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O60220

- TIM8A_HUMAN

UniProt

O60220 - TIM8A_HUMAN

Protein

Mitochondrial import inner membrane translocase subunit Tim8 A

Gene

TIMM8A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. 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

    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: Chromosome X

    Organism-specific databases

    HGNCiHGNC:11817. TIMM8A.

    Subcellular locationi

    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: UniProt

    Keywords - Cellular componenti

    Membrane, Mitochondrion, Mitochondrion inner membrane

    Pathology & Biotechi

    Involvement in diseasei

    Mohr-Tranebjaerg syndrome (MTS) [MIM:304700]: Recessive 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.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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) [MIM:311150]: X-linked disease characterized by deafness, blindness and muscle weakness.
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Keywords - Diseasei

    Deafness, Disease mutation

    Organism-specific databases

    MIMi304700. phenotype.
    311150. phenotype.
    Orphaneti3213. Deafness - opticoacoustic nerve atrophy - dementia.
    52368. Mohr-Tranebjaerg syndrome.
    PharmGKBiPA36523.

    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.

    Protein-protein interaction databases

    BioGridi108042. 8 interactions.
    IntActiO60220. 4 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.
    HOGENOMiHOG000115758.
    HOVERGENiHBG060492.
    InParanoidiO60220.
    KOiK17780.
    OMAiISEYERY.
    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

    MDSSSSSSAA GLGAVDPQLQ HFIEVETQKQ RFQQLVHQMT ELCWEKCMDK   50
    PGPKLDSRAE ACFVNCVERF IDTSQFILNR LEQTQKSKPV FSESLSD 97
    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:
    EMBL
    GenBank
    DDBJ
    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.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS14481.1.
    RefSeqi NP_004076.1. NM_004085.3.
    UniGenei Hs.447877.

    3D structure databases

    ProteinModelPortali O60220.
    SMRi O60220. Positions 29-84.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108042. 8 interactions.
    IntActi O60220. 4 interactions.
    MINTi MINT-2999881.
    STRINGi 9606.ENSP00000361993.

    PTM databases

    PhosphoSitei O60220.

    Proteomic databases

    MaxQBi O60220.
    PaxDbi O60220.
    PeptideAtlasi O60220.
    PRIDEi O60220.

    Protocols and materials databases

    DNASUi 1678.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000372902 ; ENSP00000361993 ; ENSG00000126953 .
    GeneIDi 1678.
    KEGGi hsa:1678.
    UCSCi uc004ehd.2. human.

    Organism-specific databases

    CTDi 1678.
    GeneCardsi GC0XM100600.
    GeneReviewsi TIMM8A.
    HGNCi HGNC:11817. TIMM8A.
    HPAi HPA003628.
    MIMi 300356. gene.
    304700. phenotype.
    311150. phenotype.
    neXtProti NX_O60220.
    Orphaneti 3213. Deafness - opticoacoustic nerve atrophy - dementia.
    52368. Mohr-Tranebjaerg syndrome.
    PharmGKBi PA36523.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG238740.
    HOGENOMi HOG000115758.
    HOVERGENi HBG060492.
    InParanoidi O60220.
    KOi K17780.
    OMAi ISEYERY.
    OrthoDBi EOG79W97P.
    PhylomeDBi O60220.
    TreeFami TF106191.

    Enzyme and pathway databases

    Reactomei REACT_118595. Mitochondrial protein import.

    Miscellaneous databases

    GeneWikii TIMM8A.
    GenomeRNAii 1678.
    NextBioi 6906.
    PROi O60220.
    SOURCEi Search...

    Gene expression databases

    Bgeei O60220.
    CleanExi HS_TIMM8A.
    Genevestigatori O60220.

    Family and domain databases

    Gene3Di 1.10.287.810. 1 hit.
    InterProi IPR004217. Tim10/DDP_fam_Znf.
    [Graphical view ]
    Pfami PF02953. zf-Tim10_DDP. 1 hit.
    [Graphical view ]
    SUPFAMi SSF144122. SSF144122. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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. "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.
    14. "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.
    15. "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: October 1, 2014
    This is version 131 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