Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Prostaglandin reductase 1

Gene

PTGR1

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

Functioni

Functions as 15-oxo-prostaglandin 13-reductase and acts on 15-oxo-PGE1, 15-oxo-PGE2 and 15-oxo-PGE2-alpha. Has no activity towards PGE1, PGE2 and PGE2-alpha (By similarity). Catalyzes the conversion of leukotriene B4 into its biologically less active metabolite, 12-oxo-leukotriene B4. This is an initial and key step of metabolic inactivation of leukotriene B4.By similarity

Catalytic activityi

A n-alkanal + NAD(P)+ = an alk-2-enal + NAD(P)H.
11-alpha-hydroxy-9,15-dioxoprost-5-enoate + NAD(P)+ = (5Z)-(13E)-11-alpha-hydroxy-9,15-dioxoprosta-5,13-dienoate + NAD(P)H.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei178 – 1781NADP1 Publication
Binding sitei193 – 1931NADP1 Publication
Binding sitei217 – 2171NADP1 Publication
Binding sitei321 – 3211NADP1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi152 – 1554NADP1 Publication
Nucleotide bindingi239 – 2457NADP1 Publication
Nucleotide bindingi270 – 2723NADP1 Publication

GO - Molecular functioni

GO - Biological processi

  • leukotriene metabolic process Source: UniProtKB
  • response to toxic substance Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP

Enzyme and pathway databases

ReactomeiR-HSA-2142691. Synthesis of Leukotrienes (LT) and Eoxins (EX).
R-HSA-2142700. Synthesis of Lipoxins (LX).
R-HSA-2162123. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).

Names & Taxonomyi

Protein namesi
Recommended name:
Prostaglandin reductase 1 (EC:1.3.1.-)
Short name:
PRG-1
Alternative name(s):
15-oxoprostaglandin 13-reductase (EC:1.3.1.48)
NADP-dependent leukotriene B4 12-hydroxydehydrogenase (EC:1.3.1.74)
Gene namesi
Name:PTGR1
Synonyms:LTB4DH
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:18429. PTGR1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • extracellular exosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162400322.

Polymorphism and mutation databases

BioMutaiPTGR1.
DMDMi23503081.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 329329Prostaglandin reductase 1PRO_0000218065Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei18 – 181PhosphothreonineCombined sources
Modified residuei20 – 201PhosphoserineCombined sources
Modified residuei178 – 1781N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ14914.
MaxQBiQ14914.
PaxDbiQ14914.
PRIDEiQ14914.
TopDownProteomicsiQ14914-1. [Q14914-1]

PTM databases

iPTMnetiQ14914.
PhosphoSiteiQ14914.

Expressioni

Tissue specificityi

High expression in the kidney, liver, and intestine but not in leukocytes.1 Publication

Gene expression databases

BgeeiQ14914.
CleanExiHS_PTGR1.
ExpressionAtlasiQ14914. baseline and differential.
GenevisibleiQ14914. HS.

Organism-specific databases

HPAiHPA036724.
HPA036725.

Interactioni

Subunit structurei

Monomer or homodimer.By similarity

Protein-protein interaction databases

BioGridi116604. 14 interactions.
IntActiQ14914. 2 interactions.
MINTiMINT-5004604.
STRINGi9606.ENSP00000311572.

Structurei

Secondary structure

1
329
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 118Combined sources
Beta strandi14 – 163Combined sources
Helixi19 – 213Combined sources
Beta strandi22 – 287Combined sources
Beta strandi37 – 459Combined sources
Helixi49 – 535Combined sources
Helixi54 – 563Combined sources
Beta strandi67 – 759Combined sources
Beta strandi84 – 874Combined sources
Beta strandi91 – 977Combined sources
Helixi115 – 1195Combined sources
Turni120 – 1223Combined sources
Helixi124 – 13411Combined sources
Beta strandi144 – 1496Combined sources
Helixi153 – 16412Combined sources
Beta strandi168 – 1758Combined sources
Helixi176 – 18510Combined sources
Beta strandi188 – 1925Combined sources
Turni193 – 1953Combined sources
Helixi199 – 2068Combined sources
Beta strandi211 – 2188Combined sources
Helixi220 – 2278Combined sources
Beta strandi230 – 2389Combined sources
Helixi242 – 2454Combined sources
Helixi257 – 2626Combined sources
Beta strandi266 – 2694Combined sources
Helixi272 – 2743Combined sources
Helixi277 – 29216Combined sources
Beta strandi300 – 3045Combined sources
Helixi306 – 3083Combined sources
Helixi309 – 3179Combined sources
Beta strandi322 – 3287Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZSVX-ray2.30A/B/C/D4-329[»]
2Y05X-ray2.20A/B/C/D4-329[»]
ProteinModelPortaliQ14914.
SMRiQ14914. Positions 4-329.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ14914.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi250 – 2578Pro-rich

