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Protein

Mitochondrial import inner membrane translocase subunit Tim8 A

Gene

TIMM8A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space. The TIMM8-TIMM13 complex mediates the import of proteins such as TIMM23, SLC25A12/ARALAR1 and SLC25A13/ARALAR2, while the predominant TIMM9-TIMM10 70 kDa complex mediates the import of much more proteins. Probably necessary for normal neurologic development.2 Publications

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. chaperone-mediated protein transport Source: BHF-UCL
  3. nervous system development Source: ProtInc
  4. protein targeting to mitochondrion Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Protein transport, Translocation, Transport

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_118595. Mitochondrial protein import.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitochondrial import inner membrane translocase subunit Tim8 A
Alternative name(s):
Deafness dystonia protein 1
X-linked deafness dystonia protein
Gene namesi
Name:TIMM8A
Synonyms:DDP, DDP1, TIM8A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:11817. TIMM8A.

Subcellular locationi

  1. Mitochondrion inner membrane 1 Publication; Peripheral membrane protein 1 Publication; Intermembrane side 1 Publication

GO - Cellular componenti

  1. mitochondrial inner membrane Source: UniProtKB-SubCell
  2. mitochondrial intermembrane space Source: BHF-UCL
  3. mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Involvement in diseasei

Mohr-Tranebjaerg syndrome (MTS)3 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionRecessive neurodegenerative syndrome characterized by postlingual progressive sensorineural deafness as the first presenting symptom in early childhood, followed by progressive dystonia, spasticity, dysphagia, mental deterioration, paranoia and cortical blindness.

See also OMIM:304700
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti66 – 661C → W in MTS; disrupts the assembly of the heterohexamer with TIMM13. 3 Publications
VAR_010237
Jensen syndrome (JENSS)

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionX-linked disease characterized by deafness, blindness and muscle weakness.

See also OMIM:311150

Keywords - Diseasei

Deafness, Disease mutation

Organism-specific databases

MIMi304700. phenotype.
311150. phenotype.
Orphaneti52368. Mohr-Tranebjaerg syndrome.
PharmGKBiPA36523.

Polymorphism and mutation databases

BioMutaiTIMM8A.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 9797Mitochondrial import inner membrane translocase subunit Tim8 APRO_0000193584Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi43 ↔ 66By similarity
Disulfide bondi47 ↔ 62By similarity
Modified residuei87 – 871PhosphoserineBy similarity
Modified residuei94 – 941Phosphoserine1 Publication
Modified residuei96 – 961Phosphoserine1 Publication

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

MaxQBiO60220.
PaxDbiO60220.
PeptideAtlasiO60220.
PRIDEiO60220.

PTM databases

PhosphoSiteiO60220.

Expressioni

Tissue specificityi

Highly expressed in fetal and adult brain, followed by fetal lung, liver and kidney. Also expressed in heart, placenta, lung, liver, kidney, pancreas, skeletal muscle and heart.

Gene expression databases

BgeeiO60220.
CleanExiHS_TIMM8A.
GenevestigatoriO60220.

Organism-specific databases

HPAiHPA003628.

Interactioni

Subunit structurei

Heterohexamer; composed of 3 copies of TIMM8A and 3 copies of TIMM13, named soluble 70 kDa complex. Associates with the TIM22 complex, whose core is composed of TIMM22.

Binary interactionsi

WithEntry#Exp.IntActNotes
KRT15P190123EBI-1049822,EBI-739566
STAM2O758863EBI-1049822,EBI-373258

Protein-protein interaction databases

BioGridi108042. 10 interactions.
IntActiO60220. 6 interactions.
MINTiMINT-2999881.
STRINGi9606.ENSP00000361993.

