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Protein

Progesterone receptor

Gene

PGR

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

Functioni

The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Depending on the isoform, progesterone receptor functions as transcriptional activator or repressor.Curated3 Publications
Isoform A: Ligand-dependent transdominant repressor of steroid hormone receptor transcriptional activity including repression of its isoform B, MR and ER. Transrepressional activity may involve recruitment of corepressor NCOR2.Curated3 Publications
Isoform B: Transcriptional activator of several progesteron-dependent promoters in a variety of cell types. Involved in activation of SRC-dependent MAPK signaling on hormone stimulation.1 Publication
Isoform 4: Increases mitochondrial membrane potential and cellular respiration upon stimulation by progesterone.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi567 – 639Nuclear receptorPROSITE-ProRule annotationAdd BLAST73
Zinc fingeri567 – 587NR C4-typePROSITE-ProRule annotationAdd BLAST21
Zinc fingeri603 – 627NR C4-typePROSITE-ProRule annotationAdd BLAST25

GO - Molecular functioni

  • ATPase binding Source: MGI
  • DNA binding Source: ProtInc
  • enzyme binding Source: UniProtKB
  • receptor binding Source: UniProtKB
  • RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: NTNU_SB
  • RNA polymerase II transcription factor activity, ligand-activated sequence-specific DNA binding Source: Ensembl
  • steroid binding Source: UniProtKB-KW
  • steroid hormone receptor activity Source: ProtInc
  • transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding Source: NTNU_SB
  • zinc ion binding Source: InterPro

GO - Biological processi

Keywordsi

Molecular functionDNA-binding, Receptor
Biological processTranscription, Transcription regulation
LigandLipid-binding, Metal-binding, Steroid-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-1251985. Nuclear signaling by ERBB4.
R-HSA-3371497. HSP90 chaperone cycle for steroid hormone receptors (SHR).
R-HSA-383280. Nuclear Receptor transcription pathway.
SignaLinkiP06401.
SIGNORiP06401.

Chemistry databases

SwissLipidsiSLP:000001574.

Names & Taxonomyi

Protein namesi
Recommended name:
Progesterone receptor
Short name:
PR
Alternative name(s):
Nuclear receptor subfamily 3 group C member 3
Gene namesi
Name:PGR
Synonyms:NR3C3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

EuPathDBiHostDB:ENSG00000082175.14.
HGNCiHGNC:8910. PGR.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Membrane, Mitochondrion, Mitochondrion outer membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi7K → R: Some loss of sumoylation; when associated with R-531. Complete loss of sumoylation; when associated with R-388 and R-531. 1 Publication1
Mutagenesisi55L → A: Reduces transcriptional activation; when associated with A-58 and A-59. 1 Publication1
Mutagenesisi58L → A: Reduces transcriptional activation; when associated with A-55 and A-59. 1 Publication1
Mutagenesisi59L → A: Reduces transcriptional activation; when associated with A-55 and A-58. 1 Publication1
Mutagenesisi115L → A: Reduces transcriptional activation; when associated with A-118 and A-119. 1 Publication1
Mutagenesisi118L → A: Reduces transcriptional activation; when associated with A-115 and A-119. 1 Publication1
Mutagenesisi119L → A: Reduces transcriptional activation; when associated with A-115 and A-118. 1 Publication1
Mutagenesisi140W → A, F or R: Reduces transcriptional activation. 1 Publication1
Mutagenesisi294S → A: No effect on interaction with CUEDC2. Impaired progesterone-induced transcriptional activity. No CUEDC2- nor progestin-mediated protein degradation. No change in sumoylation; when associated with A-344 and A-345. 3 Publications1
Mutagenesisi294S → D: Decreases protein stability and increases progesterone-induced transcriptional activity. 3 Publications1
Mutagenesisi344S → A: No interaction with SP1. No change in progestin-induced protein degradation; when associated with A-345. No change in sumoylation; when associated with A-294 and A-345. 2 Publications1
Mutagenesisi345S → A: No change in progestin-induced protein degradation; when associated with A-344. No change in sumoylation; when associated with A-294 and A-344. 2 Publications1
Mutagenesisi388K → R: Great loss of sumoylation; when associated with R-7. Completely abolishes sumoylation; when associated with R-7 and R-531. Loss of CUEDC2-mediated protein degradation. Increased ligand-dependent transcriptional activity. 3 Publications1
Mutagenesisi400S → A: Abolishes CDK2-induced activity in the absence, but not in the presence, of progestin. Delayed nuclear translocation in presence of progestin. 2 Publications1
Mutagenesisi531K → R: Some loss of sumoylation; when associated with R-7. Completely abolishes sumoylation; when associated with R-7 and R-388. 1 Publication1

Organism-specific databases

DisGeNETi5241.
MalaCardsiPGR.
OpenTargetsiENSG00000082175.
PharmGKBiPA266.