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1196. Eukaryota.
COG2130. LUCA.
GeneTreeiENSGT00390000009335.
HOGENOMiHOG000294663.
HOVERGENiHBG055024.
InParanoidiQ14914.
KOiK13948.
OMAiMGMPGFT.
PhylomeDBiQ14914.
TreeFamiTF324201.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProiIPR013149. ADH_C.
IPR002085. ADH_SF_Zn-type.
IPR014190. B4_12hDH.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
IPR020843. PKS_ER.
[Graphical view]
PANTHERiPTHR11695. PTHR11695. 1 hit.
PfamiPF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SMARTiSM00829. PKS_ER. 1 hit.
[Graphical view]
SUPFAMiSSF50129. SSF50129. 2 hits.
SSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR02825. B4_12hDH. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q14914-1) [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
MVRTKTWTLK KHFVGYPTNS DFELKTAELP PLKNGEVLLE ALFLTVDPYM
60 70 80 90 100
RVAAKRLKEG DTMMGQQVAK VVESKNVALP KGTIVLASPG WTTHSISDGK
110 120 130 140 150
DLEKLLTEWP DTIPLSLALG TVGMPGLTAY FGLLEICGVK GGETVMVNAA
160 170 180 190 200
AGAVGSVVGQ IAKLKGCKVV GAVGSDEKVA YLQKLGFDVV FNYKTVESLE
210 220 230 240 250
ETLKKASPDG YDCYFDNVGG EFSNTVIGQM KKFGRIAICG AISTYNRTGP
260 270 280 290 300
LPPGPPPEIV IYQELRMEAF VVYRWQGDAR QKALKDLLKW VLEGKIQYKE
310 320
YIIEGFENMP AAFMGMLKGD NLGKTIVKA
Length:329
Mass (Da):35,870
Last modified:September 19, 2002 - v2
Checksum:iE121ADB7C5BD9CF8
GO
Isoform 2 (identifier: Q14914-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     294-329: GKIQYKEYIIEGFENMPAAFMGMLKGDNLGKTIVKA → IKRENEED

Note: No experimental confirmation available.
Show »
Length:301
Mass (Da):32,895
Checksum:iBD24D01FD752BE62
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti311 – 3111A → R in BAA08382 (PubMed:8576264).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti27 – 271A → S.3 Publications
Corresponds to variant rs1053959 [ dbSNP | Ensembl ].
VAR_023111

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei294 – 32936GKIQY…TIVKA → IKRENEED in isoform 2. 1 PublicationVSP_044652Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK289597 mRNA. Translation: BAF82286.1.
AK298379 mRNA. Translation: BAG60615.1.
AL135787 Genomic DNA. Translation: CAC22151.1.
AL159168 Genomic DNA. No translation available.
CH471105 Genomic DNA. Translation: EAW59074.1.
BC035228 mRNA. Translation: AAH35228.1.
D49387 mRNA. Translation: BAA08382.1.
CCDSiCCDS55331.1. [Q14914-2]
CCDS6779.1. [Q14914-1]
RefSeqiNP_001139580.1. NM_001146108.1. [Q14914-1]
NP_001139581.1. NM_001146109.1. [Q14914-2]
NP_036344.2. NM_012212.3. [Q14914-1]
UniGeneiHs.584864.

Genome annotation databases

EnsembliENST00000309195; ENSP00000311572; ENSG00000106853. [Q14914-1]
ENST00000407693; ENSP00000385763; ENSG00000106853. [Q14914-1]
ENST00000538962; ENSP00000440281; ENSG00000106853. [Q14914-2]
GeneIDi22949.
KEGGihsa:22949.
UCSCiuc004bfh.3. human. [Q14914-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK289597 mRNA. Translation: BAF82286.1.
AK298379 mRNA. Translation: BAG60615.1.
AL135787 Genomic DNA. Translation: CAC22151.1.
AL159168 Genomic DNA. No translation available.
CH471105 Genomic DNA. Translation: EAW59074.1.
BC035228 mRNA. Translation: AAH35228.1.
D49387 mRNA. Translation: BAA08382.1.
CCDSiCCDS55331.1. [Q14914-2]
CCDS6779.1. [Q14914-1]
RefSeqiNP_001139580.1. NM_001146108.1. [Q14914-1]
NP_001139581.1. NM_001146109.1. [Q14914-2]
NP_036344.2. NM_012212.3. [Q14914-1]
UniGeneiHs.584864.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZSVX-ray2.30A/B/C/D4-329[»]
2Y05X-ray2.20A/B/C/D4-329[»]
ProteinModelPortaliQ14914.
SMRiQ14914. Positions 4-329.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116604. 14 interactions.
IntActiQ14914. 2 interactions.
MINTiMINT-5004604.
STRINGi9606.ENSP00000311572.

