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Protein

Nuclear receptor subfamily 1 group I member 2

Gene

NR1I2

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

Functioni

Nuclear receptor that binds and is activated by variety of endogenous and xenobiotic compounds. Transcription factor that activates the transcription of multiple genes involved in the metabolism and secretion of potentially harmful xenobiotics, drugs and endogenous compounds. Activated by the antibiotic rifampicin and various plant metabolites, such as hyperforin, guggulipid, colupulone, and isoflavones. Response to specific ligands is species-specific. Activated by naturally occurring steroids, such as pregnenolone and progesterone. Binds to a response element in the promoters of the CYP3A4 and ABCB1/MDR1 genes.6 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei247Agonist1
Binding sitei285Agonist1
Binding sitei288Agonist1
Binding sitei299Agonist1
Binding sitei407Agonist1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi38 – 107Nuclear receptorPROSITE-ProRule annotationAdd BLAST70
Zinc fingeri41 – 61NR C4-typePROSITE-ProRule annotationAdd BLAST21
Zinc fingeri77 – 102NR C4-typePROSITE-ProRule annotationAdd BLAST26

GO - Molecular functioni

  • drug binding Source: UniProtKB
  • RNA polymerase II regulatory region sequence-specific DNA binding Source: NTNU_SB
  • RNA polymerase II transcription factor activity, ligand-activated sequence-specific DNA binding Source: UniProtKB
  • steroid hormone receptor activity Source: InterPro
  • transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding Source: NTNU_SB
  • transcription coactivator activity Source: ProtInc
  • zinc ion binding Source: InterPro

GO - Biological processi

  • drug export Source: UniProtKB
  • exogenous drug catabolic process Source: UniProtKB
  • negative regulation of transcription, DNA-templated Source: MGI
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: NTNU_SB
  • signal transduction Source: ProtInc
  • steroid metabolic process Source: ProtInc
  • transcription initiation from RNA polymerase II promoter Source: Reactome
  • xenobiotic metabolic process Source: UniProtKB
  • xenobiotic transport Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Activator, Receptor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:ENSG00000144852-MONOMER.
ReactomeiR-HSA-383280. Nuclear Receptor transcription pathway.
SignaLinkiO75469.
SIGNORiO75469.

Chemistry databases

SwissLipidsiSLP:000001583.

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear receptor subfamily 1 group I member 2
Alternative name(s):
Orphan nuclear receptor PAR1
Orphan nuclear receptor PXR
Pregnane X receptor
Steroid and xenobiotic receptor
Short name:
SXR
Gene namesi
Name:NR1I2
Synonyms:PXR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:7968. NR1I2.

Subcellular locationi

  • Nucleus PROSITE-ProRule annotation1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi66 – 67RR → AA: Abolishes nuclear localization; when associated with 91-A-A-92. 1 Publication2
Mutagenesisi91 – 92RR → AA: Abolishes nuclear localization; when associated with 66-A-A-67. 1 Publication2

Organism-specific databases

DisGeNETi8856.
OpenTargetsiENSG00000144852.
PharmGKBiPA378.

Chemistry databases

ChEMBLiCHEMBL3401.
DrugBankiDB01248. Docetaxel.
DB00530. Erlotinib.
DB00783. Estradiol.
DB00977. Ethinyl Estradiol.
DB01229. Paclitaxel.
DB01045. Rifampicin.
DB01220. Rifaximin.
DB08864. Rilpivirine.
DB00163. Vitamin E.
GuidetoPHARMACOLOGYi606.

Polymorphism and mutation databases

BioMutaiNR1I2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000535471 – 434Nuclear receptor subfamily 1 group I member 2Add BLAST434

Proteomic databases

PaxDbiO75469.
PeptideAtlasiO75469.
PRIDEiO75469.

PTM databases

iPTMnetiO75469.
PhosphoSitePlusiO75469.

Expressioni

Tissue specificityi

Expressed in liver, colon and small intestine.