Structurei

3D structure databases

ProteinModelPortaliO60220.
SMRiO60220. Positions 29-84.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi43 – 6624Twin CX3C motifAdd
BLAST

Domaini

The twin CX3C motif contains 4 conserved Cys residues that form 2 disulfide bonds in the mitochondrial intermembrane space. However, during the transit of TIMM8A from cytoplasm into mitochondrion, the Cys residues probably coordinate zinc, thereby preventing folding and allowing its transfer across mitochondrial outer membrane (By similarity).By similarity

Sequence similaritiesi

Belongs to the small Tim family.Curated

Phylogenomic databases

eggNOGiNOG238740.
GeneTreeiENSGT00390000016102.
HOGENOMiHOG000115758.
HOVERGENiHBG060492.
InParanoidiO60220.
KOiK17780.
OMAiTEMCWDK.
OrthoDBiEOG79W97P.
PhylomeDBiO60220.
TreeFamiTF106191.

Family and domain databases

Gene3Di1.10.287.810. 1 hit.
InterProiIPR004217. Tim10/DDP_fam_Znf.
[Graphical view]
PfamiPF02953. zf-Tim10_DDP. 1 hit.
[Graphical view]
SUPFAMiSSF144122. SSF144122. 1 hit.

Sequencei

Sequence statusi: Complete.

O60220-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDSSSSSSAA GLGAVDPQLQ HFIEVETQKQ RFQQLVHQMT ELCWEKCMDK
60 70 80 90
PGPKLDSRAE ACFVNCVERF IDTSQFILNR LEQTQKSKPV FSESLSD
Length:97
Mass (Da):10,998
Last modified:August 1, 1998 - v1
Checksum:iCB72822290F20AB0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti62 – 621C → R in AAH70284 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti66 – 661C → W in MTS; disrupts the assembly of the heterohexamer with TIMM13. 3 Publications
VAR_010237

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U66035 mRNA. Translation: AAC15946.1.
AK312117 mRNA. Translation: BAG35053.1.
AL035422 Genomic DNA. Translation: CAB55875.1.
CH471115 Genomic DNA. Translation: EAX02854.1.
BC006994 mRNA. Translation: AAH06994.1.
BC015093 mRNA. Translation: AAH15093.1.
BC070284 mRNA. Translation: AAH70284.1.
CCDSiCCDS14481.1.
RefSeqiNP_004076.1. NM_004085.3.
UniGeneiHs.447877.

Genome annotation databases

EnsembliENST00000372902; ENSP00000361993; ENSG00000126953.
GeneIDi1678.
KEGGihsa:1678.
UCSCiuc004ehd.2. human.

Polymorphism and mutation databases

BioMutaiTIMM8A.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U66035 mRNA. Translation: AAC15946.1.
AK312117 mRNA. Translation: BAG35053.1.
AL035422 Genomic DNA. Translation: CAB55875.1.
CH471115 Genomic DNA. Translation: EAX02854.1.
BC006994 mRNA. Translation: AAH06994.1.
BC015093 mRNA. Translation: AAH15093.1.
BC070284 mRNA. Translation: AAH70284.1.
CCDSiCCDS14481.1.
RefSeqiNP_004076.1. NM_004085.3.
UniGeneiHs.447877.

3D structure databases

ProteinModelPortaliO60220.
SMRiO60220. Positions 29-84.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108042. 10 interactions.
IntActiO60220. 6 interactions.
MINTiMINT-2999881.
STRINGi9606.ENSP00000361993.

PTM databases

PhosphoSiteiO60220.

Polymorphism and mutation databases

BioMutaiTIMM8A.

Proteomic databases

MaxQBiO60220.
PaxDbiO60220.
PeptideAtlasiO60220.
PRIDEiO60220.

Protocols and materials databases

DNASUi1678.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000372902; ENSP00000361993; ENSG00000126953.
GeneIDi1678.
KEGGihsa:1678.
UCSCiuc004ehd.2. human.

