Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q96E52

- OMA1_HUMAN

UniProt

Q96E52 - OMA1_HUMAN

Protein

Metalloendopeptidase OMA1, mitochondrial

Gene

OMA1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Metalloprotease that is part of the quality control system in the inner membrane of mitochondria. Following stress conditions that induce loss of mitochondrial membrane potential, mediates cleavage of OPA1 at S1 position, leading to OPA1 inactivation and negative regulation of mitochondrial fusion. Its role in mitochondrial quality control is essential for regulating lipid metabolism as well as to maintain body temperature and energy expenditure under cold-stress conditions.1 Publication

    Cofactori

    Binds 1 zinc ion per subunit.Curated

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi327 – 3271Zinc; catalyticPROSITE-ProRule annotation
    Active sitei328 – 3281PROSITE-ProRule annotation
    Metal bindingi331 – 3311Zinc; catalyticCurated
    Metal bindingi392 – 3921Zinc; catalyticPROSITE-ProRule annotation

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. metalloendopeptidase activity Source: UniProtKB

    GO - Biological processi

    1. cristae formation Source: Ensembl
    2. diet induced thermogenesis Source: UniProtKB
    3. energy homeostasis Source: UniProtKB
    4. glucose metabolic process Source: UniProtKB
    5. lipid metabolic process Source: UniProtKB
    6. misfolded or incompletely synthesized protein catabolic process Source: UniProtKB
    7. mitochondrial protein processing Source: Ensembl
    8. negative regulation of mitochondrial fusion Source: UniProtKB
    9. response to stress Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Metal-binding, Zinc

    Protein family/group databases

    MEROPSiM48.017.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Metalloendopeptidase OMA1, mitochondrial (EC:3.4.24.-)
    Alternative name(s):
    Metalloprotease-related protein 1
    Short name:
    MPRP-1
    Overlapping with the m-AAA protease 1 homolog
    Gene namesi
    Name:OMA1
    Synonyms:MPRP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:29661. OMA1.

    Subcellular locationi

    Mitochondrion inner membrane 1 Publication; Multi-pass membrane protein 1 Publication

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. mitochondrial inner membrane Source: UniProtKB-SubCell
    3. mitochondrial membrane Source: UniProtKB

    Keywords - Cellular componenti

    Membrane, Mitochondrion, Mitochondrion inner membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi331 – 3311H → A: Abolishes ability to cleave OPA1 at S1 position. 1 Publication

    Organism-specific databases

    PharmGKBiPA134911478.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 1313MitochondrionSequence AnalysisAdd
    BLAST
    Chaini14 – 524511Metalloendopeptidase OMA1, mitochondrialPRO_0000302809Add
    BLAST

    Post-translational modificationi

    In normal conditions, cleaved into an inactive 40 kDa form. Following CCCP treatment that induces loss of mitochondrial membrane potential, the 40 kDa form is reduced in favor of an active 60 kDa form.1 Publication

    Proteomic databases

    MaxQBiQ96E52.
    PaxDbiQ96E52.
    PRIDEiQ96E52.

    PTM databases

    PhosphoSiteiQ96E52.

    Expressioni

    Tissue specificityi

    Widely expressed, with strong expression in the heart, skeletal muscle, kidney and liver.1 Publication

    Gene expression databases

    BgeeiQ96E52.
    CleanExiHS_OMA1.
    GenevestigatoriQ96E52.

    Organism-specific databases

    HPAiHPA055120.

    Interactioni

    Protein-protein interaction databases

    IntActiQ96E52. 1 interaction.
    STRINGi9606.ENSP00000360270.

    Structurei

    3D structure databases

    ProteinModelPortaliQ96E52.
    SMRiQ96E52. Positions 282-455.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei196 – 21621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei341 – 36121HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M48 family.Curated

    Keywords - Domaini

    Transit peptide, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0501.
    HOVERGENiHBG096685.
    InParanoidiQ96E52.
    OMAiKLSMKHF.
    PhylomeDBiQ96E52.
    TreeFamiTF329133.

