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Protein

Membrane-associated progesterone receptor component 2

Gene

PGRMC2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Receptor for steroids.Curated

GO - Molecular functioni

  • heme binding Source: GO_Central
  • steroid binding Source: ProtInc
  • steroid hormone receptor activity Source: ProtInc

GO - Biological processi

  • steroid hormone mediated signaling pathway Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Ligandi

Lipid-binding, Steroid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Membrane-associated progesterone receptor component 2
Alternative name(s):
Progesterone membrane-binding protein
Steroid receptor protein DG6
Gene namesi
Name:PGRMC2
Synonyms:DG6, PMBP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:16089. PGRMC2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei42 – 6625HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

  • endomembrane system Source: GO_Central
  • integral component of membrane Source: ProtInc
  • membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 223223Membrane-associated progesterone receptor component 2PRO_0000121743Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei90 – 901PhosphoserineCombined sources
Modified residuei104 – 1041PhosphoserineBy similarity
Modified residuei208 – 2081PhosphoserineCombined sources
Modified residuei210 – 2101PhosphotyrosineCombined sources
Modified residuei211 – 2111PhosphothreonineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiO15173.
MaxQBiO15173.
PaxDbiO15173.
PRIDEiO15173.
TopDownProteomicsiO15173-1. [O15173-1]

PTM databases

iPTMnetiO15173.
PhosphoSiteiO15173.
SwissPalmiO15173.

Expressioni

Gene expression databases

BgeeiO15173.
CleanExiHS_PGRMC2.
ExpressionAtlasiO15173. baseline and differential.
GenevisibleiO15173. HS.

Organism-specific databases

HPAiHPA041172.

Interactioni

Protein-protein interaction databases

BioGridi115693. 15 interactions.
IntActiO15173. 9 interactions.
MINTiMINT-5002204.
STRINGi9606.ENSP00000429301.

Structurei

3D structure databases

ProteinModelPortaliO15173.
SMRiO15173. Positions 102-201.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini102 – 201100Cytochrome b5 heme-bindingAdd
BLAST

Domaini

The cytochrome b5 heme-binding domain lacks the conserved iron-binding His residues at positions 137 and 161.By similarity

Sequence similaritiesi

Belongs to the cytochrome b5 family. MAPR subfamily.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1110. Eukaryota.
ENOG4111UG0. LUCA.
GeneTreeiENSGT00730000110959.
HOGENOMiHOG000187840.
HOVERGENiHBG059971.
InParanoidiO15173.
KOiK17278.
OMAiKDHSKQD.
OrthoDBiEOG7KWSKJ.
PhylomeDBiO15173.

Family and domain databases

Gene3Di3.10.120.10. 1 hit.
InterProiIPR001199. Cyt_B5-like_heme/steroid-bd.
[Graphical view]
PfamiPF00173. Cyt-b5. 1 hit.
[Graphical view]
SMARTiSM01117. Cyt-b5. 1 hit.
[Graphical view]
SUPFAMiSSF55856. SSF55856. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: O15173-1) [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
MAAGDGDVKL GTLGSGSESS NDGGSESPGD AGAAAEGGGW AAAALALLTG
60 70 80 90 100
GGEMLLNVAL VALVLLGAYR LWVRWGRRGL GAGAGAGEES PATSLPRMKK
110 120 130 140 150
RDFSLEQLRQ YDGSRNPRIL LAVNGKVFDV TKGSKFYGPA GPYGIFAGRD
160 170 180 190 200
ASRGLATFCL DKDALRDEYD DLSDLNAVQM ESVREWEMQF KEKYDYVGRL
210 220
LKPGEEPSEY TDEEDTKDHN KQD
Length:223
Mass (Da):23,818
Last modified:January 1, 1998 - v1
Checksum:iBE36229EDF0FF3AD
GO
Isoform 2 (identifier: O15173-2) [UniParc]FASTAAdd to basket

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

Note: No experimental confirmation available.
Show »
Length:247
Mass (Da):26,170
Checksum:iB0D4D72618C79519
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MGGAGRGVGEGRGRGGGGRR WRAVM in isoform 2. 1 PublicationVSP_053500

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ002030 mRNA. Translation: CAA05152.1.
AK131272 mRNA. No translation available.
DQ496105 Genomic DNA. Translation: ABF47094.1.
BC016692 mRNA. Translation: AAH16692.1.
BC092478 mRNA. Translation: AAH92478.1.
CCDSiCCDS3739.2. [O15173-2]
RefSeqiNP_006311.2. NM_006320.4. [O15173-2]
UniGeneiHs.507910.

