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Q15904

- VAS1_HUMAN

UniProt

Q15904 - VAS1_HUMAN

Protein

V-type proton ATPase subunit S1

Gene

ATP6AP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 2 (11 Jan 2001)
      Previous versions | rss
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    Functioni

    Vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.By similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. proton-transporting ATPase activity, rotational mechanism Source: InterPro
    3. proton-transporting ATP synthase activity, rotational mechanism Source: InterPro
    4. Rab GTPase binding Source: UniProt
    5. transporter activity Source: ProtInc

    GO - Biological processi

    1. ATP hydrolysis coupled proton transport Source: InterPro
    2. establishment of organelle localization Source: UniProt
    3. pH reduction Source: UniProt
    4. positive regulation of bone resorption Source: UniProt
    5. positive regulation of ERK1 and ERK2 cascade Source: UniProt
    6. positive regulation of exocytosis Source: UniProt
    7. positive regulation of osteoblast differentiation Source: UniProt
    8. positive regulation of osteoclast development Source: UniProt
    9. proton transport Source: ProtInc

    Keywords - Biological processi

    Hydrogen ion transport, Ion transport, Transport

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS01034-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    V-type proton ATPase subunit S1
    Short name:
    V-ATPase subunit S1
    Alternative name(s):
    Protein XAP-3
    V-ATPase Ac45 subunit
    V-ATPase S1 accessory protein
    Vacuolar proton pump subunit S1
    Gene namesi
    Name:ATP6AP1
    Synonyms:ATP6IP1, ATP6S1, VATPS1, XAP3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:868. ATP6AP1.

    Subcellular locationi

    Vacuole membrane By similarity; Single-pass membrane protein By similarity

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. integral component of membrane Source: UniProtKB-KW
    3. proton-transporting two-sector ATPase complex Source: ProtInc
    4. proton-transporting V-type ATPase, V1 domain Source: InterPro
    5. vacuolar membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Membrane, Vacuole

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA25145.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 4141Sequence AnalysisAdd
    BLAST
    Chaini42 – 470429V-type proton ATPase subunit S1PRO_0000002543Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi170 – 1701N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi261 – 2611N-linked (GlcNAc...)1 Publication
    Glycosylationi273 – 2731N-linked (GlcNAc...)1 Publication
    Glycosylationi296 – 2961N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi303 – 3031N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi350 – 3501N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi357 – 3571N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    MaxQBiQ15904.
    PaxDbiQ15904.
    PRIDEiQ15904.

    PTM databases

    PhosphoSiteiQ15904.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Gene expression databases

    ArrayExpressiQ15904.
    BgeeiQ15904.
    CleanExiHS_ATP6AP1.
    GenevestigatoriQ15904.

    Organism-specific databases

    HPAiCAB015218.

    Interactioni

    Subunit structurei

    Composed of at least 10 subunits.

    Protein-protein interaction databases

    BioGridi107019. 10 interactions.
    IntActiQ15904. 5 interactions.
    MINTiMINT-4722342.
    STRINGi9606.ENSP00000358777.

    Structurei

    3D structure databases

    ProteinModelPortaliQ15904.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini42 – 419378VacuolarSequence AnalysisAdd
    BLAST
    Topological domaini441 – 47030CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei420 – 44021HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the vacuolar ATPase subunit S1 family.Curated

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG322101.
    HOGENOMiHOG000000706.
    HOVERGENiHBG001090.
    InParanoidiQ15904.
    KOiK03662.
    OMAiGHITSDM.
    PhylomeDBiQ15904.
    TreeFamiTF325819.

    Family and domain databases

    InterProiIPR008388. ATPase_V1-cplx_s1su.
    IPR024722. BIG/ATPase_V1_suS1.
    [Graphical view]
    PANTHERiPTHR12471. PTHR12471. 1 hit.
    PfamiPF05827. ATP-synt_S1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q15904-1 [UniParc]FASTAAdd to Basket

    « Hide

    MMAAMATARV RMGPRCAQAL WRMPWLPVFL SLAAAAAAAA AEQQVPLVLW    50
    SSDRDLWAPA ADTHEGHITS DLQLSTYLDP ALELGPRNVL LFLQDKLSIE 100
    DFTAYGGVFG NKQDSAFSNL ENALDLAPSS LVLPAVDWYA VSTLTTYLQE 150
    KLGASPLHVD LATLRELKLN ASLPALLLIR LPYTASSGLM APREVLTGND 200
    EVIGQVLSTL KSEDVPYTAA LTAVRPSRVA RDVAVVAGGL GRQLLQKQPV 250
    SPVIHPPVSY NDTAPRILFW AQNFSVAYKD QWEDLTPLTF GVQELNLTGS 300
    FWNDSFARLS LTYERLFGTT VTFKFILANR LYPVSARHWF TMERLEVHSN 350
    GSVAYFNASQ VTGPSIYSFH CEYVSSLSKK GSLLVARTQP SPWQMMLQDF 400
    QIQAFNVMGE QFSYASDCAS FFSPGIWMGL LTSLFMLFIF TYGLHMILSL 450
    KTMDRFDDHK GPTISLTQIV 470
    Length:470
    Mass (Da):52,026
    Last modified:January 11, 2001 - v2
    Checksum:iA71C7EF0E90D0652
    GO