Chemistry databases

ChEMBLiCHEMBL208.
DrugBankiDB01431. Allylestrenol.
DB01406. Danazol.
DB00304. Desogestrel.
DB01395. Drospirenone.
DB00378. Dydrogesterone.
DB00823. Ethynodiol diacetate.
DB00294. Etonogestrel.
DB00588. Fluticasone Propionate.
DB06789. Hydroxyprogesterone caproate.
DB00367. Levonorgestrel.
DB00603. Medroxyprogesterone acetate.
DB00351. Megestrol acetate.
DB02998. Methyltrienolone.
DB00834. Mifepristone.
DB06713. Norelgestromin.
DB00717. Norethisterone.
DB00957. Norgestimate.
DB09389. Norgestrel.
DB05253. Proellex.
DB00396. Progesterone.
DB00421. Spironolactone.
DB04787. Tanaproget.
DB08867. Ulipristal.
GuidetoPHARMACOLOGYi627.

Polymorphism and mutation databases

BioMutaiPGR.
DMDMi90110048.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000536931 – 933Progesterone receptorAdd BLAST933

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki7Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Modified residuei20Phosphoserine1 Publication1
Modified residuei81Phosphoserine2 Publications1
Modified residuei102Phosphoserine2 Publications1
Modified residuei130Phosphoserine1 Publication1
Modified residuei162PhosphoserineCombined sources5 Publications1
Modified residuei190Phosphoserine4 Publications1
Modified residuei213Phosphoserine1 Publication1
Modified residuei294Phosphoserine; by MAPK17 Publications1
Modified residuei345Phosphoserine; by MAPK3 Publications1
Cross-linki388Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
Cross-linki388Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication
Modified residuei400Phosphoserine; by CDK23 Publications1
Cross-linki531Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Modified residuei676Phosphoserine1 Publication1

Post-translational modificationi

Phosphorylated on multiple serine sites. Several of these sites are hormone-dependent. Phosphorylation on Ser-294 occurs preferentially on isoform B, is highly hormone-dependent and modulates ubiquitination and sumoylation on Lys-388. Phosphorylation on Ser-102 and Ser-345 also requires induction by hormone. Basal phosphorylation on Ser-81, Ser-162, Ser-190 and Ser-400 is increased in response to progesterone and can be phosphorylated in vitro by the CDK2-A1 complex. Increased levels of phosphorylation on Ser-400 also in the presence of EGF, heregulin, IGF, PMA and FBS. Phosphorylation at this site by CDK2 is ligand-independent, and increases nuclear translocation and transcriptional activity. Phosphorylation at Ser-162 and Ser-294, but not at Ser-190, is impaired during the G2/M phase of the cell cycle. Phosphorylation on Ser-345 by ERK1/2 MAPK is required for interaction with SP1.13 Publications
Sumoylation is hormone-dependent and represses transcriptional activity. Sumoylation on all three sites is enhanced by PIAS3. Desumoylated by SENP1. Sumoylation on Lys-388, the main site of sumoylation, is repressed by ubiquitination on the same site, and modulated by phosphorylation at Ser-294.9 Publications
Ubiquitination is hormone-dependent and represses sumoylation on the same site. Promoted by MAPK-mediated phosphorylation on Ser-294.7 Publications
Palmitoylated by ZDHHC7 and ZDHHC21. Palmitoylation is required for plasma membrane targeting and for rapid intracellular signaling via ERK and AKT kinases and cAMP generation.1 Publication

Keywords - PTMi

Isopeptide bond, Lipoprotein, Palmitate, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP06401.
PaxDbiP06401.
PeptideAtlasiP06401.
PRIDEiP06401.

PTM databases

iPTMnetiP06401.
PhosphoSitePlusiP06401.
SwissPalmiP06401.

Expressioni

Tissue specificityi

In reproductive tissues the expression of isoform A and isoform B varies as a consequence of developmental and hormonal status. Isoform A and isoform B are expressed in comparable levels in uterine glandular epithelium during the proliferative phase of the menstrual cycle. Expression of isoform B but not of isoform A persists in the glands during mid-secretory phase. In the stroma, isoform A is the predominant form throughout the cycle. Heterogeneous isoform expression between the glands of the endometrium basalis and functionalis is implying region-specific responses to hormonal stimuli.1 Publication

Gene expression databases

BgeeiENSG00000082175.
CleanExiHS_PGR.
ExpressionAtlasiP06401. baseline and differential.
GenevisibleiP06401. HS.