Gene expression databases

BgeeiENSG00000144852.
ExpressionAtlasiO75469. baseline and differential.
GenevisibleiO75469. HS.

Interactioni

Subunit structurei

Heterodimer with RXR. Interacts with NCOA1.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HSP90AB1P082382EBI-3905991,EBI-352572

Protein-protein interaction databases

BioGridi114380. 34 interactors.
IntActiO75469. 9 interactors.
STRINGi9606.ENSP00000336528.

Chemistry databases

BindingDBiO75469.

Structurei

Secondary structure

1434
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi145 – 161Combined sources17
Helixi193 – 206Combined sources14
Helixi207 – 209Combined sources3
Beta strandi211 – 216Combined sources6
Beta strandi218 – 220Combined sources3
Beta strandi222 – 226Combined sources5
Beta strandi231 – 233Combined sources3
Helixi234 – 237Combined sources4
Helixi240 – 260Combined sources21
Helixi262 – 265Combined sources4
Helixi269 – 290Combined sources22
Turni294 – 297Combined sources4
Beta strandi298 – 301Combined sources4
Beta strandi304 – 308Combined sources5
Beta strandi311 – 313Combined sources3
Helixi315 – 318Combined sources4
Helixi322 – 332Combined sources11
Helixi337 – 348Combined sources12
Beta strandi351 – 353Combined sources3
Helixi359 – 380Combined sources22
Helixi384 – 386Combined sources3
Helixi389 – 417Combined sources29
Helixi423 – 428Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ILGX-ray2.52A130-434[»]
1ILHX-ray2.76A130-434[»]
1M13X-ray2.15A130-434[»]
1NRLX-ray2.00A/B130-434[»]
1SKXX-ray2.80A130-431[»]
2O9IX-ray2.80A/B142-434[»]
2QNVX-ray2.80A130-434[»]
3CTBX-ray2.00A/B130-434[»]
3HVLX-ray2.10A/B130-434[»]
3R8DX-ray2.80A130-434[»]
4J5WX-ray2.80A/B130-434[»]
4J5XX-ray2.80A/B130-434[»]
4NY9X-ray2.80A142-431[»]
4S0SX-ray2.80A/B130-434[»]
4S0TX-ray3.14A/B130-434[»]
4X1FX-ray2.00A130-434[»]
4X1GX-ray2.25A130-434[»]
4XAOX-ray2.58A130-434[»]
4XHDX-ray2.40A130-434[»]
5A86X-ray2.25A/B130-432[»]
DisProtiDP00323.
ProteinModelPortaliO75469.
SMRiO75469.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO75469.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni108 – 204HingeAdd BLAST97
Regioni205 – 434Ligand-bindingAdd BLAST230

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi66 – 92Bipartite nuclear localization signalAdd BLAST27

Sequence similaritiesi

Contains 1 nuclear receptor DNA-binding domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri41 – 61NR C4-typePROSITE-ProRule annotationAdd BLAST21
Zinc fingeri77 – 102NR C4-typePROSITE-ProRule annotationAdd BLAST26

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG3575. Eukaryota.
ENOG410XRZC. LUCA.
GeneTreeiENSGT00850000132242.
HOVERGENiHBG108655.
InParanoidiO75469.
KOiK08540.
OMAiYIECNRP.
OrthoDBiEOG091G05X3.
PhylomeDBiO75469.
TreeFamiTF316304.

Family and domain databases

Gene3Di1.10.565.10. 2 hits.
3.30.50.10. 1 hit.
InterProiIPR000536. Nucl_hrmn_rcpt_lig-bd.
IPR001723. Nuclear_hrmn_rcpt.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PfamiPF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSiPR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTiSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMiSSF48508. SSF48508. 1 hit.
PROSITEiPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]

Sequences (7)i

Sequence statusi: Complete.

