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)

P36543

- VATE1_HUMAN

UniProt

P36543 - VATE1_HUMAN

Protein

V-type proton ATPase subunit E 1

Gene

ATP6V1E1

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 149 (01 Oct 2014)
      Sequence version 1 (01 Jun 1994)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Subunit of the peripheral V1 complex of vacuolar ATPase essential for assembly or catalytic function. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.

    GO - Molecular functioni

    1. ATPase binding Source: UniProtKB
    2. hydrogen-exporting ATPase activity, phosphorylative mechanism Source: Ensembl
    3. protein binding Source: UniProtKB
    4. proton-transporting ATPase activity, rotational mechanism Source: InterPro

    GO - Biological processi

    1. ATP hydrolysis coupled proton transport Source: Ensembl
    2. cellular iron ion homeostasis Source: Reactome
    3. insulin receptor signaling pathway Source: Reactome
    4. interaction with host Source: Reactome
    5. phagosome maturation Source: Reactome
    6. proton transport Source: ProtInc
    7. transferrin transport Source: Reactome
    8. transmembrane transport Source: Reactome

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Hydrogen ion transport, Ion transport, Transport

    Enzyme and pathway databases

    BioCyciMetaCyc:HS05489-MONOMER.
    ReactomeiREACT_1109. Insulin receptor recycling.
    REACT_121256. Phagosomal maturation (early endosomal stage).
    REACT_25283. Transferrin endocytosis and recycling.

    Protein family/group databases

    TCDBi3.A.2.2.4. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    V-type proton ATPase subunit E 1
    Short name:
    V-ATPase subunit E 1
    Alternative name(s):
    V-ATPase 31 kDa subunit
    Short name:
    p31
    Vacuolar proton pump subunit E 1
    Gene namesi
    Name:ATP6V1E1
    Synonyms:ATP6E, ATP6E2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:857. ATP6V1E1.

    Subcellular locationi

    GO - Cellular componenti

    1. apical plasma membrane Source: UniProtKB
    2. cytosol Source: UniProtKB
    3. endosome Source: UniProtKB
    4. extracellular vesicular exosome Source: UniProt
    5. lysosomal membrane Source: UniProtKB
    6. microvillus Source: Ensembl
    7. mitochondrion Source: Ensembl
    8. proton-transporting two-sector ATPase complex Source: ProtInc
    9. proton-transporting two-sector ATPase complex, catalytic domain Source: InterPro

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA25158.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 226225V-type proton ATPase subunit E 1PRO_0000117295Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei56 – 561PhosphotyrosineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP36543.
    PaxDbiP36543.
    PRIDEiP36543.

    2D gel databases

    UCD-2DPAGEP36543.

    PTM databases

    PhosphoSiteiP36543.

    Expressioni

    Tissue specificityi

    Ubiquitous.1 Publication

    Gene expression databases

    ArrayExpressiP36543.
    BgeeiP36543.
    CleanExiHS_ATP6V1E1.
    GenevestigatoriP36543.

    Organism-specific databases

    HPAiCAB009528.
    CAB018699.
    HPA029196.

    Interactioni

    Subunit structurei

    V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (components A to H) attached to an integral membrane V0 proton pore complex (components: a, c, c', c'' and d). Interacts with RABL2/RABL2A; binds preferentially to GTP-bound RABL2 By similarity. Interacts with ALDOC. Interacts with RAB11B.By similarity2 Publications

    Protein-protein interaction databases

    BioGridi107012. 41 interactions.
    IntActiP36543. 7 interactions.
    MINTiMINT-5002575.
    STRINGi9606.ENSP00000253413.

    Structurei

    3D structure databases

    ProteinModelPortaliP36543.
    SMRiP36543. Positions 2-217.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the V-ATPase E subunit family.Curated

    Phylogenomic databases

    eggNOGiCOG1390.
    HOGENOMiHOG000202506.
    HOVERGENiHBG002309.
    InParanoidiP36543.
    KOiK02150.
    OMAiFKQATMS.
    OrthoDBiEOG70PC01.
    PhylomeDBiP36543.
    TreeFamiTF313479.

