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Protein

Phosphatidylethanolamine N-methyltransferase

Gene

PEMT

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

Functioni

Catalyzes three sequential methylation reactions of phosphatidylethanolamine (PE) by AdoMet, thereby producing phosphatidylcholine (PC).

Catalytic activityi

S-adenosyl-L-methionine + phosphatidyl-N-methylethanolamine = S-adenosyl-L-homocysteine + phosphatidyl-N-dimethylethanolamine.PROSITE-ProRule annotation
S-adenosyl-L-methionine + phosphatidyl-N-dimethylethanolamine = S-adenosyl-L-homocysteine + phosphatidylcholine.PROSITE-ProRule annotation
S-adenosyl-L-methionine + phosphatidylethanolamine = S-adenosyl-L-homocysteine + phosphatidyl-N-methylethanolamine.PROSITE-ProRule annotation

Enzyme regulationi

The first methylation is rate-limiting.

Pathwayi

GO - Molecular functioni

GO - Biological processi

  • cell proliferation Source: ProtInc
  • glycerophospholipid biosynthetic process Source: Reactome
  • lipid metabolic process Source: ProtInc
  • phosphatidylcholine biosynthetic process Source: Reactome
  • phospholipid metabolic process Source: Reactome
  • positive regulation of protein targeting to mitochondrion Source: ParkinsonsUK-UCL
  • small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BRENDAi2.1.1.17. 2681.
ReactomeiREACT_121238. Synthesis of PC.
UniPathwayiUPA00753.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylethanolamine N-methyltransferase (EC:2.1.1.17, EC:2.1.1.71)
Short name:
PEAMT
Short name:
PEMT
Alternative name(s):
PEMT2
Gene namesi
Name:PEMT
Synonyms:PEMPT, PNMT
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:8830. PEMT.

Subcellular locationi

Isoform 1 :
Isoform 2 :

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 1211LumenalSequence AnalysisAdd
BLAST
Intramembranei13 – 3321HelicalSequence AnalysisAdd
BLAST
Topological domaini34 – 4512LumenalSequence AnalysisAdd
BLAST
Transmembranei46 – 6621HelicalSequence AnalysisAdd
BLAST
Topological domaini67 – 9327CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei94 – 11421HelicalSequence AnalysisAdd
BLAST
Topological domaini115 – 15743LumenalSequence AnalysisAdd
BLAST
Transmembranei158 – 17821HelicalSequence AnalysisAdd
BLAST
Topological domaini179 – 19921CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33175.

Polymorphism and mutation databases

BioMutaiPEMT.
DMDMi148887406.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 199198Phosphatidylethanolamine N-methyltransferasePRO_0000193920Add
BLAST

Post-translational modificationi

Isoform 2 is N-glycosylated with high-mannose oligosaccharides.1 Publication

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ9UBM1.
PaxDbiQ9UBM1.

Expressioni

Gene expression databases

BgeeiQ9UBM1.
CleanExiHS_PEMT.
HS_PNMT.
ExpressionAtlasiQ9UBM1. baseline and differential.
GenevestigatoriQ9UBM1.

Organism-specific databases

HPAiHPA042375.

Interactioni

Protein-protein interaction databases

BioGridi115672. 1 interaction.
STRINGi9606.ENSP00000255389.

Structurei

3D structure databases

ProteinModelPortaliQ9UBM1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the class VI-like SAM-binding methyltransferase superfamily. PEMT/PEM2 methyltransferase family.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG261676.
GeneTreeiENSGT00390000007041.
HOGENOMiHOG000208789.
HOVERGENiHBG000990.
InParanoidiQ9UBM1.
KOiK00551.
OMAiTSTWALG.
OrthoDBiEOG7TQV20.
PhylomeDBiQ9UBM1.
TreeFamiTF300198.