This entry describes 7 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1A (identifier: O75469-1) [UniParc]FASTAAdd to basket
Also known as: 1, PRR1-A

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
MEVRPKESWN HADFVHCEDT ESVPGKPSVN ADEEVGGPQI CRVCGDKATG
60 70 80 90 100
YHFNVMTCEG CKGFFRRAMK RNARLRCPFR KGACEITRKT RRQCQACRLR
110 120 130 140 150
KCLESGMKKE MIMSDEAVEE RRALIKRKKS ERTGTQPLGV QGLTEEQRMM
160 170 180 190 200
IRELMDAQMK TFDTTFSHFK NFRLPGVLSS GCELPESLQA PSREEAAKWS
210 220 230 240 250
QVRKDLCSLK VSLQLRGEDG SVWNYKPPAD SGGKEIFSLL PHMADMSTYM
260 270 280 290 300
FKGIISFAKV ISYFRDLPIE DQISLLKGAA FELCQLRFNT VFNAETGTWE
310 320 330 340 350
CGRLSYCLED TAGGFQQLLL EPMLKFHYML KKLQLHEEEY VLMQAISLFS
360 370 380 390 400
PDRPGVLQHR VVDQLQEQFA ITLKSYIECN RPQPAHRFLF LKIMAMLTEL
410 420 430
RSINAQHTQR LLRIQDIHPF ATPLMQELFG ITGS
Length:434
Mass (Da):49,762
Last modified:November 1, 1998 - v1
Checksum:i1DF6A2AE3109C4DA
GO
Isoform 1B (identifier: O75469-2) [UniParc]FASTAAdd to basket
Also known as: PRR1-B

The sequence of this isoform differs from the canonical sequence as follows:
     1-55: Missing.

Show »
Length:379
Mass (Da):43,706
Checksum:i7B79CBF8A100C0F0
GO
Isoform 1C (identifier: O75469-3) [UniParc]FASTAAdd to basket
Also known as: PRR1-C

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

Show »
Length:457
Mass (Da):52,129
Checksum:i37EFF759461EFE94
GO
Isoform 2A (identifier: O75469-4) [UniParc]FASTAAdd to basket
Also known as: 2, PRR2-A

The sequence of this isoform differs from the canonical sequence as follows:
     174-210: Missing.

Show »
Length:397
Mass (Da):45,766
Checksum:i5F0007EFD27260F9
GO
Isoform 2B (identifier: O75469-5) [UniParc]FASTAAdd to basket
Also known as: PRR2-B

The sequence of this isoform differs from the canonical sequence as follows:
     1-55: Missing.
     174-210: Missing.

Show »
Length:342
Mass (Da):39,710
Checksum:i7D4EA16E5A132B0B
GO
Isoform 2C (identifier: O75469-6) [UniParc]FASTAAdd to basket
Also known as: PRR2-C

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MDPRGEVGAKNLPPNSPRGPEANL
     174-210: Missing.

Show »
Length:420
Mass (Da):48,134
Checksum:iCE6179469491C1EF
GO
Isoform 3 (identifier: O75469-7) [UniParc]FASTAAdd to basket

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

Show »
Length:473
Mass (Da):53,899
Checksum:i3049D23C9B903016
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti109K → N in CAB55489 (Ref. 5) Curated1
Sequence conflicti109K → N in CAB55490 (Ref. 5) Curated1
Sequence conflicti109K → N in CAB55491 (Ref. 5) Curated1
Sequence conflicti109K → N in CAB55492 (Ref. 5) Curated1
Sequence conflicti109K → N in CAB55493 (Ref. 5) Curated1
Sequence conflicti109K → N in CAB55494 (Ref. 5) Curated1
Sequence conflicti174Missing in AAH17304 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05058112A → T.1 PublicationCorresponds to variant rs1063955dbSNPEnsembl.1
Natural variantiVAR_03323718E → K.1 PublicationCorresponds to variant rs59371185dbSNPEnsembl.1
Natural variantiVAR_01222827P → S in allele PXR*2. 2 PublicationsCorresponds to variant rs12721613dbSNPEnsembl.1
Natural variantiVAR_01222936G → R in allele PXR*3. 1 Publication1
Natural variantiVAR_01834098R → C.1 Publication1
Natural variantiVAR_012230122R → Q in allele PXR*4; rare polymorphism. 1 Publication1
Natural variantiVAR_018341148R → Q.1 Publication1
Natural variantiVAR_033238370A → T.1 PublicationCorresponds to variant rs35761343dbSNPEnsembl.1
Natural variantiVAR_018342381R → W.1 Publication1
Natural variantiVAR_018343403I → V.1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0036681 – 55Missing in isoform 1B and isoform 2B. 1 PublicationAdd BLAST55
Alternative sequenceiVSP_0036671M → MDPRGEVGAKNLPPNSPRGP EANL in isoform 1C and isoform 2C. 1 Publication1
Alternative sequenceiVSP_0266691M → MTVTRTHHFKEGSLRAPAIP LHSAAAELASNHPRGPEANL in isoform 3. 1 Publication1
Alternative sequenceiVSP_003669174 – 210Missing in isoform 2A, isoform 2B and isoform 2C. 1 PublicationAdd BLAST37

