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Protein

GPI ethanolamine phosphate transferase 3

Gene

PIGO

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

Functioni

Ethanolamine phosphate transferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers ethanolamine phosphate to the GPI third mannose which links the GPI-anchor to the C-terminus of the proteins by an amide bond (By similarity).By similarity

Pathwayi

GO - Molecular functioni

  1. transferase activity Source: UniProtKB-KW

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. C-terminal protein lipidation Source: Reactome
  3. GPI anchor biosynthetic process Source: UniProtKB
  4. post-translational protein modification Source: Reactome
  5. preassembly of GPI anchor in ER membrane Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

GPI-anchor biosynthesis

Enzyme and pathway databases

ReactomeiREACT_952. Synthesis of glycosylphosphatidylinositol (GPI).
UniPathwayiUPA00196.

Names & Taxonomyi

Protein namesi
Recommended name:
GPI ethanolamine phosphate transferase 3 (EC:2.-.-.-)
Alternative name(s):
Phosphatidylinositol-glycan biosynthesis class O protein
Short name:
PIG-O
Gene namesi
Name:PIGO
ORF Names:UNQ632/PRO1249
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:23215. PIGO.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei4 – 2421HelicalSequence AnalysisAdd
BLAST
Transmembranei457 – 47721HelicalSequence AnalysisAdd
BLAST
Transmembranei482 – 50221HelicalSequence AnalysisAdd
BLAST
Transmembranei510 – 53021HelicalSequence AnalysisAdd
BLAST
Transmembranei541 – 56121HelicalSequence AnalysisAdd
BLAST
Transmembranei575 – 59521HelicalSequence AnalysisAdd
BLAST
Transmembranei668 – 68821HelicalSequence AnalysisAdd
BLAST
Transmembranei701 – 72121HelicalSequence AnalysisAdd
BLAST
Transmembranei747 – 76721HelicalSequence AnalysisAdd
BLAST
Transmembranei830 – 85021HelicalSequence AnalysisAdd
BLAST
Transmembranei857 – 87721HelicalSequence AnalysisAdd
BLAST
Transmembranei944 – 96421HelicalSequence AnalysisAdd
BLAST
Transmembranei1014 – 103421HelicalSequence AnalysisAdd
BLAST
Transmembranei1048 – 106821HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: UniProtKB
  2. integral component of membrane Source: UniProtKB-KW
  3. membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Involvement in diseasei

Hyperphosphatasia with mental retardation syndrome 2 (HPMRS2)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn autosomal recessive form of intellectual disability characterized by facial dysmorphism, brachytelephalangy, and persistent elevated serum alkaline phosphatase (hyperphosphatasia). Some patients may have additional features, such as cardiac septal defects or seizures.

See also OMIM:614749
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti957 – 9571L → F in HPMRS2. 1 Publication
VAR_068809

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

MIMi614749. phenotype.
Orphaneti247262. Hyperphosphatasia-intellectual disability syndrome.
PharmGKBiPA134993507.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10891089GPI ethanolamine phosphate transferase 3PRO_0000058438Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi268 – 2681N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ8TEQ8.
PaxDbiQ8TEQ8.
PRIDEiQ8TEQ8.

PTM databases

PhosphoSiteiQ8TEQ8.

Expressioni

Gene expression databases

BgeeiQ8TEQ8.
CleanExiHS_PIGO.
GenevestigatoriQ8TEQ8.

Organism-specific databases

HPAiHPA014905.

Interactioni

Subunit structurei

Forms a complex with PIGF. PIGF is required to stabilize PIGO (By similarity).By similarity

Protein-protein interaction databases

BioGridi124223. 11 interactions.
STRINGi9606.ENSP00000339382.

Structurei

3D structure databases

ProteinModelPortaliQ8TEQ8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PIGG/PIGN/PIGO family. PIGO subfamily.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1524.
GeneTreeiENSGT00780000122029.
HOVERGENiHBG031821.
InParanoidiQ8TEQ8.
KOiK05288.
OMAiPVLFVRW.
OrthoDBiEOG7XH6P8.
PhylomeDBiQ8TEQ8.
TreeFamiTF354249.

