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Q3ZCQ8 (TIM50_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mitochondrial import inner membrane translocase subunit TIM50
Gene names
Name:TIMM50
Synonyms:TIM50
ORF Names:PRO1512
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length353 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane. Has some phosphatase activity in vitro; however such activity may not be relevant in vivo. Isoform 2 may participate in the release of snRNPs and SMN from the Cajal body. Ref.1

Subunit structure

Component of the TIM23 complex at least composed of TIMM23, TIMM17 (TIMM17A or TIMM17B) and TIMM50; within this complex, directly interacts with TIMM23. The complex interacts with the TIMM44 component of the PAM complex and with DNAJC15. Isoform 2 interacts with COIL and snRNPs. Ref.1 Ref.8 Ref.10

Subcellular location

Mitochondrion inner membrane; Single-pass membrane protein Ref.1 Ref.8.

Isoform 2: Nucleus speckle. Note: Nuclear and enriched in speckles with snRNPs. Ref.1 Ref.8

Tissue specificity

Widely expressed. Expressed at higher level in brain, kidney and liver (at protein level). Ref.1 Ref.8

Domain

The FCP1 homology domain does not contain the canonical D-x-D-x-[TV] active site, suggesting that it probably does not display phosphatase activity in vivo.

Sequence similarities

Belongs to the TIM50 family.

Contains 1 FCP1 homology domain.

Sequence caution

The sequence AAG35534.1 differs from that shown. Reason: Chimera.

Ontologies

Keywords
   Biological processProtein transport
Translocation
Transport
   Cellular componentMembrane
Mitochondrion
Mitochondrion inner membrane
Nucleus
   Coding sequence diversityAlternative splicing
   DomainTransit peptide
Transmembrane
Transmembrane helix
   LigandRNA-binding
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcellular protein metabolic process

Traceable author statement. Source: Reactome

mitochondrial membrane organization

Inferred from mutant phenotype Ref.1. Source: UniProtKB

peptidyl-tyrosine dephosphorylation

Inferred from direct assay Ref.1. Source: GOC

protein dephosphorylation

Inferred from direct assay Ref.1. Source: UniProtKB

protein targeting to mitochondrion

Traceable author statement. Source: Reactome

release of cytochrome c from mitochondria

Inferred from direct assay Ref.1. Source: MGI

   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

mitochondrial inner membrane

Inferred from direct assay Ref.1. Source: UniProtKB

mitochondrial inner membrane presequence translocase complex

Inferred from physical interaction Ref.1. Source: UniProtKB

mitochondrion

Inferred from direct assay. Source: HPA

nuclear speck

Inferred from direct assay Ref.8. Source: UniProtKB

   Molecular_functionRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

interleukin-2 receptor binding

Inferred from direct assay Ref.1. Source: MGI

phosphoprotein phosphatase activity

Inferred from direct assay Ref.1. Source: MGI

protein serine/threonine phosphatase activity

Inferred from direct assay Ref.1. Source: UniProtKB

protein tyrosine phosphatase activity

Inferred from direct assay Ref.1. Source: UniProtKB

ribonucleoprotein complex binding

Inferred from direct assay Ref.8. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q3ZCQ8-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q3ZCQ8-2)

Also known as: Tim50a;

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MASALSLGNK...GGAAWRQRKM
Isoform 3 (identifier: Q3ZCQ8-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-11: MAASAAVFSRL → MVPRFLMSSTM
     12-124: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4444Mitochondrion Potential
Chain45 – 353309Mitochondrial import inner membrane translocase subunit TIM50
PRO_0000043115

Regions

Topological domain45 – 6521Mitochondrial matrix Potential
Transmembrane66 – 8621Helical; Potential
Topological domain87 – 353267Mitochondrial intermembrane Potential
Domain143 – 286144FCP1 homology

Natural variations

Alternative sequence1 – 1111MAASAAVFSRL → MVPRFLMSSTM in isoform 3.
VSP_047682
Alternative sequence11M → MASALSLGNKCDPFLRCVLC RGGGALQGPRGRGPDDFESQ LSPPGSARRLVRSKRACGNP PDAFGLSRASVHPPLPRVSI GCSSGPGRAKRERVGGAAWR QRKM in isoform 2.
VSP_016389
Alternative sequence12 – 124113Missing in isoform 3.
VSP_047683

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 6, 2005. Version 2.
Checksum: 524EB9989BBF6988

FASTA35339,646
        10         20         30         40         50         60 
MAASAAVFSR LRSGLRLGSR GLCTRLATPP RRAPDQAAEI GSRGSTKAQG PQQQPGSEGP 

        70         80         90        100        110        120 
SYAKKVALWL AGLLGAGGTV SVVYIFGNNP VDENGAKIPD EFDNDPILVQ QLRRTYKYFK 

       130        140        150        160        170        180 
DYRQMIIEPT SPCLLPDPLQ EPYYQPPYTL VLELTGVLLH PEWSLATGWR FKKRPGIETL 

       190        200        210        220        230        240 
FQQLAPLYEI VIFTSETGMT AFPLIDSVDP HGFISYRLFR DATRYMDGHH VKDISCLNRD 

       250        260        270        280        290        300 
PARVVVVDCK KEAFRLQPYN GVALRPWDGN SDDRVLLDLS AFLKTIALNG VEDVRTVLEH 

       310        320        330        340        350 
YALEDDPLAA FKQRQSRLEQ EEQQRLAELS KSNKQNLFLG SLTSRLWPRS KQP 

« Hide

Isoform 2 (Tim50a) [UniParc].