Organism-specific databases

CTDi1678.
GeneCardsiGC0XM100600.
GeneReviewsiTIMM8A.
HGNCiHGNC:11817. TIMM8A.
HPAiHPA003628.
MIMi300356. gene.
304700. phenotype.
311150. phenotype.
neXtProtiNX_O60220.
Orphaneti52368. Mohr-Tranebjaerg syndrome.
PharmGKBiPA36523.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG238740.
GeneTreeiENSGT00390000016102.
HOGENOMiHOG000115758.
HOVERGENiHBG060492.
InParanoidiO60220.
KOiK17780.
OMAiTEMCWDK.
OrthoDBiEOG79W97P.
PhylomeDBiO60220.
TreeFamiTF106191.

Enzyme and pathway databases

ReactomeiREACT_118595. Mitochondrial protein import.

Miscellaneous databases

GeneWikiiTIMM8A.
GenomeRNAii1678.
NextBioi6906.
PROiO60220.
SOURCEiSearch...

Gene expression databases

BgeeiO60220.
CleanExiHS_TIMM8A.
GenevestigatoriO60220.

Family and domain databases

Gene3Di1.10.287.810. 1 hit.
InterProiIPR004217. Tim10/DDP_fam_Znf.
[Graphical view]
PfamiPF02953. zf-Tim10_DDP. 1 hit.
[Graphical view]
SUPFAMiSSF144122. SSF144122. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A novel X-linked gene, DDP, shows mutations in families with deafness (DFN-1), dystonia, mental deficiency and blindness."
    Jin H., May M., Tranebjaerg L., Kendall E., Fontan G., Jackson J., Subramony S.H., Arena F., Lubs H., Smith S., Stevenson R., Schwartz C., Vetrie D.
    Nat. Genet. 14:177-180(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Tongue.
  3. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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].
    Tissue: Brain, Kidney and Urinary bladder.
  6. Cited for: PROBABLE FUNCTION.
  7. "Mitochondria and dystonia: the movement disorder connection?"
    Wallace D.C., Murdock D.G.
    Proc. Natl. Acad. Sci. U.S.A. 96:1817-1819(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROBABLE FUNCTION.
  8. "Role of the deafness dystonia peptide 1 (DDP1) in import of human Tim23 into the inner membrane of mitochondria."
    Rothbauer U., Hofmann S., Muehlenbein N., Paschen S.A., Gerbitz K.-D., Neupert W., Brunner M., Bauer M.F.
    J. Biol. Chem. 276:37327-37334(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, ZINC-BINDING, INTERACTION WITH TIMM13.
  9. "The calcium-binding aspartate/glutamate carriers, citrin and aralar1, are new substrates for the DDP1/TIMM8a-TIMM13 complex."
    Roesch K., Hynds P.J., Varga R., Tranebjaerg L., Koehler C.M.
    Hum. Mol. Genet. 13:2101-2111(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  14. "A de novo missense mutation in a critical domain of the X-linked DDP gene causes the typical deafness-dystonia-optic atrophy syndrome."
    Tranebjaerg L., Hamel B.C.J., Gabreels F.J.M., Renier W.O., Van Ghelue M.
    Eur. J. Hum. Genet. 8:464-467(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT MTS TRP-66.
  15. "Human deafness dystonia syndrome is caused by a defect in assembly of the DDP1/TIMM8a-TIMM13 complex."
    Roesch K., Curran S.P., Tranebjaerg L., Koehler C.M.
    Hum. Mol. Genet. 11:477-486(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT MTS TRP-66.
  16. "The C66W mutation in the deafness dystonia peptide 1 (DDP1) affects the formation of functional DDP1.TIM13 complexes in the mitochondrial intermembrane space."
    Hofmann S., Rothbauer U., Muehlenbein N., Neupert W., Gerbitz K.-D., Brunner M., Bauer M.F.
    J. Biol. Chem. 277:23287-23293(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT MTS TRP-66.

Entry informationi

Entry nameiTIM8A_HUMAN
AccessioniPrimary (citable) accession number: O60220
Secondary accession number(s): B2R5A6, Q6IRW6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: August 1, 1998
Last modified: April 29, 2015
This is version 136 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.