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Protein

Cytochrome P450 4A11

Gene

CYP4A11

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

Functioni

Catalyzes the omega- and (omega-1)-hydroxylation of various fatty acids such as laurate, myristate and palmitate. Has little activity toward prostaglandins A1 and E1. Oxidizes arachidonic acid to 20-hydroxyeicosatetraenoic acid (20-HETE).3 Publications

Catalytic activityi

Octane + 2 reduced rubredoxin + O2 + 2 H+ = 1-octanol + 2 oxidized rubredoxin + H2O.2 Publications

Cofactori

heme1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei321 – 3211Heme (covalent; via 1 link)1 Publication
Metal bindingi457 – 4571Iron (heme axial ligand)1 Publication

GO - Molecular functioni

  1. alkane 1-monooxygenase activity Source: BHF-UCL
  2. arachidonic acid epoxygenase activity Source: UniProtKB
  3. arachidonic acid omega-hydroxylase activity Source: UniProtKB-EC
  4. heme binding Source: InterPro
  5. iron ion binding Source: InterPro
  6. leukotriene-B4 20-monooxygenase activity Source: UniProtKB

GO - Biological processi

  1. arachidonic acid metabolic process Source: UniProtKB
  2. cellular lipid metabolic process Source: Reactome
  3. epoxygenase P450 pathway Source: UniProtKB
  4. fatty acid metabolic process Source: ProtInc
  5. leukotriene B4 catabolic process Source: GOC
  6. leukotriene metabolic process Source: UniProtKB
  7. long-chain fatty acid metabolic process Source: BHF-UCL
  8. omega-hydroxylase P450 pathway Source: Reactome
  9. oxidation-reduction process Source: UniProtKB
  10. positive regulation of icosanoid secretion Source: UniProtKB
  11. pressure natriuresis Source: UniProtKB
  12. renal water homeostasis Source: UniProtKB
  13. small molecule metabolic process Source: Reactome
  14. sodium ion homeostasis Source: UniProtKB
  15. xenobiotic metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_116145. PPARA activates gene expression.
REACT_13425. Miscellaneous substrates.
REACT_13645. Eicosanoids.
REACT_13814. Fatty acids.
REACT_150134. Synthesis of (16-20)-hydroxyeicosatetraenoic acids (HETE).
REACT_150420. Synthesis of Leukotrienes (LT) and Eoxins (EX).

Names & Taxonomyi

Protein namesi
Recommended name:
Cytochrome P450 4A11
Alternative name(s):
20-hydroxyeicosatetraenoic acid synthase
Short name:
20-HETE synthase
CYP4AII
CYPIVA11
Cytochrome P-450HK-omega
Cytochrome P450HL-omega
Fatty acid omega-hydroxylase
Lauric acid omega-hydroxylase (EC:1.14.15.3)
Gene namesi
Name:CYP4A11
Synonyms:CYP4A2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:2642. CYP4A11.

Subcellular locationi

GO - Cellular componenti

  1. apical plasma membrane Source: UniProtKB
  2. cytoplasm Source: UniProtKB
  3. endoplasmic reticulum membrane Source: Reactome
  4. extracellular vesicular exosome Source: UniProtKB
  5. intracellular membrane-bounded organelle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi130 – 1301G → S: Loss of activity. 1 Publication
Mutagenesisi321 – 3211E → A: Loss of covalent heme binding. 1 Publication

Organism-specific databases

PharmGKBiPA27118.

Chemistry

DrugBankiDB00515. Cisplatin.
DB00636. Clofibrate.
DB01234. Dexamethasone.
DB00655. Estrone.
DB00898. Ethanol.
DB00448. Lansoprazole.
DB00082. Pegvisomant.
DB00738. Pentamidine.
DB01174. Phenobarbital.
DB01045. Rifampicin.
DB00755. Tretinoin.

Polymorphism and mutation databases

BioMutaiCYP4A11.
DMDMi2493371.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Propeptidei2 – 432 PublicationsPRO_0000003579
Chaini5 – 519515Cytochrome P450 4A11PRO_0000003580Add
BLAST

Proteomic databases

PaxDbiQ02928.
PRIDEiQ02928.

PTM databases

PhosphoSiteiQ02928.