Family and domain databases

Gene3Di3.40.720.10. 1 hit.
InterProiIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR002591. Phosphodiest/P_Trfase.
[Graphical view]
PfamiPF01663. Phosphodiest. 1 hit.
[Graphical view]
SUPFAMiSSF53649. SSF53649. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: Q8TEQ8-1) [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
MQKASVLLFL AWVCFLFYAG IALFTSGFLL TRLELTNHSS CQEPPGPGSL
60 70 80 90 100
PWGSQGKPGA CWMASRFSRV VLVLIDALRF DFAQPQHSHV PREPPVSLPF
110 120 130 140 150
LGKLSSLQRI LEIQPHHARL YRSQVDPPTT TMQRLKALTT GSLPTFIDAG
160 170 180 190 200
SNFASHAIVE DNLIKQLTSA GRRVVFMGDD TWKDLFPGAF SKAFFFPSFN
210 220 230 240 250
VRDLDTVDNG ILEHLYPTMD SGEWDVLIAH FLGVDHCGHK HGPHHPEMAK
260 270 280 290 300
KLSQMDQVIQ GLVERLENDT LLVVAGDHGM TTNGDHGGDS ELEVSAALFL
310 320 330 340 350
YSPTAVFPST PPEEPEVIPQ VSLVPTLALL LGLPIPFGNI GEVMAELFSG
360 370 380 390 400
GEDSQPHSSA LAQASALHLN AQQVSRFLHT YSAATQDLQA KELHQLQNLF
410 420 430 440 450
SKASADYQWL LQSPKGAEAT LPTVIAELQQ FLRGARAMCI ESWARFSLVR
460 470 480 490 500
MAGGTALLAA SCFICLLASQ WAISPGFPFC PLLLTPVAWG LVGAIAYAGL
510 520 530 540 550
LGTIELKLDL VLLGAVAAVS SFLPFLWKAW AGWGSKRPLA TLFPIPGPVL
560 570 580 590 600
LLLLFRLAVF FSDSFVVAEA RATPFLLGSF ILLLVVQLHW EGQLLPPKLL
610 620 630 640 650
TMPRLGTSAT TNPPRHNGAY ALRLGIGLLL CTRLAGLFHR CPEETPVCHS
660 670 680 690 700
SPWLSPLASM VGGRAKNLWY GACVAALVAL LAAVRLWLRR YGNLKSPEPP
710 720 730 740 750
MLFVRWGLPL MALGTAAYWA LASGADEAPP RLRVLVSGAS MVLPRAVAGL
760 770 780 790 800
AASGLALLLW KPVTVLVKAG AGAPRTRTVL TPFSGPPTSQ ADLDYVVPQI
810 820 830 840 850
YRHMQEEFRG RLERTKSQGP LTVAAYQLGS VYSAAMVTAL TLLAFPLLLL
860 870 880 890 900
HAERISLVFL LLFLQSFLLL HLLAAGIPVT TPGPFTVPWQ AVSAWALMAT
910 920 930 940 950
QTFYSTGHQP VFPAIHWHAA FVGFPEGHGS CTWLPALLVG ANTFASHLLF
960 970 980 990 1000
AVGCPLLLLW PFLCESQGLR KRQQPPGNEA DARVRPEEEE EPLMEMRLRD
1010 1020 1030 1040 1050
APQHFYAALL QLGLKYLFIL GIQILACALA ASILRRHLMV WKVFAPKFIF
1060 1070 1080
EAVGFIVSSV GLLLGIALVM RVDGAVSSWF RQLFLAQQR
Length:1,089
Mass (Da):118,699
Last modified:March 14, 2005 - v3
Checksum:i0F47404F6FAD50B6
GO
Isoform 2 (identifier: Q8TEQ8-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     449-865: Missing.

Note: No experimental confirmation available.

Show »
Length:672
Mass (Da):73,992
Checksum:iEF2958613DFFC47A
GO

Sequence cautioni

The sequence AAC07985.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence AAH01030.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAH13987.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAB84890.1 differs from that shown. Reason: Frameshift at several positions. Curated
The sequence BAC03414.1 differs from that shown. Reason: Frameshift at several positions. Curated
The sequence CAD38806.1 differs from that shown. Reason: Frameshift at position 46. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti179 – 1813DDT → ARG in AAH13987 (PubMed:15489334).Curated
Sequence conflicti225 – 2317DVLIAHF → EVSNQHV in AAH01030 (PubMed:15489334).Curated
Sequence conflicti350 – 3501G → W in AAH29271 (PubMed:15489334).Curated
Sequence conflicti353 – 3531D → Y in AAH29271 (PubMed:15489334).Curated
Sequence conflicti415 – 4162KG → R in CAD38806 (PubMed:17974005).Curated
Sequence conflicti884 – 96986PFTVP…ESQGL → KYLSSDSLKDNSDVSSAPLV FKEVLLLMFLSLTEGPMPHT TRKVFLVSSLLPAIAKQIDP SCWFPGFMERRDKESSKTPC GNAASS in BAB89338 (PubMed:12044878).CuratedAdd
BLAST