Family and domain databases

InterProiIPR024960. PEMT/MFAP.
IPR007318. Phopholipid_MeTrfase.
[Graphical view]
PANTHERiPTHR15458. PTHR15458. 1 hit.
PfamiPF04191. PEMT. 1 hit.
[Graphical view]
PIRSFiPIRSF005444. PEMT. 1 hit.
PROSITEiPS51599. SAM_PEMT_PEM2. 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. AlignAdd to basket

Isoform 1 (identifier: Q9UBM1-1) [UniParc]FASTAAdd to basket

Also known as: PEMT-S

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

        10         20         30         40         50
MTRLLGYVDP LDPSFVAAVI TITFNPLYWN VVARWEHKTR KLSRAFGSPY
60 70 80 90 100
LACYSLSVTI LLLNFLRSHC FTQAMLSQPR MESLDTPAAY SLGLALLGLG
110 120 130 140 150
VVLVLSSFFA LGFAGTFLGD YFGILKEARV TVFPFNILDN PMYWGSTANY
160 170 180 190
LGWAIMHASP TGLLLTVLVA LTYIVALLYE EPFTAEIYRQ KASGSHKRS
Length:199
Mass (Da):22,134
Last modified:June 12, 2007 - v4
Checksum:i98C07AB54B3B4E6A
GO
Isoform 2 (identifier: Q9UBM1-2) [UniParc]FASTAAdd to basket

Also known as: PEMT-L

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MKRSGNPGAEVTNSSVAGPDCCGGLGNIDFRQADFCVM

Note: Much lower enzymatic activity than isoform 1.1 Publication

Show »
Length:236
Mass (Da):25,890
Checksum:i024AEDF227E93FEE
GO
Isoform 3 (identifier: Q9UBM1-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MKRSGNPGAEVTNSSVAGPDCCGGLGNIDFRQADFCVM
     156-199: MHASPTGLLL...QKASGSHKRS → IPAPAGAVGS...GSPIRRALHR

Note: No experimental confirmation available.Curated

Show »
Length:232
Mass (Da):24,967
Checksum:iACB01FB93D481894
GO

Sequence cautioni

The sequence AAF14867.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Isoform 3 (identifier: Q9UBM1-3)
Sequence conflicti222 – 2221S → N in BAG63603 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti3 – 31R → W.
Corresponds to variant rs70959686 [ dbSNP | Ensembl ].
VAR_055372
Natural varianti58 – 581V → I.4 Publications
Corresponds to variant rs897453 [ dbSNP | Ensembl ].
VAR_032771
Natural varianti58 – 581V → L.
Corresponds to variant rs897453 [ dbSNP | Ensembl ].
VAR_060083
Natural varianti175 – 1751V → M.6 Publications
Corresponds to variant rs7946 [ dbSNP | Ensembl ].
VAR_016093
Natural varianti194 – 1941G → R.
Corresponds to variant rs70965427 [ dbSNP | Ensembl ].
VAR_055373
Isoform 2 (identifier: Q9UBM1-2)
Natural varianti11 – 111V → A.1 Publication

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MKRSGNPGAEVTNSSVAGPD CCGGLGNIDFRQADFCVM in isoform 2 and isoform 3. 2 PublicationsVSP_037311
Alternative sequencei156 – 19944MHASP…SHKRS → IPAPAGAVGSEARQPHGPAP DGAGGPHLHSGSPIRRALHR in isoform 3. 1 PublicationVSP_046034Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF176807 mRNA. Translation: AAD53292.1.
AF176806 mRNA. Translation: AAD53291.1.
AF294468
, AF294463, AF294464, AF294465, AF294466, AF294467 Genomic DNA. Translation: AAK19172.1.
AB029821 mRNA. Translation: BAA82407.1.
AF113126 mRNA. Translation: AAF14867.1. Different initiation.
AK302251 mRNA. Translation: BAG63603.1.
CR457099 mRNA. Translation: CAG33380.1.
EU574003 Genomic DNA. Translation: ACB21050.1.
AC020558 Genomic DNA. No translation available.
CH471196 Genomic DNA. Translation: EAW55701.1.
CH471196 Genomic DNA. Translation: EAW55702.1.
BC000557 mRNA. Translation: AAH00557.1.
BC050593 mRNA. Translation: AAH50593.1.
CCDSiCCDS11186.1. [Q9UBM1-2]
CCDS11187.1. [Q9UBM1-1]
CCDS58520.1. [Q9UBM1-3]
RefSeqiNP_001254480.1. NM_001267551.1.
NP_001254481.1. NM_001267552.1. [Q9UBM1-3]
NP_009100.2. NM_007169.2. [Q9UBM1-1]
NP_680477.1. NM_148172.2. [Q9UBM1-2]
NP_680478.1. NM_148173.1. [Q9UBM1-1]
UniGeneiHs.714193.

