; -.
DR   OMA; INTTAEP; -.
DR   OrthoDB; EOG7H4DST; -.
DR   PhylomeDB; O75382; -.
DR   TreeFam; TF331018; -.
DR   GeneWiki; TRIM3; -.
DR   GenomeRNAi; 10612; -.
DR   NextBio; 40314; -.
DR   PRO; PR:O75382; -.
DR   ArrayExpress; O75382; -.
DR   Bgee; O75382; -.
DR   CleanEx; HS_TRIM3; -.
DR   Genevestigator; O75382; -.
DR   GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR   GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0008022; F:protein C-terminus binding; TAS:ProtInc.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0007399; P:nervous system development; TAS:ProtInc.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   Gene3D; 2.120.10.30; -; 1.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 3.30.40.10; -; 1.
DR   Gene3D; 4.10.45.10; -; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR003649; Bbox_C.
DR   InterPro; IPR017868; Filamin/ABP280_repeat-like.
DR   InterPro; IPR001298; Filamin/ABP280_rpt.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR001258; NHL_repeat.
DR   InterPro; IPR013017; NHL_repeat_subgr.
DR   InterPro; IPR000315; Znf_B-box.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   Pfam; PF00630; Filamin; 1.
DR   Pfam; PF01436; NHL; 6.
DR   Pfam; PF00643; zf-B_box; 1.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   SMART; SM00502; BBC; 1.
DR   SMART; SM00336; BBOX; 1.
DR   SMART; SM00557; IG_FLMN; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF81296; SSF81296; 1.
DR   PROSITE; PS50194; FILAMIN_REPEAT; 1.
DR   PROSITE; PS51125; NHL; 6.
DR   PROSITE; PS50119; ZF_BBOX; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Coiled coil; Complete proteome;
KW   Cytoplasm; Endosome; Metal-binding; Phosphoprotein; Polymorphism;
KW   Protein transport; Reference proteome; Repeat; Transport; Zinc;
KW   Zinc-finger.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:19413330}.
FT   CHAIN         2    744       Tripartite motif-containing protein 3.
FT                                /FTId=PRO_0000056197.
FT   REPEAT      317    418       Filamin.
FT   REPEAT      473    516       NHL 1.
FT   REPEAT      520    563       NHL 2.
FT   REPEAT      564    605       NHL 3.
FT   REPEAT      609    652       NHL 4.
FT   REPEAT      656    699       NHL 5.
FT   REPEAT      700    743       NHL 6.
FT   ZN_FING      22     63       RING-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00175}.
FT   ZN_FING     110    151       B box-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00024}.
FT   COILED      153    224       {ECO:0000255}.
FT   MOD_RES       2      2       N-acetylalanine.
FT                                {ECO:0000269|PubMed:19413330}.
FT   MOD_RES       7      7       Phosphoserine. {ECO:0000250}.
FT   VAR_SEQ       1    119       Missing (in isoform 4).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_044780.
FT   VAR_SEQ     120    120       G -> M (in isoform 4).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_044781.
FT   VAR_SEQ     146    156       Missing (in isoform Beta).
FT                                {ECO:0000303|PubMed:11331580}.
FT                                /FTId=VSP_005758.
FT   VAR_SEQ     224    302       Missing (in isoform Gamma).
FT                                {ECO:0000303|PubMed:11331580}.
FT                                /FTId=VSP_005759.
FT   VARIANT     298    298       L -> R (in dbSNP:rs10128723).
FT                                /FTId=VAR_052124.
FT   CONFLICT    113    113       L -> F (in Ref. 1; AAC24809 and 2;
FT                                AAG53474/AAG53475/AAG53476).
FT                                {ECO:0000305}.
FT   CONFLICT    236    236       S -> T (in Ref. 1; AAC24809 and 2;
FT                                AAG53474/AAG53475). {ECO:0000305}.
FT   CONFLICT    347    347       T -> A (in Ref. 1; AAC24809 and 2;
FT                                AAG53474/AAG53475/AAG53476).
FT                                {ECO:0000305}.
FT   CONFLICT    450    450       V -> L (in Ref. 3; BAH12882).
FT                                {ECO:0000305}.
FT   CONFLICT    631    631       N -> S (in Ref. 1; AAC24809 and 2;
FT                                AAG53474/AAG53475/AAG53476).
FT                                {ECO:0000305}.
FT   CONFLICT    636    636       I -> V (in Ref. 1; AAC24809 and 2;
FT                                AAG53474/AAG53475/AAG53476).
FT                                {ECO:0000305}.
FT   CONFLICT    646    646       V -> E (in Ref. 1; AAC24809 and 2;
FT                                AAG53474/AAG53475/AAG53476).
FT                                {ECO:0000305}.
SQ   SEQUENCE   744 AA;  80830 MW;  FF9829CB52314DD2 CRC64;
     MAKREDSPGP EVQPMDKQFL VCSICLDRYQ CPKVLPCLHT FCERCLQNYI PAQSLTLSCP
     VCRQTSILPE QGVSALQNNF FISSLMEAMQ QAPDGAHDPE DPHPLSVVAG RPLSCPNHEG
     KTMEFYCEAC ETAMCGECRA GEHREHGTVL LRDVVEQHKA ALQRQLEAVR GRLPQLSAAI
     ALVGGISQQL QERKAEALAQ ISAAFEDLEQ ALQQRKQALV SDLETICGAK QKVLQSQLDT
     LRQGQEHIGS SCSFAEQALR LGSAPEVLLV RKHMRERLAA LAAQAFPERP HENAQLELVL
     EVDGLRRSVL NLGALLTTSA TAHETVATGE GLRQALVGQP ASLTVTTKDK DGRLVRTGSA
     ELRAEITGPD GTRLPVPVVD HKNGTYELVY TARTEGELLL SVLLYGQPVR GSPFRVRALR
     PGDLPPSPDD VKRRVKSPGG PGSHVRQKAV RRPSSMYSTG GKRKDNPIED ELVFRVGSRG
     REKGEFTNLQ GVSAASSGRI VVADSNNQCI QVFSNEGQFK FRFGVRGRSP GQLQRPTGVA
     VDTNGDIIVA DYDNRWVSIF SPEGKFKTKI GAGRLMGPKG VAVDRNGHII VVDNKSCCVF
     TFQPNGKLVG RFGGRGATDR HFAGPHFVAV NNKNEIVVTD FHNHSVKVYS ADGEFLFKFG
     SHGEGNGQFN APTGVAVDSN GNIIVADWGN SRIQVFDSSG SFLSYINTSA EPLYGPQGLA
     LTSDGHVVVA DAGNHCFKAY RYLQ
//
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