    Family and domain databases

    InterProiIPR001915. Peptidase_M48.
    [Graphical view]
    PfamiPF01435. Peptidase_M48. 1 hit.
    [Graphical view]
    PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q96E52-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MSFICGLQSA ARNHVFFRFN SLSNWRKCNT LASTSRGCHQ VQVNHIVNKY    50
    QGLGVNQCDR WSFLPGNFHF YSTFNNKRTG GLSSTKSKEI WRITSKCTVW 100
    NDAFSRQLLI KEVTAVPSLS VLHPLSPASI RAIRNFHTSP RFQAAPVPLL 150
    LMILKPVQKL FAIIVGRGIR KWWQALPPNK KEVVKENIRK NKWKLFLGLS 200
    SFGLLFVVFY FTHLEVSPIT GRSKLLLLGK EQFRLLSELE YEAWMEEFKN 250
    DMLTEKDARY LAVKEVLCHL IECNKDVPGI SQINWVIHVV DSPIINAFVL 300
    PNGQMFVFTG FLNSVTDIHQ LSFLLGHEIA HAVLGHAAEK AGMVHLLDFL 350
    GMIFLTMIWA ICPRDSLALL CQWIQSKLQE YMFNRPYSRK LEAEADKIGL 400
    LLAAKACADI RASSVFWQQM EFVDSLHGQP KMPEWLSTHP SHGNRVEYLD 450
    RLIPQALKIR EMCNCPPLSN PDPRLLFKLS TKHFLEESEK EDLNITKKQK 500
    MDTLPIQKQE QIPLTYIVEK RTGS 524
    Length:524
    Mass (Da):60,120
    Last modified:December 1, 2001 - v1
    Checksum:iF8F9B37489B0EFF1
    GO
    Isoform 2 (identifier: Q96E52-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         456-524: ALKIREMCNC...TYIVEKRTGS → LVREEKFIEQPEQIAELTLNSFIQNTEICRS

    Note: No experimental confirmation available.

    Show »
    Length:486
    Mass (Da):55,744
    Checksum:iF2D48060E2D25826
    GO

    Sequence cautioni

    The sequence BAC03583.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence CAI13522.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAI13523.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAI13524.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAI13525.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAI13526.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAI22238.1 differs from that shown. Reason: Erroneous gene model prediction.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti67 – 671N → K.
    Corresponds to variant rs34466938 [ dbSNP | Ensembl ].
    VAR_034958
    Natural varianti69 – 691H → Y in a patient with amyotrophic lateral sclerosis. 1 Publication
    Corresponds to variant rs75220198 [ dbSNP | Ensembl ].
    VAR_065755
    Natural varianti117 – 1171P → L.1 Publication
    Corresponds to variant rs17117720 [ dbSNP | Ensembl ].
    VAR_034959
    Natural varianti211 – 2111F → C.
    Corresponds to variant rs17117699 [ dbSNP | Ensembl ].
    VAR_034960
    Natural varianti226 – 2261L → V in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_035708
    Natural varianti272 – 2721E → G in a patient with amyotrophic lateral sclerosis. 1 Publication
    VAR_065756
    Natural varianti329 – 3291I → L.1 Publication
    Corresponds to variant rs17117678 [ dbSNP | Ensembl ].
    VAR_034961
    Natural varianti365 – 3651D → Y.1 Publication
    Corresponds to variant rs77980955 [ dbSNP | Ensembl ].
    VAR_065757

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei456 – 52469ALKIR…KRTGS → LVREEKFIEQPEQIAELTLN SFIQNTEICRS in isoform 2. 1 PublicationVSP_027958Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB048348 mRNA. Translation: BAC79381.1.
    AL365187 Genomic DNA. Translation: CAI13522.1. Sequence problems.
    AL365187 Genomic DNA. Translation: CAI13523.1. Sequence problems.
    AL365187 Genomic DNA. Translation: CAI13524.1. Sequence problems.
    AL365187 Genomic DNA. Translation: CAI13525.1. Sequence problems.
    AL365187, AL109845 Genomic DNA. Translation: CAI13526.1. Sequence problems.
    AL109845, AL365187 Genomic DNA. Translation: CAI22238.1. Sequence problems.
    AL365187, AL109845 Genomic DNA. Translation: CAI13527.1.
    AL109845, AL365187 Genomic DNA. Translation: CAI22239.1.
    CH471059 Genomic DNA. Translation: EAX06631.1.
    CH471059 Genomic DNA. Translation: EAX06632.1.
    CH471059 Genomic DNA. Translation: EAX06633.1.
    BC012915 mRNA. Translation: AAH12915.1.
    AK091101 mRNA. Translation: BAC03583.1. Different initiation.
    CCDSiCCDS608.1. [Q96E52-1]
    RefSeqiNP_660286.1. NM_145243.3. [Q96E52-1]
    UniGeneiHs.425769.

