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P36543

- VATE1_HUMAN

UniProt

P36543 - VATE1_HUMAN

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Protein
V-type proton ATPase subunit E 1
Gene
ATP6V1E1, ATP6E, ATP6E2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.UniRule annotation

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
Complete GO annotation...

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
Complete GO annotation...

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
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
Complete GO annotation...

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 1UniRule annotation
PRO_0000117295Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei56 – 561Phosphotyrosine By 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.2 Publications

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliP36543.
SMRiP36543. Positions 2-217.

Family & Domainsi

Sequence similaritiesi

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

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.
VSP_042925Add
BLAST
Alternative sequencei93 – 12230Missing in isoform 3.
VSP_044589Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti32 – 321A → R in CAA50592. 1 Publication
Sequence conflicti86 – 861A → G no nucleotide entry 1 Publication

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...

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 148 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

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