Organism-specific databases

HPAiCAB000068.
CAB055100.
HPA004751.
HPA008428.
HPA017176.

Interactioni

Subunit structurei

Interacts with SMARD1 and UNC45A. Interacts with CUEDC2; the interaction promotes ubiquitination, decreases sumoylation, and repesses transcriptional activity. Interacts with PIAS3; the interaction promotes sumoylation of PR in a hormone-dependent manner, inhibits DNA-binding, and alters nuclear export. Interacts with SP1; the interaction requires ligand-induced phosphorylation on Ser-345 by ERK1/2 MAPK. Interacts with PRMT2. Isoform A interacts with NCOR2. Isoform B (but not isoform A) interacts with NCOA2 and NCOA1. Isoform B (but not isoform A) interacts with KLF9.By similarity7 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • ATPase binding Source: MGI
  • enzyme binding Source: UniProtKB
  • receptor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi111260. 68 interactors.
DIPiDIP-5967N.
ELMiP06401.
IntActiP06401. 12 interactors.
MINTiMINT-1505587.
STRINGi9606.ENSP00000325120.

Chemistry databases

BindingDBiP06401.

Structurei

Secondary structure

1933
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni568 – 570Combined sources3
Beta strandi576 – 578Combined sources3
Beta strandi581 – 583Combined sources3
Helixi585 – 596Combined sources12
Beta strandi604 – 607Combined sources4
Turni613 – 618Combined sources6
Helixi620 – 629Combined sources10
Helixi686 – 694Combined sources9
Helixi711 – 735Combined sources25
Helixi739 – 741Combined sources3
Helixi744 – 771Combined sources28
Beta strandi774 – 779Combined sources6
Beta strandi782 – 784Combined sources3
Helixi786 – 788Combined sources3
Helixi792 – 811Combined sources20
Helixi815 – 826Combined sources12
Beta strandi828 – 830Combined sources3
Helixi838 – 857Combined sources20
Helixi863 – 896Combined sources34
Helixi898 – 901Combined sources4
Helixi907 – 921Combined sources15
Beta strandi925 – 927Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A28X-ray1.80A/B678-933[»]
1E3KX-ray2.80A/B676-933[»]
1SQNX-ray1.45A/B673-933[»]
1SR7X-ray1.46A/B676-933[»]
1ZUCX-ray2.00A/B676-933[»]
2C7AX-ray2.50A/B563-640[»]
2OVHX-ray2.00A678-933[»]
2OVMX-ray2.60A678-933[»]
2W8YX-ray1.80A/B678-933[»]
3D90X-ray2.26A/B676-933[»]
3G8OX-ray1.90A/B673-933[»]
3HQ5X-ray2.10A/B678-933[»]
3KBAX-ray2.00A/B681-933[»]
3ZR7X-ray1.65A/B678-933[»]
3ZRAX-ray1.90A/B678-933[»]
3ZRBX-ray1.80A/B678-933[»]
4A2JX-ray2.00A/B678-933[»]
4APUX-ray1.90A/B678-933[»]
4OARX-ray2.41A678-933[»]
5CC0X-ray2.40A/B561-641[»]
ProteinModelPortaliP06401.
SMRiP06401.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06401.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 566Modulating, Pro-RichAdd BLAST566
Regioni1 – 164AF3; mediates transcriptional activation (in isoform B)1 PublicationAdd BLAST164
Regioni165 – 305Mediates transcriptional transrepression (in isoform A)1 PublicationAdd BLAST141
Regioni456 – 546AF1; mediates transcriptional activation1 PublicationAdd BLAST91
Regioni681 – 933Steroid-bindingAdd BLAST253
Regioni687 – 933AF2; mediates transcriptional activation1 PublicationAdd BLAST247

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi55 – 59LXXL motif 11 Publication5
Motifi115 – 119LXXL motif 21 Publication5
Motifi183 – 187Nuclear localization signalSequence analysis5

Domaini

Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain.

Sequence similaritiesi

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri567 – 587NR C4-typePROSITE-ProRule annotationAdd BLAST21
Zinc fingeri603 – 627NR C4-typePROSITE-ProRule annotationAdd BLAST25

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG3575. Eukaryota.
ENOG410XRZC. LUCA.
GeneTreeiENSGT00760000118887.
HOGENOMiHOG000290653.
HOVERGENiHBG007583.
InParanoidiP06401.
KOiK08556.
OMAiCAYPPDA.
OrthoDBiEOG091G04YC.
PhylomeDBiP06401.
TreeFamiTF106510.

