ID TRI35_HUMAN STANDARD; PRT; 493 AA. AC Q9UPQ4; Q86XQ0; Q8WVA4; DT 01-FEB-2005 (Rel. 46, Created) DT 01-FEB-2005 (Rel. 46, Last sequence update) DT 01-MAY-2005 (Rel. 47, Last annotation update) DE Tripartite motif protein 35 (Hemopoeitic lineage switch protein 5). GN Name=TRIM35; Synonyms=HLS5, KIAA1098; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE (ISOFORM 1). RC TISSUE=Liver; RX PubMed=14662771; DOI=10.1074/jbc.M306751200; RA Lalonde J.-P., Lim R., Ingley E., Tilbrook P.A., Thompson M.J., RA McCulloch R., Beaumont J.G., Wicking C., Eyre H.J., Sutherland G.R., RA Howe K., Solomon E., Williams J.H., Klinken S.P.; RT "HLS5, a novel RBCC (ring finger, B box, coiled-coil) family member RT isolated from a hemopoietic lineage switch, is a candidate tumor RT suppressor."; RL J. Biol. Chem. 279:8181-8189(2004). RN [2] RP NUCLEOTIDE SEQUENCE (ISOFORM 1). RC TISSUE=Brain; RX MEDLINE=99397452; PubMed=10470851; RA Kikuno R., Nagase T., Ishikawa K.-I., Hirosawa M., Miyajima N., RA Tanaka A., Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XIV. RT The complete sequences of 100 new cDNA clones from brain which code RT for large proteins in vitro."; RL DNA Res. 6:197-205(1999). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Brain, and Lung; RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). CC -!- FUNCTION: May play a role as a tumor suppressor. Implicated in the CC cell death mechanism (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasmic and nuclear. Found predominantly CC in cytoplasm with a granular distribution. Found in punctuate CC nuclear bodies (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9UPQ4-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9UPQ4-2; Sequence=VSP_012061; CC Note=No experimental confirmation available; CC -!- DOMAIN: The RING finger domain and the coiled-coil region are CC required for the apoptosis-inducing activity (By similarity). CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. CC -!- SIMILARITY: Contains 1 B box-type zinc finger. CC -!- SIMILARITY: Contains 1 B30.2-like domain. CC -!- SIMILARITY: Contains 1 RING-type zinc finger. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF492463; AAO85480.1; -. DR EMBL; AB029021; BAA83050.1; ALT_INIT. DR EMBL; BC018337; AAH18337.1; -. DR EMBL; BC069226; AAH69226.1; -. DR HSSP; Q99728; 1JM7. DR Ensembl; ENSG00000104228; Homo sapiens. DR Genew; HGNC:16285; TRIM35. DR InterPro; IPR001870; B302. DR InterPro; IPR003879; Butyrophylin. DR InterPro; IPR006574; PRY. DR InterPro; IPR003877; SPRY_receptor. DR InterPro; IPR000315; Znf_Bbox. DR InterPro; IPR001841; Znf_ring. DR Pfam; PF00622; SPRY; 1. DR Pfam; PF00643; zf-B_box; 1. DR Pfam; PF00097; zf-C3HC4; 1. DR PRINTS; PR01406; BBOXZNFINGER. 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 PROSITE; PS50119; ZF_BBOX; 1. DR PROSITE; PS00518; ZF_RING_1; 1. DR PROSITE; PS50089; ZF_RING_2; 1. KW Alternative splicing; Apoptosis; Coiled coil; Metal-binding; KW Nuclear protein; Zinc; Zinc-finger. FT ZN_FING 21 61 RING-type. FT ZN_FING 96 137 B box-type. FT DOMAIN 304 467 B30.2-like. FT DOMAIN 210 251 Coiled coil (Potential). FT VARSPLIC 146 206 AKCRNMEHALREKAKAFWAMRRSYEAIAKHNQVEAAWLEGR FT IRQEFDKLREFLRVEEQAIL -> VRSLIAEERRNFLPTHQ FT WIVTKTRLQTSSPNLQSRRQGQVQEHGACTAGEGQGLLGHA FT ALL (in isoform 2). FT /FTId=VSP_012061. SQ SEQUENCE 493 AA; 56540 MW; BFB7E5BFD3AD7E2D CRC64; MERSPDVSPG PSRSFKEELL CAVCYDPFRD AVTLRCGHNF CRGCVSRCWE VQVSPTCPVC KDRASPADLR TNHTLNNLVE KLLREEAEGA RWTSYRFSRV CRLHRGQLSL FCLEDKELLC CSCQADPRHQ GHRVQPVKDT AHDFRAKCRN MEHALREKAK AFWAMRRSYE AIAKHNQVEA AWLEGRIRQE FDKLREFLRV EEQAILDAMA EETRQKQLLA DEKMKQLTEE TEVLAHEIER LQMEMKEDDV SFLMKHKSRK RRLFCTMEPE PVQPGMLIDV CKYLGSLQYR VWKKMLASVE SVPFSFDPNT AAGWLSVSDD LTSVTNHGYR VQVENPERFS SAPCLLGSRV FSQGSHAWEV ALGGLQSWRV GVVRVRQDSG AEGHSHSCYH DTRSGFWYVC RTQGVEGDHC VTSDPATSPL VLAIPRRLRV ELECEEGELS FYDAERHCHL YTFHARFGEV RPYFYLGGAR GAGPPEPLRI CPLHISVKEE LDG //