    Family and domain databases

    HAMAPiMF_00311. ATP_synth_E_arch.
    InterProiIPR002842. ATPase_V1/A1-cplx_esu.
    [Graphical view]
    PfamiPF01991. vATP-synt_E. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P36543-1) [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

    MALSDADVQK QIKHMMAFIE QEANEKAEEI DAKAEEEFNI EKGRLVQTQR    50
    LKIMEYYEKK EKQIEQQKKI QMSNLMNQAR LKVLRARDDL ITDLLNEAKQ 100
    RLSKVVKDTT RYQVLLDGLV LQGLYQLLEP RMIVRCRKQD FPLVKAAVQK 150
    AIPMYKIATK NDVDVQIDQE SYLPEDIAGG VEIYNGDRKI KVSNTLESRL 200
    DLIAQQMMPE VRGALFGANA NRKFLD 226
    Length:226
    Mass (Da):26,145
    Last modified:June 1, 1994 - v1
    Checksum:iDFD0D44E6D9AEA17
    GO
    Isoform 2 (identifier: P36543-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         12-33: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:204
    Mass (Da):23,587
    Checksum:i25B2BADC0BE9B22B
    GO
    Isoform 3 (identifier: P36543-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         93-122: Missing.

    Show »
    Length:196
    Mass (Da):22,706
    Checksum:i32EEBB32390D88A2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti32 – 321A → R in CAA50592. (PubMed:8250920)Curated
    Sequence conflicti86 – 861A → G no nucleotide entry (PubMed:1533641)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti50 – 501R → G in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036565

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei12 – 3322Missing in isoform 2. 1 PublicationVSP_042925Add
    BLAST
    Alternative sequencei93 – 12230Missing in isoform 3. 1 PublicationVSP_044589Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X76228 mRNA. Translation: CAA53814.1.
    X71491 mRNA. Translation: CAA50592.1.
    CR456385 mRNA. Translation: CAG30271.1.
    AK294623 mRNA. Translation: BAG57804.1.
    AK315941 mRNA. Translation: BAH14312.1.
    AC004019 Genomic DNA. No translation available.
    AC006285 Genomic DNA. No translation available.
    AC007666 Genomic DNA. No translation available.
    BC004443 mRNA. Translation: AAH04443.1.
    CCDSiCCDS13745.1. [P36543-1]
    CCDS42977.1. [P36543-2]
    CCDS42978.1. [P36543-3]
    PIRiS60562.
    RefSeqiNP_001034455.1. NM_001039366.1. [P36543-2]
    NP_001034456.1. NM_001039367.1. [P36543-3]
    NP_001687.1. NM_001696.3. [P36543-1]
    UniGeneiHs.517338.

    Genome annotation databases

    EnsembliENST00000253413; ENSP00000253413; ENSG00000131100. [P36543-1]
    ENST00000399796; ENSP00000382694; ENSG00000131100. [P36543-3]
    ENST00000399798; ENSP00000382696; ENSG00000131100. [P36543-2]
    GeneIDi529.
    KEGGihsa:529.
    UCSCiuc002zmr.1. human. [P36543-1]
    uc002zms.1. human.
    uc002zmt.1. human. [P36543-2]

    Polymorphism databases

    DMDMi549207.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X76228 mRNA. Translation: CAA53814.1 .
    X71491 mRNA. Translation: CAA50592.1 .
    CR456385 mRNA. Translation: CAG30271.1 .
    AK294623 mRNA. Translation: BAG57804.1 .
    AK315941 mRNA. Translation: BAH14312.1 .
    AC004019 Genomic DNA. No translation available.
    AC006285 Genomic DNA. No translation available.
    AC007666 Genomic DNA. No translation available.
    BC004443 mRNA. Translation: AAH04443.1 .
    CCDSi CCDS13745.1. [P36543-1 ]
    CCDS42977.1. [P36543-2 ]
    CCDS42978.1. [P36543-3 ]
    PIRi S60562.
    RefSeqi NP_001034455.1. NM_001039366.1. [P36543-2 ]
    NP_001034456.1. NM_001039367.1. [P36543-3 ]
    NP_001687.1. NM_001696.3. [P36543-1 ]
    UniGenei Hs.517338.

    3D structure databases

    ProteinModelPortali P36543.
    SMRi P36543. Positions 2-217.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107012. 41 interactions.
    IntActi P36543. 7 interactions.
    MINTi MINT-5002575.
    STRINGi 9606.ENSP00000253413.

    Protein family/group databases

    TCDBi 3.A.2.2.4. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

    PTM databases

    PhosphoSitei P36543.