Family and domain databases

Gene3Di3.30.50.10. 1 hit.
InterProiView protein in InterPro
IPR000536. Nucl_hrmn_rcpt_lig-bd.
IPR001723. Nuclear_hrmn_rcpt.
IPR000128. Progest_rcpt.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
PfamiView protein in Pfam
PF00104. Hormone_recep. 1 hit.
PF02161. Prog_receptor. 1 hit.
PF00105. zf-C4. 1 hit.
PRINTSiPR00544. PROGESTRONER.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTiView protein in SMART
SM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
SUPFAMiSSF48508. SSF48508. 2 hits.
PROSITEiView protein in PROSITE
PS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative promoter usage and alternative splicing. AlignAdd to basket

Isoform B (identifier: P06401-1) [UniParc]FASTAAdd to basket
Also known as: PRB, PR-B

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
MTELKAKGPR APHVAGGPPS PEVGSPLLCR PAAGPFPGSQ TSDTLPEVSA
60 70 80 90 100
IPISLDGLLF PRPCQGQDPS DEKTQDQQSL SDVEGAYSRA EATRGAGGSS
110 120 130 140 150
SSPPEKDSGL LDSVLDTLLA PSGPGQSQPS PPACEVTSSW CLFGPELPED
160 170 180 190 200
PPAAPATQRV LSPLMSRSGC KVGDSSGTAA AHKVLPRGLS PARQLLLPAS
210 220 230 240 250
ESPHWSGAPV KPSPQAAAVE VEEEDGSESE ESAGPLLKGK PRALGGAAAG
260 270 280 290 300
GGAAAVPPGA AAGGVALVPK EDSRFSAPRV ALVEQDAPMA PGRSPLATTV
310 320 330 340 350
MDFIHVPILP LNHALLAART RQLLEDESYD GGAGAASAFA PPRSSPCASS
360 370 380 390 400
TPVAVGDFPD CAYPPDAEPK DDAYPLYSDF QPPALKIKEE EEGAEASARS
410 420 430 440 450
PRSYLVAGAN PAAFPDFPLG PPPPLPPRAT PSRPGEAAVT AAPASASVSS
460 470 480 490 500
ASSSGSTLEC ILYKAEGAPP QQGPFAPPPC KAPGASGCLL PRDGLPSTSA
510 520 530 540 550
SAAAAGAAPA LYPALGLNGL PQLGYQAAVL KEGLPQVYPP YLNYLRPDSE
560 570 580 590 600
ASQSPQYSFE SLPQKICLIC GDEASGCHYG VLTCGSCKVF FKRAMEGQHN
610 620 630 640 650
YLCAGRNDCI VDKIRRKNCP ACRLRKCCQA GMVLGGRKFK KFNKVRVVRA
660 670 680 690 700
LDAVALPQPV GVPNESQALS QRFTFSPGQD IQLIPPLINL LMSIEPDVIY
710 720 730 740 750
AGHDNTKPDT SSSLLTSLNQ LGERQLLSVV KWSKSLPGFR NLHIDDQITL
760 770 780 790 800
IQYSWMSLMV FGLGWRSYKH VSGQMLYFAP DLILNEQRMK ESSFYSLCLT
810 820 830 840 850
MWQIPQEFVK LQVSQEEFLC MKVLLLLNTI PLEGLRSQTQ FEEMRSSYIR
860 870 880 890 900
ELIKAIGLRQ KGVVSSSQRF YQLTKLLDNL HDLVKQLHLY CLNTFIQSRA
910 920 930
LSVEFPEMMS EVIAAQLPKI LAGMVKPLLF HKK
Note: Produced by alternative promoter usage.
Length:933
Mass (Da):98,981
Last modified:March 21, 2006 - v4
Checksum:i80452E54FF3A0454
GO
Isoform A (identifier: P06401-2) [UniParc]FASTAAdd to basket
Also known as: PRA, PR-A

The sequence of this isoform differs from the canonical sequence as follows:
     1-164: Missing.

Note: Produced by alternative promoter usage.
Show »
Length:769
Mass (Da):82,295
Checksum:iFE676F25282983F3
GO
Isoform 3 (identifier: P06401-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-594: Missing.

Note: Produced by alternative splicing of isoform B.
Show »
Length:339
Mass (Da):38,798
Checksum:i4496D6B5A4EC95FD
GO
Isoform 4 (identifier: P06401-4) [UniParc]FASTAAdd to basket
Also known as: PR-M

The sequence of this isoform differs from the canonical sequence as follows:
     1-16: MTELKAKGPRAPHVAG → MEFIYIYMNFFFFFSV
     17-635: Missing.