Checksum: 870E81E2A0289BC4
Show »

FASTA45650,465
Isoform 3 [UniParc].

Checksum: 4DD423B7CF6FC444
Show »

FASTA24027,579

References

« Hide 'large scale' references
[1]"Tim50, a component of the mitochondrial translocator, regulates mitochondrial integrity and cell death."
Guo Y., Cheong N., Zhang Z., De Rose R., Deng Y., Farber S.A., Fernandes-Alnemri T., Alnemri E.S.
J. Biol. Chem. 279:24813-24825(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH TIMM23.
[2]"Cloning of a novel splice variant of TIM50L."
Zheng H., Xie Y., Mao Y.
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[3]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Brain, Eye and Pancreas.
[5]"Functional prediction of the coding sequences of 75 new genes deduced by analysis of cDNA clones from human fetal liver."
Zhang C., Yu Y., Zhang S., Wei H., Bi J., Zhou G., Dong C., Zai Y., Xu W., Gao F., Liu M., He F.
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 68-353.
Tissue: Fetal liver.
[6]Bienvenut W.V.
Submitted (JUN-2005) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 98-113; 275-284; 285-295 AND 335-345, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: B-cell lymphoma.
[7]Lubec G., Afjehi-Sadat L.
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 98-113, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain and Cajal-Retzius cell.
[8]"Tim50a, a nuclear isoform of the mitochondrial Tim50, interacts with proteins involved in snRNP biogenesis."
Xu H., Somers Z.B., Robinson M.L. II, Hebert M.D.
BMC Cell Biol. 6:29-29(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORM 2), RNA-BINDING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH COIL.
[9]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Methylation-controlled J-protein MCJ acts in the import of proteins into human mitochondria."
Schusdziarra C., Blamowska M., Azem A., Hell K.
Hum. Mol. Genet. 22:1348-1357(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DNAJC15.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY551341 mRNA. Translation: AAT01208.1.
AY444561 mRNA. Translation: AAS68537.1.
AC011500 Genomic DNA. No translation available.
BC009072 mRNA. Translation: AAH09072.1.
BC010736 mRNA. Translation: AAH10736.1.
BC050082 mRNA. Translation: AAH50082.1.
BC121146 mRNA. Translation: AAI21147.1.
AF130109 mRNA. Translation: AAG35534.1. Sequence problems.
RefSeqNP_001001563.1. NM_001001563.1.
UniGeneHs.590956.
Hs.597106.

3D structure databases

ProteinModelPortalQ3ZCQ8.
SMRQ3ZCQ8. Positions 151-314.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid124961. 54 interactions.
IntActQ3ZCQ8. 24 interactions.
MINTMINT-1148586.
STRING9606.ENSP00000318115.

PTM databases

PhosphoSiteQ3ZCQ8.

Polymorphism databases

DMDM83305924.

Proteomic databases

PaxDbQ3ZCQ8.
PRIDEQ3ZCQ8.

Protocols and materials databases

DNASU92609.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000314349; ENSP00000318115; ENSG00000105197. [Q3ZCQ8-2]
ENST00000544017; ENSP00000445806; ENSG00000105197. [Q3ZCQ8-3]
ENST00000607714; ENSP00000475531; ENSG00000105197. [Q3ZCQ8-1]
GeneID92609.
KEGGhsa:92609.
UCSCuc002olt.2. human.
uc002olu.1. human. [Q3ZCQ8-2]

Organism-specific databases

CTD92609.
GeneCardsGC19P039971.
H-InvDBHIX0040029.
HGNCHGNC:23656. TIMM50.
HPAHPA048843.
MIM607381. gene.
neXtProtNX_Q3ZCQ8.
PharmGKBPA134902846.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5190.
HOVERGENHBG084157.
InParanoidQ3ZCQ8.
KOK17496.
OMAMEGHHVK.
OrthoDBEOG773XH7.
PhylomeDBQ3ZCQ8.
TreeFamTF106198.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.

Gene expression databases

ArrayExpressQ3ZCQ8.
BgeeQ3ZCQ8.
CleanExHS_TIMM50.
GenevestigatorQ3ZCQ8.

Family and domain databases

Gene3D3.40.50.1000. 1 hit.
InterProIPR023214. HAD-like_dom.
IPR004274. NIF.
IPR027111. Tim50.
[Graphical view]
PANTHERPTHR12210:SF3. PTHR12210:SF3. 1 hit.
PfamPF03031. NIF. 1 hit.
[Graphical view]
SMARTSM00577. CPDc. 1 hit.
[Graphical view]
SUPFAMSSF56784. SSF56784. 1 hit.
PROSITEPS50969. FCP1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiTIMM50.
GenomeRNAi92609.
NextBio77819.
PROQ3ZCQ8.
SOURCESearch...

Entry information

Entry nameTIM50_HUMAN
AccessionPrimary (citable) accession number: Q3ZCQ8
Secondary accession number(s): Q330K1 expand/collapse secondary AC list , Q6QA00, Q96FJ5, Q96GY2, Q9H370
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: December 6, 2005
Last modified: April 16, 2014
This is version 91 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM