ID TIM50_HUMAN Reviewed; 353 AA. AC Q3ZCQ8; Q6QA00; Q96FJ5; Q96GY2; Q9H370; DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 06-DEC-2005, sequence version 2. DT 07-JUL-2009, entry version 43. DE RecName: Full=Mitochondrial import inner membrane translocase subunit TIM50; DE Flags: Precursor; GN Name=TIMM50; Synonyms=TIM50; ORFNames=PRO1512; 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 1), FUNCTION, SUBCELLULAR RP LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH TIMM23. RX PubMed=15044455; DOI=10.1074/jbc.M402049200; RA Guo Y., Cheong N., Zhang Z., De Rose R., Deng Y., Farber S.A., RA Fernandes-Alnemri T., Alnemri E.S.; RT "Tim50, a component of the mitochondrial translocator, regulates RT mitochondrial integrity and cell death."; RL J. Biol. Chem. 279:24813-24825(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND PARTIAL RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Brain, Eye, and Pancreas; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 68-353. RC TISSUE=Fetal liver; RA Zhang C., Yu Y., Zhang S., Wei H., Bi J., Zhou G., Dong C., Zai Y., RA Xu W., Gao F., Liu M., He F.; RT "Functional prediction of the coding sequences of 75 new genes deduced RT by analysis of cDNA clones from human fetal liver."; RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases. RN [4] RP PROTEIN SEQUENCE OF 98-113; 275-284; 285-295 AND 335-345, AND MASS RP SPECTROMETRY. RC TISSUE=B-cell lymphoma; RA Bienvenut W.V.; RL Submitted (JUN-2005) to UniProtKB. RN [5] RP PROTEIN SEQUENCE OF 98-113, AND MASS SPECTROMETRY. RC TISSUE=Brain, and Cajal-Retzius cell; RA Lubec G., Afjehi-Sadat L.; RL Submitted (MAR-2007) to UniProtKB. RN [6] RP ALTERNATIVE SPLICING (ISOFORM 2), RNA-BINDING, SUBCELLULAR LOCATION, RP TISSUE SPECIFICITY, AND INTERACTION WITH COIL. RX PubMed=16008839; DOI=10.1186/1471-2121-6-29; RA Xu H., Somers Z.B., Robinson M.L. II, Hebert M.D.; RT "Tim50a, a nuclear isoform of the mitochondrial Tim50, interacts with RT proteins involved in snRNP biogenesis."; RL BMC Cell Biol. 6:29-29(2005). RN [7] RP IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. RA Colinge J., Superti-Furga G., Bennett K.L.; RL Submitted (OCT-2008) to UniProtKB. CC -!- FUNCTION: Essential component of the TIM23 complex, a complex that CC mediates the translocation of transit peptide-containing proteins CC across the mitochondrial inner membrane. Has some phosphatase CC activity in vitro; however such activity may not be relevant in CC vivo. Isoform 2 may participate in the release of snRNPs and SMN CC from the Cajal body. CC -!- SUBUNIT: Component of the TIM23 complex at least composed of CC TIMM23, TIMM17 (TIMM17A or TIMM17B) and TIMM50. Interacts directly CC with TIMM23. Isoform 2 interacts with COIL and snRNPs. CC -!- INTERACTION: CC Q9H8T0:AKTIP; NbExp=1; IntAct=EBI-355175, EBI-711399; CC P10398:ARAF; NbExp=2; IntAct=EBI-355175, EBI-365961; CC Q9Y5V3:MAGED1; NbExp=1; IntAct=EBI-355175, EBI-716006; CC Q9BRX2:PELO; NbExp=1; IntAct=EBI-355175, EBI-1043580; CC Q99623:PHB2; NbExp=1; IntAct=EBI-355175, EBI-358348; CC P04049:RAF1; NbExp=3; IntAct=EBI-355175, EBI-365996; CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass CC membrane protein. CC -!- SUBCELLULAR LOCATION: Isoform 2: Nucleus speckle. Note=Nuclear and CC enriched in speckles with snRNPs. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q3ZCQ8-1; Sequence=Displayed; CC Name=2; Synonyms=Tim50a; CC IsoId=Q3ZCQ8-2; Sequence=VSP_016389; CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed at higher level in CC brain, kidney and liver (at protein level). CC -!- DOMAIN: The FCP1 homology domain does not contain the canonical D- CC x-D-x-[TV] active site, suggesting that it probably does not CC display phosphatase activity in vivo. CC -!- SIMILARITY: Belongs to the TIM50 family. CC -!- SIMILARITY: Contains 1 FCP1 homology domain. CC -!- SEQUENCE CAUTION: CC Sequence=AAG35534.1; Type=Miscellaneous discrepancy; Note=Chimera; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY551341; AAT01208.1; -; mRNA. DR EMBL; BC009072; AAH09072.1; -; mRNA. DR EMBL; BC010736; AAH10736.1; -; mRNA. DR EMBL; BC050082; AAH50082.1; -; mRNA. DR EMBL; AF130109; AAG35534.1; ALT_SEQ; mRNA. DR IPI; IPI00418497; -. DR IPI; IPI00656071; -. DR RefSeq; NP_001001563.1; -. DR UniGene; Hs.590956; -. DR UniGene; Hs.597106; -. DR IntAct; Q3ZCQ8; 30. DR PhosphoSite; Q3ZCQ8; -. DR PRIDE; Q3ZCQ8; -. DR Ensembl; ENSG00000105197; Homo sapiens. DR GeneID; 92609; -. DR KEGG; hsa:92609; -. DR UCSC; uc002olu.1; human. DR GeneCards; GC19P044663; -. DR H-InvDB; HIX0040029; -. DR HGNC; HGNC:23656; TIMM50. DR MIM; 607381; gene. DR PharmGKB; PA134902846; -. DR HOVERGEN; Q3ZCQ8; -. DR OMA; Q3ZCQ8; PVDENGA. DR NextBio; 77819; -. DR ArrayExpress; Q3ZCQ8; -. DR Bgee; Q3ZCQ8; -. DR CleanEx; HS_TIMM50; -. DR GermOnline; ENSG00000105197; Homo sapiens. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. DR GO; GO:0005744; C:mitochondrial inner membrane presequence tr...; IPI:UniProtKB. DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:UniProtKB. DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:UniProtKB. DR GO; GO:0043021; F:ribonucleoprotein binding; IDA:UniProtKB. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0065002; P:intracellular protein transmembrane transport; IEA:UniProtKB-KW. DR GO; GO:0007006; P:mitochondrial membrane organization; IMP:UniProtKB. DR GO; GO:0006470; P:protein amino acid dephosphorylation; IDA:UniProtKB. DR InterPro; IPR004274; NIF. DR Pfam; PF03031; NIF; 1. DR SMART; SM00577; CPDc; 1. DR PROSITE; PS50969; FCP1; 1. PE 1: Evidence at protein level; KW Alternative splicing; Complete proteome; Direct protein sequencing; KW Membrane; Mitochondrion; Mitochondrion inner membrane; Nucleus; KW Protein transport; RNA-binding; Transit peptide; Translocation; KW Transmembrane; Transport. FT TRANSIT 1 44 Mitochondrion (Potential). FT CHAIN 45 353 Mitochondrial import inner membrane FT translocase subunit TIM50. FT /FTId=PRO_0000043115. FT TOPO_DOM 45 65 Mitochondrial matrix (Potential). FT TRANSMEM 66 86 Potential. FT TOPO_DOM 87 353 Mitochondrial intermembrane (Potential). FT DOMAIN 143 286 FCP1 homology. FT VAR_SEQ 1 1 M -> MASALSLGNKCDPFLRCVLCRGGGALQGPRGRGPDD FT FESQLSPPGSARRLVRSKRACGNPPDAFGLSRASVHPPLPR FT VSIGCSSGPGRAKRERVGGAAWRQRKM (in isoform FT 2). FT /FTId=VSP_016389. SQ SEQUENCE 353 AA; 39646 MW; 524EB9989BBF6988 CRC64; MAASAAVFSR LRSGLRLGSR GLCTRLATPP RRAPDQAAEI GSRGSTKAQG PQQQPGSEGP SYAKKVALWL AGLLGAGGTV SVVYIFGNNP VDENGAKIPD EFDNDPILVQ QLRRTYKYFK DYRQMIIEPT SPCLLPDPLQ EPYYQPPYTL VLELTGVLLH PEWSLATGWR FKKRPGIETL FQQLAPLYEI VIFTSETGMT AFPLIDSVDP HGFISYRLFR DATRYMDGHH VKDISCLNRD PARVVVVDCK KEAFRLQPYN GVALRPWDGN SDDRVLLDLS AFLKTIALNG VEDVRTVLEH YALEDDPLAA FKQRQSRLEQ EEQQRLAELS KSNKQNLFLG SLTSRLWPRS KQP //