Expressioni

Tissue specificityi

Kidney and liver.1 Publication

Gene expression databases

BgeeiQ02928.
CleanExiHS_CYP4A11.
ExpressionAtlasiQ02928. baseline.
GenevestigatoriQ02928.

Interactioni

Protein-protein interaction databases

BioGridi107951. 3 interactions.
IntActiQ02928. 1 interaction.
STRINGi9606.ENSP00000311095.

Structurei

3D structure databases

ProteinModelPortaliQ02928.
SMRiQ02928. Positions 48-505.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi24 – 318Poly-Leu
Compositional biasi131 – 1344Poly-Leu

Sequence similaritiesi

Belongs to the cytochrome P450 family.Curated

Phylogenomic databases

eggNOGiCOG2124.
GeneTreeiENSGT00760000118816.
HOVERGENiHBG000182.
InParanoidiQ02928.
KOiK17687.
OrthoDBiEOG7CNZFK.
PhylomeDBiQ02928.
TreeFamiTF105088.

Family and domain databases

Gene3Di1.10.630.10. 1 hit.
InterProiIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
[Graphical view]
PfamiPF00067. p450. 1 hit.
[Graphical view]
PRINTSiPR00463. EP450I.
PR00385. P450.
SUPFAMiSSF48264. SSF48264. 1 hit.
PROSITEiPS00086. CYTOCHROME_P450. 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. AlignAdd to basket

Isoform 1 (identifier: Q02928-1) [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

        10         20         30         40         50
MSVSVLSPSR LLGDVSGILQ AASLLILLLL LIKAVQLYLH RQWLLKALQQ
60 70 80 90 100
FPCPPSHWLF GHIQELQQDQ ELQRIQKWVE TFPSACPHWL WGGKVRVQLY
110 120 130 140 150
DPDYMKVILG RSDPKSHGSY RFLAPWIGYG LLLLNGQTWF QHRRMLTPAF
160 170 180 190 200
HYDILKPYVG LMADSVRVML DKWEELLGQD SPLEVFQHVS LMTLDTIMKC
210 220 230 240 250
AFSHQGSIQV DRNSQSYIQA ISDLNNLVFS RVRNAFHQND TIYSLTSAGR
260 270 280 290 300
WTHRACQLAH QHTDQVIQLR KAQLQKEGEL EKIKRKRHLD FLDILLLAKM
310 320 330 340 350
ENGSILSDKD LRAEVDTFMF EGHDTTASGI SWILYALATH PKHQERCREE
360 370 380 390 400
IHSLLGDGAS ITWNHLDQMP YTTMCIKEAL RLYPPVPGIG RELSTPVTFP
410 420 430 440 450
DGRSLPKGIM VLLSIYGLHH NPKVWPNPEV FDPFRFAPGS AQHSHAFLPF
460 470 480 490 500
SGGSRNCIGK QFAMNELKVA TALTLLRFEL LPDPTRIPIP IARLVLKSKN
510
GIHLRLRRLP NPCEDKDQL
Length:519
Mass (Da):59,348
Last modified:November 1, 1997 - v1
Checksum:iA8D3073EEFF48AE9
GO
Isoform 2 (identifier: Q02928-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     356-519: Missing.

Show »
Length:355
Mass (Da):41,052
Checksum:iA108E4661ACF9824
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51V → A AA sequence (PubMed:1739747).Curated
Sequence conflicti383 – 3831Y → F in AAO16078 (PubMed:12464262).Curated
Sequence conflicti390 – 3901G → S in CAA50586 (PubMed:8363569).Curated
Sequence conflicti410 – 4123MVL → TVM in CAA50586 (PubMed:8363569).Curated

Polymorphismi

CYP4A11v seems to be a rare allelic variant of CYP4A11, it seems to be unstable and not to metabolize lauric acid.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti226 – 2261N → S.
Corresponds to variant rs12759923 [ dbSNP | Ensembl ].
VAR_048452
Natural varianti353 – 3531S → G.2 Publications
VAR_044377
Natural varianti434 – 4341F → S Associated with hypertension; significantly reduced arachidonic acid and lauric acid metabolizing activity. 5 Publications
Corresponds to variant rs1126742 [ dbSNP | Ensembl ].
VAR_019160
Natural varianti500 – 51920NGIHL…DKDQL → MESTCVSGGSLTLVKTRTSF EGLHLPSCLPDPRFCPLPVC PYPVFCLPTFPSSHLPAVPQ SACPSLSHLSPGLPTCLSTC LLPTCISCWEKS in CYP4A11V.
VAR_001257Add
BLAST