    Polymorphism databases

    DMDMi 549207.

    2D gel databases

    UCD-2DPAGE P36543.

    Proteomic databases

    MaxQBi P36543.
    PaxDbi P36543.
    PRIDEi P36543.

    Protocols and materials databases

    DNASUi 529.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000253413 ; ENSP00000253413 ; ENSG00000131100 . [P36543-1 ]
    ENST00000399796 ; ENSP00000382694 ; ENSG00000131100 . [P36543-3 ]
    ENST00000399798 ; ENSP00000382696 ; ENSG00000131100 . [P36543-2 ]
    GeneIDi 529.
    KEGGi hsa:529.
    UCSCi uc002zmr.1. human. [P36543-1 ]
    uc002zms.1. human.
    uc002zmt.1. human. [P36543-2 ]

    Organism-specific databases

    CTDi 529.
    GeneCardsi GC22M018074.
    HGNCi HGNC:857. ATP6V1E1.
    HPAi CAB009528.
    CAB018699.
    HPA029196.
    MIMi 108746. gene.
    neXtProti NX_P36543.
    PharmGKBi PA25158.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1390.
    HOGENOMi HOG000202506.
    HOVERGENi HBG002309.
    InParanoidi P36543.
    KOi K02150.
    OMAi FKQATMS.
    OrthoDBi EOG70PC01.
    PhylomeDBi P36543.
    TreeFami TF313479.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS05489-MONOMER.
    Reactomei REACT_1109. Insulin receptor recycling.
    REACT_121256. Phagosomal maturation (early endosomal stage).
    REACT_25283. Transferrin endocytosis and recycling.

    Miscellaneous databases

    GeneWikii ATP6V1E1.
    GenomeRNAii 529.
    NextBioi 2197.
    PROi P36543.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P36543.
    Bgeei P36543.
    CleanExi HS_ATP6V1E1.
    Genevestigatori P36543.

    Family and domain databases

    HAMAPi MF_00311. ATP_synth_E_arch.
    InterProi IPR002842. ATPase_V1/A1-cplx_esu.
    [Graphical view ]
    Pfami PF01991. vATP-synt_E. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Immunologic evidence that vacuolar H+ ATPases with heterogeneous forms of Mr = 31,000 subunit have different membrane distributions in mammalian kidney."
      Hemken P., Guo X.-L., Wang Z.-Q., Zhang K., Gluck S.
      J. Biol. Chem. 267:9948-9957(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "The E subunit of vacuolar H(+)-ATPase localizes close to the centromere on human chromosome 22."
      Baud V., Mears A., Lamour V., Scamps C., McDermid A., Lipinski M.
      Hum. Mol. Genet. 3:335-339(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Cloning and tissue distribution of subunits C, D, and E of the human vacuolar H(+)-ATPase."
      van Hille B., Vanek M., Richener H., Green J.R., Bilbe G.
      Biochem. Biophys. Res. Commun. 197:15-21(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Osteoclastoma.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    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] (ISOFORMS 2 AND 3).
      Tissue: Brain and Cerebellum.
    6. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      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] (ISOFORM 1).
      Tissue: Lung.
    8. Lubec G., Vishwanath V.
      Submitted (MAR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 112-131, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain and Cajal-Retzius cell.
    9. "Interaction between aldolase and vacuolar H+-ATPase: evidence for direct coupling of glycolysis to the ATP-hydrolyzing proton pump."
      Lu M., Holliday L.S., Zhang L., Dunn W.A. Jr., Gluck S.L.
      J. Biol. Chem. 276:30407-30413(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ALDOC.
    10. "A human gene, ATP6E1, encoding a testis-specific isoform of H(+)-ATPase subunit E."
      Imai-Senga Y., Sun-Wada G.H., Wada Y., Futai M.
      Gene 289:7-12(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Rab11b and its effector Rip11 regulate the acidosis-induced traffic of V-ATPase in salivary ducts."
      Oehlke O., Martin H.W., Osterberg N., Roussa E.
      J. Cell. Physiol. 226:638-651(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RAB11B.
    14. Cited for: VARIANT [LARGE SCALE ANALYSIS] GLY-50.

    Entry informationi

    Entry nameiVATE1_HUMAN
    AccessioniPrimary (citable) accession number: P36543
    Secondary accession number(s): A8MUE4, A8MUN4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 149 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 22
      Human chromosome 22: 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