Note: Produced by alternative promoter usage.
Show »
Length:314
Mass (Da):36,318
Checksum:iA85692E905BFB9B3
GO
Isoform 5 (identifier: P06401-5) [UniParc]FASTAAdd to basket
Also known as: delta4

The sequence of this isoform differs from the canonical sequence as follows:
     636-737: Missing.

Note: Produced by alternative splicing of isoform B.
Show »
Length:831
Mass (Da):87,747
Checksum:iEC4882171DD1C48B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti226G → S in CAA36018 (PubMed:2328727).Curated1
Sequence conflicti256V → S in CAA36018 (PubMed:2328727).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01922150A → T1 PublicationCorresponds to variant dbSNP:rs11571143Ensembl.1
Natural variantiVAR_019222120A → V1 PublicationCorresponds to variant dbSNP:rs11571144Ensembl.1
Natural variantiVAR_019223186P → L1 PublicationCorresponds to variant dbSNP:rs11571145Ensembl.1
Natural variantiVAR_019224301M → R1 PublicationCorresponds to variant dbSNP:rs11571146Ensembl.1
Natural variantiVAR_016117344S → T2 PublicationsCorresponds to variant dbSNP:rs3740753Ensembl.1
Natural variantiVAR_025555347C → S. Corresponds to variant dbSNP:rs11571147Ensembl.1
Natural variantiVAR_019225444A → S1 PublicationCorresponds to variant dbSNP:rs11571150Ensembl.1
Natural variantiVAR_019226529V → L1 PublicationCorresponds to variant dbSNP:rs11571151Ensembl.1
Natural variantiVAR_019227536Q → P1 PublicationCorresponds to variant dbSNP:rs11571152Ensembl.1
Natural variantiVAR_014627625R → I. Corresponds to variant dbSNP:rs2020874Ensembl.1
Natural variantiVAR_019228651L → V1 PublicationCorresponds to variant dbSNP:rs11571222Ensembl.1
Natural variantiVAR_016118660V → L3 PublicationsCorresponds to variant dbSNP:rs1042838Ensembl.1
Natural variantiVAR_014628865S → L1 PublicationCorresponds to variant dbSNP:rs2020880Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0469421 – 594Missing in isoform 3. 1 PublicationAdd BLAST594
Alternative sequenceiVSP_0037061 – 164Missing in isoform A. CuratedAdd BLAST164
Alternative sequenceiVSP_0474541 – 16MTELK…PHVAG → MEFIYIYMNFFFFFSV in isoform 4. 1 PublicationAdd BLAST16
Alternative sequenceiVSP_04745517 – 635Missing in isoform 4. 1 PublicationAdd BLAST619
Alternative sequenceiVSP_053543636 – 737Missing in isoform 5. 1 PublicationAdd BLAST102

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51730 mRNA. Translation: CAA36018.1.
M15716 mRNA. Translation: AAA60081.1.
AF016381 mRNA. Translation: AAD01587.1.
AB084248 mRNA. Translation: BAB91074.1.
DQ234979 Genomic DNA. Translation: ABB72139.1.
AY212933 mRNA. Translation: AAO61671.1.
AK304853 mRNA. Translation: BAG65592.1.
AY525610 Genomic DNA. Translation: AAS00096.1.
AP001533 Genomic DNA. No translation available.
CH471065 Genomic DNA. Translation: EAW66999.1.
CH471065 Genomic DNA. Translation: EAW67000.1.
CCDSiCCDS59229.1. [P06401-3]
CCDS8310.1. [P06401-1]
PIRiS09971. QRHUP.
RefSeqiNP_000917.3. NM_000926.4. [P06401-1]
NP_001189403.1. NM_001202474.3. [P06401-2]
NP_001258090.1. NM_001271161.2.
NP_001258091.1. NM_001271162.1. [P06401-3]
UniGeneiHs.32405.
Hs.742403.

Genome annotation databases

EnsembliENST00000263463; ENSP00000263463; ENSG00000082175. [P06401-5]
ENST00000325455; ENSP00000325120; ENSG00000082175. [P06401-1]
ENST00000534013; ENSP00000436561; ENSG00000082175. [P06401-3]
GeneIDi5241.
KEGGihsa:5241.
UCSCiuc001pgh.3. human. [P06401-1]

Keywords - Coding sequence diversityi

Alternative promoter usage, Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiPRGR_HUMAN
AccessioniPrimary (citable) accession number: P06401
Secondary accession number(s): A7LQ08
, A7X8B0, B4E3T0, Q8TDS3, Q9UPF7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: March 21, 2006
Last modified: September 27, 2017
This is version 222 of the entry and version 4 of the sequence. See 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: 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