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei356 – 519164Missing in isoform 2. 1 PublicationVSP_034595Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L04751 mRNA. Translation: AAA58436.1.
D26481 mRNA. Translation: BAA05491.1.
S67580 mRNA. Translation: AAB29502.1.
S67581 mRNA. Translation: AAB29503.1.
AF525488 Genomic DNA. Translation: AAO16078.1.
AY369778 Genomic DNA. Translation: AAQ56847.1.
AL731892 Genomic DNA. Translation: CAH72778.1.
AL731892 Genomic DNA. Translation: CAH72779.1.
BC041158 mRNA. Translation: AAH41158.1.
X71480 mRNA. Translation: CAA50586.1.
CCDSiCCDS543.1. [Q02928-1]
PIRiA56859.
I53015.
I65981.
JX0331.
RefSeqiNP_000769.2. NM_000778.3. [Q02928-1]
UniGeneiHs.1645.
Hs.726474.

Genome annotation databases

EnsembliENST00000310638; ENSP00000311095; ENSG00000187048. [Q02928-1]
GeneIDi1579.
KEGGihsa:1579.
UCSCiuc001cqp.4. human. [Q02928-1]

Polymorphism and mutation databases

BioMutaiCYP4A11.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Cytochrome P450 Allele Nomenclature Committee

CYP4A11 alleles

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L04751 mRNA. Translation: AAA58436.1.
D26481 mRNA. Translation: BAA05491.1.
S67580 mRNA. Translation: AAB29502.1.
S67581 mRNA. Translation: AAB29503.1.
AF525488 Genomic DNA. Translation: AAO16078.1.
AY369778 Genomic DNA. Translation: AAQ56847.1.
AL731892 Genomic DNA. Translation: CAH72778.1.
AL731892 Genomic DNA. Translation: CAH72779.1.
BC041158 mRNA. Translation: AAH41158.1.
X71480 mRNA. Translation: CAA50586.1.
CCDSiCCDS543.1. [Q02928-1]
PIRiA56859.
I53015.
I65981.
JX0331.
RefSeqiNP_000769.2. NM_000778.3. [Q02928-1]
UniGeneiHs.1645.
Hs.726474.

3D structure databases

ProteinModelPortaliQ02928.
SMRiQ02928. Positions 48-505.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107951. 3 interactions.
IntActiQ02928. 1 interaction.
STRINGi9606.ENSP00000311095.

Chemistry

DrugBankiDB00515. Cisplatin.
DB00636. Clofibrate.
DB01234. Dexamethasone.
DB00655. Estrone.
DB00898. Ethanol.
DB00448. Lansoprazole.
DB00082. Pegvisomant.
DB00738. Pentamidine.
DB01174. Phenobarbital.
DB01045. Rifampicin.
DB00755. Tretinoin.

PTM databases

PhosphoSiteiQ02928.

Polymorphism and mutation databases

BioMutaiCYP4A11.
DMDMi2493371.

Proteomic databases

PaxDbiQ02928.
PRIDEiQ02928.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000310638; ENSP00000311095; ENSG00000187048. [Q02928-1]
GeneIDi1579.
KEGGihsa:1579.
UCSCiuc001cqp.4. human. [Q02928-1]

Organism-specific databases

CTDi1579.
GeneCardsiGC01M047394.
HGNCiHGNC:2642. CYP4A11.
MIMi601310. gene.
neXtProtiNX_Q02928.
PharmGKBiPA27118.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2124.
GeneTreeiENSGT00760000118816.
HOVERGENiHBG000182.
InParanoidiQ02928.
KOiK17687.
OrthoDBiEOG7CNZFK.
PhylomeDBiQ02928.
TreeFamiTF105088.

Enzyme and pathway databases

ReactomeiREACT_116145. PPARA activates gene expression.
REACT_13425. Miscellaneous substrates.
REACT_13645. Eicosanoids.
REACT_13814. Fatty acids.
REACT_150134. Synthesis of (16-20)-hydroxyeicosatetraenoic acids (HETE).
REACT_150420. Synthesis of Leukotrienes (LT) and Eoxins (EX).