    Sequence cautioni

    The sequence BAA03938.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence CAB66785.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti68 – 681I → V in BAC11520. (PubMed:16303743)Curated
    Sequence conflicti74 – 741L → P in BAC11520. (PubMed:16303743)Curated
    Sequence conflicti229 – 2291V → A in AK026519. (PubMed:14702039)Curated
    Sequence conflicti307 – 3071A → T in AK026519. (PubMed:14702039)Curated
    Sequence conflicti335 – 3351S → F in AK026519. (PubMed:14702039)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L44140 Genomic DNA. No translation available.
    AL136851 mRNA. Translation: CAB66785.1. Different initiation.
    AK026519 mRNA. No translation available.
    AK289452 mRNA. Translation: BAF82141.1.
    AK075284 mRNA. Translation: BAC11520.1.
    BX936347, BX936385 Genomic DNA. Translation: CAI43213.3.
    BX936385, BX936347 Genomic DNA. Translation: CAI95782.2.
    CH471172 Genomic DNA. Translation: EAW72715.1.
    BC000724 mRNA. Translation: AAH00724.1.
    D16469 mRNA. Translation: BAA03938.1. Different initiation.
    CCDSiCCDS35451.1.
    RefSeqiNP_001174.2. NM_001183.5.
    UniGeneiHs.633817.
    Hs.6551.

    Genome annotation databases

    EnsembliENST00000369762; ENSP00000358777; ENSG00000071553.
    GeneIDi537.
    KEGGihsa:537.
    UCSCiuc004flf.1. human.

    Polymorphism databases

    DMDMi12230759.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L44140 Genomic DNA. No translation available.
    AL136851 mRNA. Translation: CAB66785.1 . Different initiation.
    AK026519 mRNA. No translation available.
    AK289452 mRNA. Translation: BAF82141.1 .
    AK075284 mRNA. Translation: BAC11520.1 .
    BX936347 , BX936385 Genomic DNA. Translation: CAI43213.3 .
    BX936385 , BX936347 Genomic DNA. Translation: CAI95782.2 .
    CH471172 Genomic DNA. Translation: EAW72715.1 .
    BC000724 mRNA. Translation: AAH00724.1 .
    D16469 mRNA. Translation: BAA03938.1 . Different initiation.
    CCDSi CCDS35451.1.
    RefSeqi NP_001174.2. NM_001183.5.
    UniGenei Hs.633817.
    Hs.6551.

    3D structure databases

    ProteinModelPortali Q15904.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107019. 10 interactions.
    IntActi Q15904. 5 interactions.
    MINTi MINT-4722342.
    STRINGi 9606.ENSP00000358777.

    Chemistry

    BindingDBi Q15904.
    ChEMBLi CHEMBL4790.

    PTM databases

    PhosphoSitei Q15904.

    Polymorphism databases

    DMDMi 12230759.

    Proteomic databases

    MaxQBi Q15904.
    PaxDbi Q15904.
    PRIDEi Q15904.

    Protocols and materials databases

    DNASUi 537.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000369762 ; ENSP00000358777 ; ENSG00000071553 .
    GeneIDi 537.
    KEGGi hsa:537.
    UCSCi uc004flf.1. human.

    Organism-specific databases

    CTDi 537.
    GeneCardsi GC0XP153657.
    HGNCi HGNC:868. ATP6AP1.
    HPAi CAB015218.
    MIMi 300197. gene.
    neXtProti NX_Q15904.
    PharmGKBi PA25145.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG322101.
    HOGENOMi HOG000000706.
    HOVERGENi HBG001090.
    InParanoidi Q15904.
    KOi K03662.
    OMAi GHITSDM.
    PhylomeDBi Q15904.
    TreeFami TF325819.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS01034-MONOMER.

    Miscellaneous databases

    GeneWikii ATP6AP1.
    GenomeRNAii 537.
    NextBioi 2227.
    PROi Q15904.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15904.
    Bgeei Q15904.
    CleanExi HS_ATP6AP1.
    Genevestigatori Q15904.

    Family and domain databases

    InterProi IPR008388. ATPase_V1-cplx_s1su.
    IPR024722. BIG/ATPase_V1_suS1.
    [Graphical view ]
    PANTHERi PTHR12471. PTHR12471. 1 hit.
    Pfami PF05827. ATP-synt_S1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Long-range sequence analysis in Xq28: thirteen known and six candidate genes in 219.4 kb of high GC DNA between the RCP/GCP and G6PD loci."
      Chen E.Y., Zollo M., Mazzarella R.A., Ciccodicola A., Chen C.-N., Zuo L., Heiner C., Burough F.W., Ripetto M., Schlessinger D., D'Urso M.
      Hum. Mol. Genet. 5:659-668(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Testis.
    3. "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].
    4. "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
      Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.
      , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
      DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    5. "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].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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: Kidney.
    8. "Isolation of expressed sequences encoded by the human Xq terminal portion using microclone probes generated by laser microdissection."
      Yokoi H., Hadano S., Kogi M., Kang X., Wakasa K., Ikeda J.
      Genomics 20:404-411(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 97-470.
      Tissue: Brain.
    9. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-261 AND ASN-273.
      Tissue: Liver.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiVAS1_HUMAN
    AccessioniPrimary (citable) accession number: Q15904
    Secondary accession number(s): A6ZKI4, Q8NBT4, Q9H0C7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 11, 2001
    Last sequence update: January 11, 2001
    Last modified: October 1, 2014
    This is version 143 of the entry and version 2 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. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3