Full text data of PGRMC2
PGRMC2
(DG6, PMBP)
[Confidence: high (present in two of the MS resources)]
Membrane-associated progesterone receptor component 2 (Progesterone membrane-binding protein; Steroid receptor protein DG6)
Membrane-associated progesterone receptor component 2 (Progesterone membrane-binding protein; Steroid receptor protein DG6)
hRBCD
IPI00005202
IPI00005202 Membrane associated progesterone receptor component 2 Membrane associated progesterone receptor component 2 membrane n/a 1 1 n/a 1 n/a 1 n/a 2 n/a n/a n/a 1 n/a n/a n/a n/a n/a 1 n/a integral membrane protein n/a found at its expected molecular weight found at molecular weight
IPI00005202 Membrane associated progesterone receptor component 2 Membrane associated progesterone receptor component 2 membrane n/a 1 1 n/a 1 n/a 1 n/a 2 n/a n/a n/a 1 n/a n/a n/a n/a n/a 1 n/a integral membrane protein n/a found at its expected molecular weight found at molecular weight
UniProt
O15173
ID PGRC2_HUMAN Reviewed; 223 AA.
AC O15173; Q569H1;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JAN-1998, sequence version 1.
DT 22-JAN-2014, entry version 115.
DE RecName: Full=Membrane-associated progesterone receptor component 2;
DE AltName: Full=Progesterone membrane-binding protein;
DE AltName: Full=Steroid receptor protein DG6;
GN Name=PGRMC2; Synonyms=DG6, PMBP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=9705155;
RA Gerdes D., Wehling M., Leube B., Falkenstein E.;
RT "Cloning and tissue expression of two putative steroid membrane
RT receptors.";
RL Biol. Chem. 379:907-911(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NIEHS SNPs program;
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-210 AND THR-211, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by
RT enrichment and fractionation of phosphopeptides with strong anion
RT exchange chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, AND MASS
RP SPECTROMETRY.
RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90 AND THR-211, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-211, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Receptor for steroids (Potential).
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein
CC (Potential).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O15173-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O15173-2; Sequence=VSP_053500;
CC Note=No experimental confirmation available;
CC -!- DOMAIN: The cytochrome b5 heme-binding domain lacks the conserved
CC iron-binding His residues at positions 137 and 161 (By
CC similarity).
CC -!- SIMILARITY: Belongs to the cytochrome b5 family. MAPR subfamily.
CC -!- SIMILARITY: Contains 1 cytochrome b5 heme-binding domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AJ002030; CAA05152.1; -; mRNA.
DR EMBL; AK131272; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; DQ496105; ABF47094.1; -; Genomic_DNA.
DR EMBL; BC016692; AAH16692.1; -; mRNA.
DR EMBL; BC092478; AAH92478.1; -; mRNA.
DR RefSeq; NP_006311.2; NM_006320.4.
DR UniGene; Hs.507910; -.
DR ProteinModelPortal; O15173; -.
DR SMR; O15173; 102-201.
DR IntAct; O15173; 2.
DR MINT; MINT-5002204; -.
DR STRING; 9606.ENSP00000377817; -.
DR PhosphoSite; O15173; -.
DR PaxDb; O15173; -.
DR PRIDE; O15173; -.
DR Ensembl; ENST00000296425; ENSP00000296425; ENSG00000164040.
DR GeneID; 10424; -.
DR UCSC; uc003igg.3; human.
DR GeneCards; GC04M129190; -.
DR H-InvDB; HIX0004497; -.
DR HGNC; HGNC:16089; PGRMC2.
DR HPA; HPA041172; -.
DR MIM; 607735; gene.
DR neXtProt; NX_O15173; -.
DR eggNOG; NOG291734; -.
DR HOGENOM; HOG000187840; -.
DR HOVERGEN; HBG059971; -.
DR InParanoid; O15173; -.
DR OrthoDB; EOG7KWSKJ; -.
DR PhylomeDB; O15173; -.
DR ChiTaRS; PGRMC2; human.
DR NextBio; 13601376; -.
DR PRO; PR:O15173; -.
DR ArrayExpress; O15173; -.
DR Bgee; O15173; -.
DR CleanEx; HS_PGRMC2; -.
DR Genevestigator; O15173; -.
DR GO; GO:0016021; C:integral to membrane; TAS:ProtInc.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005496; F:steroid binding; TAS:ProtInc.
DR GO; GO:0003707; F:steroid hormone receptor activity; TAS:ProtInc.
DR Gene3D; 3.10.120.10; -; 1.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR Pfam; PF00173; Cyt-b5; 1.
DR SUPFAM; SSF55856; SSF55856; 1.