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti130 – 1301T → N Found in a patient with epileptic encephalopathy; unknown pathological significance. 1 Publication
VAR_071074
Natural varianti686 – 6861L → M in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036332
Natural varianti957 – 9571L → F in HPMRS2. 1 Publication
VAR_068809

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei449 – 865417Missing in isoform 2. 1 PublicationVSP_003944Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL833956 mRNA. Translation: CAD38806.1. Frameshift.
AK074064 mRNA. Translation: BAB84890.1. Frameshift.
AK090433 mRNA. Translation: BAC03414.1. Frameshift.
AY358472 mRNA. Translation: AAQ88836.1.
AC004472 Genomic DNA. Translation: AAC07985.1. Sequence problems.
AL353795 Genomic DNA. Translation: CAH70995.2.
AL353795 Genomic DNA. Translation: CAH70996.1.
CH471071 Genomic DNA. Translation: EAW58397.1.
BC001030 mRNA. Translation: AAH01030.1. Different initiation.
BC013987 mRNA. Translation: AAH13987.1. Different initiation.
BC029271 mRNA. Translation: AAH29271.1.
BC036916 mRNA. Translation: AAH36916.1.
BC065282 mRNA. Translation: AAH65282.1.
AB083625 Genomic DNA. Translation: BAB89338.1.
CCDSiCCDS6575.1. [Q8TEQ8-1]
CCDS6576.1. [Q8TEQ8-2]
PIRiT02245.
RefSeqiNP_001188413.1. NM_001201484.1. [Q8TEQ8-2]
NP_116023.2. NM_032634.3. [Q8TEQ8-1]
NP_690577.2. NM_152850.3. [Q8TEQ8-2]
XP_005251676.1. XM_005251619.1. [Q8TEQ8-1]
UniGeneiHs.522099.
Hs.735712.

Genome annotation databases

EnsembliENST00000298004; ENSP00000298004; ENSG00000165282. [Q8TEQ8-2]
ENST00000361778; ENSP00000354678; ENSG00000165282. [Q8TEQ8-2]
ENST00000378617; ENSP00000367880; ENSG00000165282. [Q8TEQ8-1]
GeneIDi84720.
KEGGihsa:84720.
UCSCiuc003zwd.3. human. [Q8TEQ8-1]
uc003zwe.3. human. [Q8TEQ8-2]

Polymorphism databases

DMDMi61252289.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL833956 mRNA. Translation: CAD38806.1. Frameshift.
AK074064 mRNA. Translation: BAB84890.1. Frameshift.
AK090433 mRNA. Translation: BAC03414.1. Frameshift.
AY358472 mRNA. Translation: AAQ88836.1.
AC004472 Genomic DNA. Translation: AAC07985.1. Sequence problems.
AL353795 Genomic DNA. Translation: CAH70995.2.
AL353795 Genomic DNA. Translation: CAH70996.1.
CH471071 Genomic DNA. Translation: EAW58397.1.
BC001030 mRNA. Translation: AAH01030.1. Different initiation.
BC013987 mRNA. Translation: AAH13987.1. Different initiation.
BC029271 mRNA. Translation: AAH29271.1.
BC036916 mRNA. Translation: AAH36916.1.
BC065282 mRNA. Translation: AAH65282.1.
AB083625 Genomic DNA. Translation: BAB89338.1.
CCDSiCCDS6575.1. [Q8TEQ8-1]
CCDS6576.1. [Q8TEQ8-2]
PIRiT02245.
RefSeqiNP_001188413.1. NM_001201484.1. [Q8TEQ8-2]
NP_116023.2. NM_032634.3. [Q8TEQ8-1]
NP_690577.2. NM_152850.3. [Q8TEQ8-2]
XP_005251676.1. XM_005251619.1. [Q8TEQ8-1]
UniGeneiHs.522099.
Hs.735712.