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY091855 mRNA. Translation: AAM26736.1.
AF061056 mRNA. Translation: AAD05436.1.
AF084644 mRNA. Translation: AAC64557.1.
AF084645 mRNA. Translation: AAC64558.1.
AF364606 Genomic DNA. Translation: AAK38720.1.
AF364606 Genomic DNA. Translation: AAK38721.1.
AF364606 Genomic DNA. Translation: AAK38722.1.
AJ009936 mRNA. Translation: CAB55489.1.
AJ009936 mRNA. Translation: CAB55490.1.
AJ009936 mRNA. Translation: CAB55491.1.
AJ009937 mRNA. Translation: CAB55492.1.
AJ009937 mRNA. Translation: CAB55493.1.
AJ009937 mRNA. Translation: CAB55494.1.
DQ911122 Genomic DNA. Translation: ABJ52965.1.
DQ923326 Genomic DNA. Translation: ABJ52966.1.
EF614253 Genomic DNA. Translation: ABR09276.1.
BC017304 mRNA. Translation: AAH17304.2.
CCDSiCCDS2995.1. [O75469-7]
CCDS43136.1. [O75469-1]
CCDS54627.1. [O75469-4]
RefSeqiNP_003880.3. NM_003889.3. [O75469-1]
NP_071285.1. NM_022002.2. [O75469-7]
NP_148934.1. NM_033013.2. [O75469-4]
UniGeneiHs.7303.

Genome annotation databases

EnsembliENST00000337940; ENSP00000336528; ENSG00000144852. [O75469-7]
GeneIDi8856.
KEGGihsa:8856.
UCSCiuc003edk.3. human. [O75469-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY091855 mRNA. Translation: AAM26736.1.
AF061056 mRNA. Translation: AAD05436.1.
AF084644 mRNA. Translation: AAC64557.1.
AF084645 mRNA. Translation: AAC64558.1.
AF364606 Genomic DNA. Translation: AAK38720.1.
AF364606 Genomic DNA. Translation: AAK38721.1.
AF364606 Genomic DNA. Translation: AAK38722.1.
AJ009936 mRNA. Translation: CAB55489.1.
AJ009936 mRNA. Translation: CAB55490.1.
AJ009936 mRNA. Translation: CAB55491.1.
AJ009937 mRNA. Translation: CAB55492.1.
AJ009937 mRNA. Translation: CAB55493.1.
AJ009937 mRNA. Translation: CAB55494.1.
DQ911122 Genomic DNA. Translation: ABJ52965.1.
DQ923326 Genomic DNA. Translation: ABJ52966.1.
EF614253 Genomic DNA. Translation: ABR09276.1.
BC017304 mRNA. Translation: AAH17304.2.
CCDSiCCDS2995.1. [O75469-7]
CCDS43136.1. [O75469-1]
CCDS54627.1. [O75469-4]
RefSeqiNP_003880.3. NM_003889.3. [O75469-1]
NP_071285.1. NM_022002.2. [O75469-7]
NP_148934.1. NM_033013.2. [O75469-4]
UniGeneiHs.7303.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ILGX-ray2.52A130-434[»]
1ILHX-ray2.76A130-434[»]
1M13X-ray2.15A130-434[»]
1NRLX-ray2.00A/B130-434[»]
1SKXX-ray2.80A130-431[»]
2O9IX-ray2.80A/B142-434[»]
2QNVX-ray2.80A130-434[»]
3CTBX-ray2.00A/B130-434[»]
3HVLX-ray2.10A/B130-434[»]
3R8DX-ray2.80A130-434[»]
4J5WX-ray2.80A/B130-434[»]
4J5XX-ray2.80A/B130-434[»]
4NY9X-ray2.80A142-431[»]
4S0SX-ray2.80A/B130-434[»]
4S0TX-ray3.14A/B130-434[»]
4X1FX-ray2.00A130-434[»]
4X1GX-ray2.25A130-434[»]
4XAOX-ray2.58A130-434[»]
4XHDX-ray2.40A130-434[»]
5A86X-ray2.25A/B130-432[»]
DisProtiDP00323.
ProteinModelPortaliO75469.
SMRiO75469.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114380. 34 interactors.
IntActiO75469. 9 interactors.
STRINGi9606.ENSP00000336528.