Genome annotation databases

EnsembliENST00000296425; ENSP00000296425; ENSG00000164040. [O15173-1]
ENST00000520121; ENSP00000429301; ENSG00000164040. [O15173-2]
ENST00000613358; ENSP00000481886; ENSG00000164040. [O15173-2]
GeneIDi10424.
KEGGihsa:10424.
UCSCiuc003igg.4. human. [O15173-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ002030 mRNA. Translation: CAA05152.1.
AK131272 mRNA. No translation available.
DQ496105 Genomic DNA. Translation: ABF47094.1.
BC016692 mRNA. Translation: AAH16692.1.
BC092478 mRNA. Translation: AAH92478.1.
CCDSiCCDS3739.2. [O15173-2]
RefSeqiNP_006311.2. NM_006320.4. [O15173-2]
UniGeneiHs.507910.

3D structure databases

ProteinModelPortaliO15173.
SMRiO15173. Positions 102-201.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115693. 15 interactions.
IntActiO15173. 9 interactions.
MINTiMINT-5002204.
STRINGi9606.ENSP00000429301.

PTM databases

iPTMnetiO15173.
PhosphoSiteiO15173.
SwissPalmiO15173.

Proteomic databases

EPDiO15173.
MaxQBiO15173.
PaxDbiO15173.
PRIDEiO15173.
TopDownProteomicsiO15173-1. [O15173-1]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000296425; ENSP00000296425; ENSG00000164040. [O15173-1]
ENST00000520121; ENSP00000429301; ENSG00000164040. [O15173-2]
ENST00000613358; ENSP00000481886; ENSG00000164040. [O15173-2]
GeneIDi10424.
KEGGihsa:10424.
UCSCiuc003igg.4. human. [O15173-1]

Organism-specific databases

CTDi10424.
GeneCardsiPGRMC2.
H-InvDBHIX0004497.
HGNCiHGNC:16089. PGRMC2.
HPAiHPA041172.
MIMi607735. gene.
neXtProtiNX_O15173.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1110. Eukaryota.
ENOG4111UG0. LUCA.
GeneTreeiENSGT00730000110959.
HOGENOMiHOG000187840.
HOVERGENiHBG059971.
InParanoidiO15173.
KOiK17278.
OMAiKDHSKQD.
OrthoDBiEOG7KWSKJ.
PhylomeDBiO15173.

Miscellaneous databases

ChiTaRSiPGRMC2. human.
GenomeRNAii10424.
NextBioi13601376.
PROiO15173.
SOURCEiSearch...

Gene expression databases

BgeeiO15173.
CleanExiHS_PGRMC2.
ExpressionAtlasiO15173. baseline and differential.
GenevisibleiO15173. HS.

Family and domain databases

Gene3Di3.10.120.10. 1 hit.
InterProiIPR001199. Cyt_B5-like_heme/steroid-bd.
[Graphical view]
PfamiPF00173. Cyt-b5. 1 hit.
[Graphical view]
SMARTiSM01117. Cyt-b5. 1 hit.
[Graphical view]
SUPFAMiSSF55856. SSF55856. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Liver.
  2. "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] (ISOFORM 2).
    Tissue: Tongue.
  3. NIEHS SNPs program
    Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  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).
    Tissue: Kidney and Testis.
  5. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-210 AND THR-211, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  9. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  12. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90 AND THR-211, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-211, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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 SER-90; SER-208 AND THR-211, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPGRC2_HUMAN
AccessioniPrimary (citable) accession number: O15173
Secondary accession number(s): Q569H1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: May 11, 2016
This is version 137 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. 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.