PTM databases

iPTMnetiQ14914.
PhosphoSiteiQ14914.

Polymorphism and mutation databases

BioMutaiPTGR1.
DMDMi23503081.

Proteomic databases

EPDiQ14914.
MaxQBiQ14914.
PaxDbiQ14914.
PRIDEiQ14914.
TopDownProteomicsiQ14914-1. [Q14914-1]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000309195; ENSP00000311572; ENSG00000106853. [Q14914-1]
ENST00000407693; ENSP00000385763; ENSG00000106853. [Q14914-1]
ENST00000538962; ENSP00000440281; ENSG00000106853. [Q14914-2]
GeneIDi22949.
KEGGihsa:22949.
UCSCiuc004bfh.3. human. [Q14914-1]

Organism-specific databases

CTDi22949.
GeneCardsiPTGR1.
H-InvDBHIX0008283.
HGNCiHGNC:18429. PTGR1.
HPAiHPA036724.
HPA036725.
MIMi601274. gene.
neXtProtiNX_Q14914.
PharmGKBiPA162400322.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1196. Eukaryota.
COG2130. LUCA.
GeneTreeiENSGT00390000009335.
HOGENOMiHOG000294663.
HOVERGENiHBG055024.
InParanoidiQ14914.
KOiK13948.
OMAiMGMPGFT.
PhylomeDBiQ14914.
TreeFamiTF324201.

Enzyme and pathway databases

ReactomeiR-HSA-2142691. Synthesis of Leukotrienes (LT) and Eoxins (EX).
R-HSA-2142700. Synthesis of Lipoxins (LX).
R-HSA-2162123. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).

Miscellaneous databases

ChiTaRSiPTGR1. human.
EvolutionaryTraceiQ14914.
GenomeRNAii22949.
PROiQ14914.
SOURCEiSearch...

Gene expression databases

BgeeiQ14914.
CleanExiHS_PTGR1.
ExpressionAtlasiQ14914. baseline and differential.
GenevisibleiQ14914. HS.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProiIPR013149. ADH_C.
IPR002085. ADH_SF_Zn-type.
IPR014190. B4_12hDH.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
IPR020843. PKS_ER.
[Graphical view]
PANTHERiPTHR11695. PTHR11695. 1 hit.
PfamiPF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SMARTiSM00829. PKS_ER. 1 hit.
[Graphical view]
SUPFAMiSSF50129. SSF50129. 2 hits.
SSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR02825. B4_12hDH. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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 1 AND 2), VARIANT SER-27.
    Tissue: Brain cortex and Kidney.
  2. "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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT SER-27.
  4. "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), VARIANT SER-27.
    Tissue: Cervix.
  5. "cDNA cloning, expression, and mutagenesis study of leukotriene B4 12-hydroxydehydrogenase."
    Yokomizo T., Ogawa Y., Uozumi N., Kume K., Izumi T., Shimizu T.
    J. Biol. Chem. 271:2844-2850(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-311 (ISOFORM 1), TISSUE SPECIFICITY.
    Tissue: Kidney.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-18 AND SER-20, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. "Crystal structure of human NADP-dependent leukotriene B4 12-hydroxydehydrogenase."
    Structural genomics consortium (SGC)
    Submitted (MAY-2005) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 4-239.
  9. "Crystal structure of human leukotriene B4 12-hydroxydehydrogenase in complex with NADP and raloxifene."
    Structural genomics consortium (SGC)
    Submitted (JAN-2011) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 4-329 IN COMPLEX WITH NADP AND RALOXIFENE.

Entry informationi

Entry nameiPTGR1_HUMAN
AccessioniPrimary (citable) accession number: Q14914
Secondary accession number(s): A8K0N2
, B4DPK3, F5GY50, Q8IYQ0, Q9H1X6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: September 19, 2002
Last modified: June 8, 2016
This is version 158 of the entry and version 2 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

3D-structure, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

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 one 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.