Chemistry databases

BindingDBiO75469.
ChEMBLiCHEMBL3401.
DrugBankiDB01248. Docetaxel.
DB00530. Erlotinib.
DB00783. Estradiol.
DB00977. Ethinyl Estradiol.
DB01229. Paclitaxel.
DB01045. Rifampicin.
DB01220. Rifaximin.
DB08864. Rilpivirine.
DB00163. Vitamin E.
GuidetoPHARMACOLOGYi606.
SwissLipidsiSLP:000001583.

PTM databases

iPTMnetiO75469.
PhosphoSitePlusiO75469.

Polymorphism and mutation databases

BioMutaiNR1I2.

Proteomic databases

PaxDbiO75469.
PeptideAtlasiO75469.
PRIDEiO75469.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000337940; ENSP00000336528; ENSG00000144852. [O75469-7]
GeneIDi8856.
KEGGihsa:8856.
UCSCiuc003edk.3. human. [O75469-1]

Organism-specific databases

CTDi8856.
DisGeNETi8856.
GeneCardsiNR1I2.
HGNCiHGNC:7968. NR1I2.
MIMi603065. gene.
neXtProtiNX_O75469.
OpenTargetsiENSG00000144852.
PharmGKBiPA378.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3575. Eukaryota.
ENOG410XRZC. LUCA.
GeneTreeiENSGT00850000132242.
HOVERGENiHBG108655.
InParanoidiO75469.
KOiK08540.
OMAiYIECNRP.
OrthoDBiEOG091G05X3.
PhylomeDBiO75469.
TreeFamiTF316304.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000144852-MONOMER.
ReactomeiR-HSA-383280. Nuclear Receptor transcription pathway.
SignaLinkiO75469.
SIGNORiO75469.

Miscellaneous databases

ChiTaRSiNR1I2. human.
EvolutionaryTraceiO75469.
GeneWikiiPregnane_X_receptor.
GenomeRNAii8856.
PROiO75469.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000144852.
ExpressionAtlasiO75469. baseline and differential.
GenevisibleiO75469. HS.

Family and domain databases

Gene3Di1.10.565.10. 2 hits.
3.30.50.10. 1 hit.
InterProiIPR000536. Nucl_hrmn_rcpt_lig-bd.
IPR001723. Nuclear_hrmn_rcpt.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PfamiPF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSiPR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTiSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMiSSF48508. SSF48508. 1 hit.
PROSITEiPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNR1I2_HUMAN
AccessioniPrimary (citable) accession number: O75469
Secondary accession number(s): Q006P5
, Q008C8, Q96AC7, Q9UJ22, Q9UJ23, Q9UJ24, Q9UJ25, Q9UJ26, Q9UJ27, Q9UNW4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1998
Last modified: November 2, 2016
This is version 184 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: 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.