O00264 (PGRC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Membrane-associated progesterone receptor component 1
Short name=mPR

Gene names

Name:	PGRMC1
Synonyms:	HPR6.6, PGRMC

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	195 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Receptor for progesterone By similarity.
Subcellular location	Microsome membrane; Single-pass membrane protein By similarity. Endoplasmic reticulum membrane; Single-pass membrane protein By similarity.
Tissue specificity	Widely expressed, with highest expression in liver and kidney.
Domain	The cytochrome b5 heme-binding domain lacks the conserved iron-binding His residues at positions 107 and 131 By similarity.
Sequence similarities	Belongs to the cytochrome b5 family. MAPR subfamily. Contains 1 cytochrome b5 heme-binding domain.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane Microsome
Domain	Transmembrane Transmembrane helix
Ligand	Lipid-binding Steroid-binding
Molecular function	Receptor
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Cellular component	cell surface Inferred from direct assay. Source: UniProtKB endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW microsome Inferred from electronic annotation. Source: UniProtKB-SubCell nucleolus Inferred from direct assay. Source: HPA
Molecular function	heme binding Inferred from electronic annotation. Source: InterPro receptor activity Inferred from electronic annotation. Source: UniProtKB-KW steroid binding Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ABCD3	P28288	1	EBI-1045534,EBI-80992
DDOST	P39656	1	EBI-1045534,EBI-358866
EFHD1	Q9BUP0	1	EBI-1045534,EBI-1055068
HEATR2	Q86Y56	1	EBI-1045534,EBI-719966
SFXN1	Q9H9B4	1	EBI-1045534,EBI-355861

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 195	194	Membrane-associated progesterone receptor component 1		PRO_0000121739
Regions
	Topological domain	2 – 24	23	Lumenal Potential
	Transmembrane	25 – 43	19	Helical; Potential
	Topological domain	44 – 195	152	Cytoplasmic Potential
	Domain	72 – 171	100	Cytochrome b5 heme-binding
Amino acid modifications
	Modified residue	54	1	Phosphoserine Ref.13 Ref.17 Ref.18
	Modified residue	57	1	Phosphoserine Ref.5 Ref.6 Ref.10 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18
	Modified residue	74	1	Phosphothreonine Ref.13 Ref.14
	Modified residue	178	1	Phosphothreonine Ref.16 Ref.17
	Modified residue	180	1	Phosphotyrosine Ref.6 Ref.17
	Modified residue	181	1	Phosphoserine Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17

Sequences

	Sequence		Length	Mass (Da)
	O00264 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: CCD5E802E1C9E604	FASTA	195	21,671
	10 20 30 40 50 60 MAAEDVVATG ADPSDLESGG LLHEIFTSPL NLLLLGLCIF LLYKIVRGDQ PAASGDSDDD 70 80 90 100 110 120 EPPPLPRLKR RDFTPAELRR FDGVQDPRIL MAINGKVFDV TKGRKFYGPE GPYGVFAGRD 130 140 150 160 170 180 ASRGLATFCL DKEALKDEYD DLSDLTAAQQ ETLSDWESQF TFKYHHVGKL LKEGEEPTVY 190 SDEEEPKDES ARKND

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and tissue expression of two putative steroid membrane receptors." Gerdes D., Wehling M., Leube B., Falkenstein E. Biol. Chem. 379:907-911(1998) [PubMed: 9705155] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[2]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Ovary.
[3]	"The human membrane progesterone receptor gene: genomic structure and promoter analysis." Bernauer S., Wehling M., Gerdes D., Falkenstein E. DNA Seq. 12:13-25(2001) [PubMed: 11697142] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-109.
[4]	Bienvenut W.V., Waridel P., Quadroni M. Submitted (MAR-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 48-67; 81-88; 105-119; 124-132 AND 173-192, PHOSPHORYLATION AT SER-181, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[5]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57 AND SER-181, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[6]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57; TYR-180 AND SER-181, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"Phosphoproteome analysis of the human mitotic spindle." Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R. Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, MASS SPECTROMETRY. Tissue: Cervix adenocarcinoma.
[8]	"Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line." Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S. Electrophoresis 28:2027-2034(2007) [PubMed: 17487921] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, MASS SPECTROMETRY. Tissue: Prostate cancer.
[9]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57 AND SER-181, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[11]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, MASS SPECTROMETRY. Tissue: Platelet.
[12]	"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment." Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J. J. Proteome Res. 7:5167-5176(2008) [PubMed: 19367720] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57, MASS SPECTROMETRY. Tissue: T-cell.
[13]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54; SER-57; THR-74 AND SER-181, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57; THR-74 AND SER-181, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography." Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J. Proteomics 8:1346-1361(2008) [PubMed: 18318008] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57 AND SER-181, MASS SPECTROMETRY. Tissue: Liver.
[16]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57; THR-178 AND SER-181, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[17]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54; SER-57; THR-178; TYR-180 AND SER-181, MASS SPECTROMETRY.
[18]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54 AND SER-57, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[19]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y12711 mRNA. Translation: CAA73248.1. BC034238 mRNA. Translation: AAH34238.1. AJ249131 Genomic DNA. Translation: CAB65109.1.
IPI	IPI00220739.
RefSeq	NP_006658.1. NM_006667.3.
UniGene	Hs.90061.
3D structure databases
ProteinModelPortal	O00264.
SMR	O00264. Positions 70-172.
ModBase	Search...
Protein-protein interaction databases
IntAct	O00264. 1 interaction.
STRING	O00264.
PTM databases
PhosphoSite	O00264.
2D gel databases
OGP	O00264.
Proteomic databases
PeptideAtlas	O00264.
PRIDE	O00264.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000217971; ENSP00000217971; ENSG00000101856.
GeneID	10857.
KEGG	hsa:10857.
UCSC	uc004erb.1. human.
Organism-specific databases
CTD	10857.
GeneCards	GC0XP118370.
H-InvDB	HIX0017010.
HGNC	HGNC:16090. PGRMC1.
HPA	HPA002877.
MIM	300435. gene.
neXtProt	NX_O00264.
PharmGKB	PA33248.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG14875.
HOGENOM	HBG715794.
HOVERGEN	HBG059971.
InParanoid	O00264.
OMA	DVTRGKK.
OrthoDB	EOG4SXNDQ.
PhylomeDB	O00264.
Gene expression databases
ArrayExpress	O00264.
Bgee	O00264.
CleanEx	HS_PGRMC1.
Genevestigator	O00264.
GermOnline	ENSG00000101856. Homo sapiens.
Family and domain databases
InterPro	IPR001199. Cyt_B5. [Graphical view]
Gene3D	G3DSA:3.10.120.10. Cyt_B5. 1 hit.
Pfam	PF00173. Cyt-b5. 1 hit. [Graphical view]
SUPFAM	SSF55856. Cyt_B5. 1 hit.
PROSITE	PS00191. CYTOCHROME_B5_1. False negative. PS50255. CYTOCHROME_B5_2. False negative. [Graphical view]
ProtoNet	Search...
Other
NextBio	41215.
SOURCE	Search...

Entry information

Entry name

PGRC1_HUMAN

Accession

Primary (citable) accession number: O00264
Secondary accession number(s): Q9UGJ9

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 110 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.