Miscellaneous databases

ChiTaRSiCYP4A11. human.
GeneWikiiCYP4A11.
GenomeRNAii1579.
NextBioi6485.
PROiQ02928.
SOURCEiSearch...

Gene expression databases

BgeeiQ02928.
CleanExiHS_CYP4A11.
ExpressionAtlasiQ02928. baseline.
GenevestigatoriQ02928.

Family and domain databases

Gene3Di1.10.630.10. 1 hit.
InterProiIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
[Graphical view]
PfamiPF00067. p450. 1 hit.
[Graphical view]
PRINTSiPR00463. EP450I.
PR00385. P450.
SUPFAMiSSF48264. SSF48264. 1 hit.
PROSITEiPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of a cDNA encoding a human kidney, cytochrome P-450 4A fatty acid omega-hydroxylase and the cognate enzyme expressed in Escherichia coli."
    Palmer C.N.A., Richardson T.H., Griffin K.J., Hsu M.-H., Muerhoff A.S., Clark J.E., Johnson E.F.
    Biochim. Biophys. Acta 1172:161-166(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
    Tissue: Kidney.
  2. "Purification and cDNA cloning of human liver CYP4A fatty acid omega-hydroxylase."
    Kawashima H., Kusunose E., Kikuta Y., Kinoshita H., Tanaka S., Yamamoto S., Kishimoto T., Kusunose M.
    J. Biochem. 116:74-80(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 5-24, CHARACTERIZATION.
    Tissue: Liver.
  3. "Complete cDNA sequence and cDNA-directed expression of CYP4A11, a fatty acid omega-hydroxylase expressed in human kidney."
    Imaoka S., Ogawa H., Kimura S., Gonzalez F.J.
    DNA Cell Biol. 12:893-899(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT SER-434, CHARACTERIZATION.
    Tissue: Kidney.
  4. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  5. SeattleSNPs variation discovery resource
    Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), VARIANT SER-434.
  6. "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].
  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 2).
    Tissue: Colon.
  8. "Purification and NH2-terminal amino acid sequences of human and rat kidney fatty acid omega-hydroxylases."
    Kawashima H., Kusunose E., Kubota I., Maekawa M., Kusunose M.
    Biochim. Biophys. Acta 1123:156-162(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 5-39, FUNCTION, CATALYTIC ACTIVITY.
    Tissue: Kidney.
  9. "Species-specific induction of cytochrome P-450 4A RNAs: PCR cloning of partial guinea-pig, human and mouse CYP4A cDNAs."
    Bell D.R., Plant N.J., Rider C.G., Na L., Brown S., Ateitalla I., Acharya S.K., Davies M.H., Elias E.E., Jenkins N.A., Gilbert D.J., Copeland N.G., Elcombe C.R.
    Biochem. J. 294:173-180(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 317-457, VARIANTS GLY-353 AND SER-434.
    Tissue: Liver.
  10. "Covalently linked heme in cytochrome P4504A fatty acid hydroxylases."
    Hoch U., Ortiz de Montellano P.R.
    J. Biol. Chem. 276:11339-11346(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: COVALENT HEME ATTACHMENT.
  11. "Autocatalytic mechanism and consequences of covalent heme attachment in the cytochrome P4504A family."
    LeBrun L.A., Hoch U., Ortiz de Montellano P.R.
    J. Biol. Chem. 277:12755-12761(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: COVALENT HEME ATTACHMENT, MUTAGENESIS OF GLU-321.
  12. "Functional variant of CYP4A11 20-hydroxyeicosatetraenoic acid synthase is associated with essential hypertension."
    Gainer J.V., Bellamine A., Dawson E.P., Womble K.E., Grant S.W., Wang Y., Cupples L.A., Guo C.-Y., Demissie S., O'Donnell C.J., Brown N.J., Waterman M.R., Capdevila J.H.
    Circulation 111:63-69(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF GLY-130, VARIANT SER-434.
  13. Cited for: VARIANTS GLY-353 AND SER-434.

Entry informationi

Entry nameiCP4AB_HUMAN
AccessioniPrimary (citable) accession number: Q02928
Secondary accession number(s): Q06766
, Q16865, Q16866, Q5VSP8, Q86SU6, Q8IWY5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: April 29, 2015
This is version 143 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 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. 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

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.