3D structure databases

ProteinModelPortaliQ8TEQ8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124223. 11 interactions.
STRINGi9606.ENSP00000339382.

PTM databases

PhosphoSiteiQ8TEQ8.

Polymorphism databases

DMDMi61252289.

Proteomic databases

MaxQBiQ8TEQ8.
PaxDbiQ8TEQ8.
PRIDEiQ8TEQ8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000298004; ENSP00000298004; ENSG00000165282. [Q8TEQ8-2]
ENST00000361778; ENSP00000354678; ENSG00000165282. [Q8TEQ8-2]
ENST00000378617; ENSP00000367880; ENSG00000165282. [Q8TEQ8-1]
GeneIDi84720.
KEGGihsa:84720.
UCSCiuc003zwd.3. human. [Q8TEQ8-1]
uc003zwe.3. human. [Q8TEQ8-2]

Organism-specific databases

CTDi84720.
GeneCardsiGC09M035088.
HGNCiHGNC:23215. PIGO.
HPAiHPA014905.
MIMi614730. gene.
614749. phenotype.
neXtProtiNX_Q8TEQ8.
Orphaneti247262. Hyperphosphatasia-intellectual disability syndrome.
PharmGKBiPA134993507.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1524.
GeneTreeiENSGT00780000122029.
HOVERGENiHBG031821.
InParanoidiQ8TEQ8.
KOiK05288.
OMAiPVLFVRW.
OrthoDBiEOG7XH6P8.
PhylomeDBiQ8TEQ8.
TreeFamiTF354249.

Enzyme and pathway databases

UniPathwayiUPA00196.
ReactomeiREACT_952. Synthesis of glycosylphosphatidylinositol (GPI).

Miscellaneous databases

GenomeRNAii84720.
NextBioi74822.
PROiQ8TEQ8.
SOURCEiSearch...

Gene expression databases

BgeeiQ8TEQ8.
CleanExiHS_PIGO.
GenevestigatoriQ8TEQ8.

Family and domain databases

Gene3Di3.40.720.10. 1 hit.
InterProiIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR002591. Phosphodiest/P_Trfase.
[Graphical view]
PfamiPF01663. Phosphodiest. 1 hit.
[Graphical view]
SUPFAMiSSF53649. SSF53649. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Testis.
  2. "The nucleotide sequence of a long cDNA clone isolated from human spleen."
    Jikuya H., Takano J., Nomura N., Kikuno R., Nagase T., Ohara O.
    Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Spleen.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2003) [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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Duodenum, Eye and Lung.
  8. "Identification of G protein-coupled receptor genes from the human genome sequence."
    Takeda S., Kadowaki S., Haga T., Takaesu H., Mitaku S.
    FEBS Lett. 520:97-101(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 601-968.
  9. Cited for: VARIANT [LARGE SCALE ANALYSIS] MET-686.
  10. "Mutations in PIGO, a member of the GPI-anchor-synthesis pathway, cause hyperphosphatasia with mental retardation."
    Krawitz P.M., Murakami Y., Hecht J., Kruger U., Holder S.E., Mortier G.R., Delle Chiaie B., De Baere E., Thompson M.D., Roscioli T., Kielbasa S., Kinoshita T., Mundlos S., Robinson P.N., Horn D.
    Am. J. Hum. Genet. 91:146-151(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT HPMRS2 PHE-957.
  11. "PIGO mutations in intractable epilepsy and severe developmental delay with mild elevation of alkaline phosphatase levels."
    Nakamura K., Osaka H., Murakami Y., Anzai R., Nishiyama K., Kodera H., Nakashima M., Tsurusaki Y., Miyake N., Kinoshita T., Matsumoto N., Saitsu H.
    Epilepsia 55:E13-E17(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ASN-130.

Entry informationi

Entry nameiPIGO_HUMAN
AccessioniPrimary (citable) accession number: Q8TEQ8
Secondary accession number(s): B1AML3
, Q6P154, Q6UX80, Q8TDS8, Q96CS9, Q9BVN9, Q9Y4B0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 12, 2002
Last sequence update: March 14, 2005
Last modified: February 3, 2015
This is version 120 of the entry and version 3 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 9
    Human chromosome 9: 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.