    Genome annotation databases

    EnsembliENST00000371226; ENSP00000360270; ENSG00000162600. [Q96E52-1]
    GeneIDi115209.
    KEGGihsa:115209.
    UCSCiuc001cyx.1. human. [Q96E52-2]
    uc001cyy.3. human. [Q96E52-1]

    Polymorphism databases

    DMDMi74751828.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB048348 mRNA. Translation: BAC79381.1 .
    AL365187 Genomic DNA. Translation: CAI13522.1 . Sequence problems.
    AL365187 Genomic DNA. Translation: CAI13523.1 . Sequence problems.
    AL365187 Genomic DNA. Translation: CAI13524.1 . Sequence problems.
    AL365187 Genomic DNA. Translation: CAI13525.1 . Sequence problems.
    AL365187 , AL109845 Genomic DNA. Translation: CAI13526.1 . Sequence problems.
    AL109845 , AL365187 Genomic DNA. Translation: CAI22238.1 . Sequence problems.
    AL365187 , AL109845 Genomic DNA. Translation: CAI13527.1 .
    AL109845 , AL365187 Genomic DNA. Translation: CAI22239.1 .
    CH471059 Genomic DNA. Translation: EAX06631.1 .
    CH471059 Genomic DNA. Translation: EAX06632.1 .
    CH471059 Genomic DNA. Translation: EAX06633.1 .
    BC012915 mRNA. Translation: AAH12915.1 .
    AK091101 mRNA. Translation: BAC03583.1 . Different initiation.
    CCDSi CCDS608.1. [Q96E52-1 ]
    RefSeqi NP_660286.1. NM_145243.3. [Q96E52-1 ]
    UniGenei Hs.425769.

    3D structure databases

    ProteinModelPortali Q96E52.
    SMRi Q96E52. Positions 282-455.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q96E52. 1 interaction.
    STRINGi 9606.ENSP00000360270.

    Protein family/group databases

    MEROPSi M48.017.

    PTM databases

    PhosphoSitei Q96E52.

    Polymorphism databases

    DMDMi 74751828.

    Proteomic databases

    MaxQBi Q96E52.
    PaxDbi Q96E52.
    PRIDEi Q96E52.

    Protocols and materials databases

    DNASUi 115209.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000371226 ; ENSP00000360270 ; ENSG00000162600 . [Q96E52-1 ]
    GeneIDi 115209.
    KEGGi hsa:115209.
    UCSCi uc001cyx.1. human. [Q96E52-2 ]
    uc001cyy.3. human. [Q96E52-1 ]

    Organism-specific databases

    CTDi 115209.
    GeneCardsi GC01M058881.
    H-InvDB HIX0077405.
    HGNCi HGNC:29661. OMA1.
    HPAi HPA055120.
    neXtProti NX_Q96E52.
    PharmGKBi PA134911478.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0501.
    HOVERGENi HBG096685.
    InParanoidi Q96E52.
    OMAi KLSMKHF.
    PhylomeDBi Q96E52.
    TreeFami TF329133.

    Miscellaneous databases

    GenomeRNAii 115209.
    NextBioi 79540.
    PROi Q96E52.

    Gene expression databases

    Bgeei Q96E52.
    CleanExi HS_OMA1.
    Genevestigatori Q96E52.

    Family and domain databases

    InterProi IPR001915. Peptidase_M48.
    [Graphical view ]
    Pfami PF01435. Peptidase_M48. 1 hit.
    [Graphical view ]
    PROSITEi PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of a human cDNA sequence which encodes a novel membrane-associated protein containing a zinc metalloprotease motif."
      Bao Y.-C., Tsuruga H., Hirai M., Yasuda K., Yokoi N., Kitamura T., Kumagai H.
      DNA Res. 10:123-128(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    2. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. 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] (ISOFORM 1).
      Tissue: Liver.
    5. "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] OF 160-524 (ISOFORM 2).
      Tissue: Substantia nigra.
    6. "Inducible proteolytic inactivation of OPA1 mediated by the OMA1 protease in mammalian cells."
      Head B., Griparic L., Amiri M., Gandre-Babbe S., van der Bliek A.M.
      J. Cell Biol. 187:959-966(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING, MUTAGENESIS OF HIS-331.
    7. Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-226.
    8. "Resequencing of 29 candidate genes in patients with familial and sporadic amyotrophic lateral sclerosis."
      Daoud H., Valdmanis P.N., Gros-Louis F., Belzil V., Spiegelman D., Henrion E., Diallo O., Desjarlais A., Gauthier J., Camu W., Dion P.A., Rouleau G.A.
      Arch. Neurol. 68:587-593(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS TYR-69; LEU-117; GLY-272; LEU-329 AND TYR-365.

    Entry informationi

    Entry nameiOMA1_HUMAN
    AccessioniPrimary (citable) accession number: Q96E52
    Secondary accession number(s): D3DQ54
    , Q5T3G6, Q5T3G7, Q5T3G8, Q5T3G9, Q5T3H0, Q8NBB3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 11, 2007
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 109 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 1
      Human chromosome 1: 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. Peptidase families
      Classification of peptidase families and list of entries
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3