Genome annotation databases

EnsembliENST00000255389; ENSP00000255389; ENSG00000133027. [Q9UBM1-2]
ENST00000395781; ENSP00000379127; ENSG00000133027. [Q9UBM1-3]
ENST00000395782; ENSP00000379128; ENSG00000133027. [Q9UBM1-1]
ENST00000395783; ENSP00000379129; ENSG00000133027. [Q9UBM1-1]
GeneIDi10400.
KEGGihsa:10400.
UCSCiuc002grj.3. human. [Q9UBM1-1]
uc002grl.4. human. [Q9UBM1-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF176807 mRNA. Translation: AAD53292.1.
AF176806 mRNA. Translation: AAD53291.1.
AF294468
, AF294463, AF294464, AF294465, AF294466, AF294467 Genomic DNA. Translation: AAK19172.1.
AB029821 mRNA. Translation: BAA82407.1.
AF113126 mRNA. Translation: AAF14867.1. Different initiation.
AK302251 mRNA. Translation: BAG63603.1.
CR457099 mRNA. Translation: CAG33380.1.
EU574003 Genomic DNA. Translation: ACB21050.1.
AC020558 Genomic DNA. No translation available.
CH471196 Genomic DNA. Translation: EAW55701.1.
CH471196 Genomic DNA. Translation: EAW55702.1.
BC000557 mRNA. Translation: AAH00557.1.
BC050593 mRNA. Translation: AAH50593.1.
CCDSiCCDS11186.1. [Q9UBM1-2]
CCDS11187.1. [Q9UBM1-1]
CCDS58520.1. [Q9UBM1-3]
RefSeqiNP_001254480.1. NM_001267551.1.
NP_001254481.1. NM_001267552.1. [Q9UBM1-3]
NP_009100.2. NM_007169.2. [Q9UBM1-1]
NP_680477.1. NM_148172.2. [Q9UBM1-2]
NP_680478.1. NM_148173.1. [Q9UBM1-1]
UniGeneiHs.714193.

3D structure databases

ProteinModelPortaliQ9UBM1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115672. 1 interaction.
STRINGi9606.ENSP00000255389.

Polymorphism and mutation databases

BioMutaiPEMT.
DMDMi148887406.

Proteomic databases

MaxQBiQ9UBM1.
PaxDbiQ9UBM1.

Protocols and materials databases

DNASUi10400.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000255389; ENSP00000255389; ENSG00000133027. [Q9UBM1-2]
ENST00000395781; ENSP00000379127; ENSG00000133027. [Q9UBM1-3]
ENST00000395782; ENSP00000379128; ENSG00000133027. [Q9UBM1-1]
ENST00000395783; ENSP00000379129; ENSG00000133027. [Q9UBM1-1]
GeneIDi10400.
KEGGihsa:10400.
UCSCiuc002grj.3. human. [Q9UBM1-1]
uc002grl.4. human. [Q9UBM1-2]

Organism-specific databases

CTDi10400.
GeneCardsiGC17M017408.
HGNCiHGNC:8830. PEMT.
HPAiHPA042375.
MIMi602391. gene.
neXtProtiNX_Q9UBM1.
PharmGKBiPA33175.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG261676.
GeneTreeiENSGT00390000007041.
HOGENOMiHOG000208789.
HOVERGENiHBG000990.
InParanoidiQ9UBM1.
KOiK00551.
OMAiTSTWALG.
OrthoDBiEOG7TQV20.
PhylomeDBiQ9UBM1.
TreeFamiTF300198.

Enzyme and pathway databases

UniPathwayiUPA00753.
BRENDAi2.1.1.17. 2681.
ReactomeiREACT_121238. Synthesis of PC.

Miscellaneous databases

ChiTaRSiPEMT. human.
GeneWikiiPhosphatidyl_ethanolamine_methyltransferase.
GenomeRNAii10400.
NextBioi39408.
PROiQ9UBM1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UBM1.
CleanExiHS_PEMT.
HS_PNMT.
ExpressionAtlasiQ9UBM1. baseline and differential.
GenevestigatoriQ9UBM1.

Family and domain databases

InterProiIPR024960. PEMT/MFAP.
IPR007318. Phopholipid_MeTrfase.
[Graphical view]
PANTHERiPTHR15458. PTHR15458. 1 hit.
PfamiPF04191. PEMT. 1 hit.
[Graphical view]
PIRSFiPIRSF005444. PEMT. 1 hit.
PROSITEiPS51599. SAM_PEMT_PEM2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of three novel cDNAs for human phosphatidylethanolamine N-methyltransferase and localization of the human gene on chromosome 17p11.2."
    Walkey C.J., Shields D.J., Vance D.E.
    Biochim. Biophys. Acta 1436:405-412(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT MET-175.
    Tissue: Liver.
  2. "Structure, expression profile and alternative processing of the human phosphatidylethanolamine N-methyltransferase (PEMT) gene."
    Shields D.J., Agellon L.B., Vance D.E.
    Biochim. Biophys. Acta 1532:105-114(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT MET-175.
  3. "Homo sapiens phosphatidylethanolamine N-methyltransferase mRNA."
    Maeda E., Watanabe M., Wang J., Kasuga M.
    Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS ILE-58 AND MET-175.
    Tissue: Liver.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Hypothalamus.
  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] (ISOFORM 3), VARIANT ILE-58.
    Tissue: Testis.
  6. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS ILE-58 AND MET-175.
  7. NIEHS SNPs program
    Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS TRP-3; ILE-58; MET-175 AND ARG-194 (ISOFORM 1), VARIANT ALA-11 (ISOFORM 2).
  8. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT MET-175.
  10. "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 2), VARIANTS ILE-58 AND MET-175.
    Tissue: Brain and Skin.
  11. "Phosphatidylethanolamine N-methyltransferase (PEMT) gene expression is induced by estrogen in human and mouse primary hepatocytes."
    Resseguie M., Song J., Niculescu M.D., da Costa K.A., Randall T.A., Zeisel S.H.
    FASEB J. 21:2622-2632(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING.
  12. "Functional analysis of two isoforms of phosphatidylethanolamine N-methyltransferase."
    Morita S.Y., Takeuchi A., Kitagawa S.
    Biochem. J. 432:387-398(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING, TOPOLOGY, GLYCOSYLATION (ISOFORM 2), SUBCELLULAR LOCATION (ISOFORMS 1 AND 2).

Entry informationi

Entry nameiPEMT_HUMAN
AccessioniPrimary (citable) accession number: Q9UBM1
Secondary accession number(s): A8MZ66
, B4DY41, D3DXC3, Q6IAQ5, Q86VL3, Q9BW86, Q9UHY6, Q9Y6V9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: June 12, 2007
Last modified: April 29, 2015
This is version 123 of the entry and version 4 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 17
    Human chromosome 17: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.