DR PROSITE; PS00191; CYTOCHROME_B5_1; FALSE_NEG.
DR PROSITE; PS50255; CYTOCHROME_B5_2; FALSE_NEG.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Lipid-binding; Membrane;
KW Phosphoprotein; Receptor; Reference proteome; Steroid-binding;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1 223 Membrane-associated progesterone receptor
FT component 2.
FT /FTId=PRO_0000121743.
FT TRANSMEM 42 66 Helical; (Potential).
FT DOMAIN 102 201 Cytochrome b5 heme-binding.
FT MOD_RES 90 90 Phosphoserine.
FT MOD_RES 208 208 Phosphoserine (By similarity).
FT MOD_RES 210 210 Phosphotyrosine.
FT MOD_RES 211 211 Phosphothreonine.
FT VAR_SEQ 1 1 M -> MGGAGRGVGEGRGRGGGGRRWRAVM (in
FT isoform 2).
FT /FTId=VSP_053500.
SQ SEQUENCE 223 AA; 23818 MW; BE36229EDF0FF3AD CRC64;
MAAGDGDVKL GTLGSGSESS NDGGSESPGD AGAAAEGGGW AAAALALLTG GGEMLLNVAL
VALVLLGAYR LWVRWGRRGL GAGAGAGEES PATSLPRMKK RDFSLEQLRQ YDGSRNPRIL
LAVNGKVFDV TKGSKFYGPA GPYGIFAGRD ASRGLATFCL DKDALRDEYD DLSDLNAVQM
ESVREWEMQF KEKYDYVGRL LKPGEEPSEY TDEEDTKDHN KQD
//
ID PGRC2_HUMAN Reviewed; 223 AA.
AC O15173; Q569H1;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JAN-1998, sequence version 1.
DT 22-JAN-2014, entry version 115.
DE RecName: Full=Membrane-associated progesterone receptor component 2;
DE AltName: Full=Progesterone membrane-binding protein;
DE AltName: Full=Steroid receptor protein DG6;
GN Name=PGRMC2; Synonyms=DG6, PMBP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=9705155;
RA Gerdes D., Wehling M., Leube B., Falkenstein E.;
RT "Cloning and tissue expression of two putative steroid membrane
RT receptors.";
RL Biol. Chem. 379:907-911(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NIEHS SNPs program;
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-210 AND THR-211, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by
RT enrichment and fractionation of phosphopeptides with strong anion
RT exchange chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, AND MASS
RP SPECTROMETRY.
RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90 AND THR-211, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-211, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Receptor for steroids (Potential).
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein
CC (Potential).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O15173-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O15173-2; Sequence=VSP_053500;
CC Note=No experimental confirmation available;
CC -!- DOMAIN: The cytochrome b5 heme-binding domain lacks the conserved
CC iron-binding His residues at positions 137 and 161 (By
CC similarity).
CC -!- SIMILARITY: Belongs to the cytochrome b5 family. MAPR subfamily.
CC -!- SIMILARITY: Contains 1 cytochrome b5 heme-binding domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AJ002030; CAA05152.1; -; mRNA.
DR EMBL; AK131272; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; DQ496105; ABF47094.1; -; Genomic_DNA.
DR EMBL; BC016692; AAH16692.1; -; mRNA.
DR EMBL; BC092478; AAH92478.1; -; mRNA.
DR RefSeq; NP_006311.2; NM_006320.4.
DR UniGene; Hs.507910; -.
DR ProteinModelPortal; O15173; -.
DR SMR; O15173; 102-201.
DR IntAct; O15173; 2.
DR MINT; MINT-5002204; -.
DR STRING; 9606.ENSP00000377817; -.
DR PhosphoSite; O15173; -.
DR PaxDb; O15173; -.
DR PRIDE; O15173; -.
DR Ensembl; ENST00000296425; ENSP00000296425; ENSG00000164040.
DR GeneID; 10424; -.
DR UCSC; uc003igg.3; human.
DR GeneCards; GC04M129190; -.
DR H-InvDB; HIX0004497; -.
DR HGNC; HGNC:16089; PGRMC2.
DR HPA; HPA041172; -.
DR MIM; 607735; gene.
DR neXtProt; NX_O15173; -.
DR eggNOG; NOG291734; -.
DR HOGENOM; HOG000187840; -.
DR HOVERGEN; HBG059971; -.
DR InParanoid; O15173; -.
DR OrthoDB; EOG7KWSKJ; -.
DR PhylomeDB; O15173; -.
DR ChiTaRS; PGRMC2; human.
DR NextBio; 13601376; -.
DR PRO; PR:O15173; -.
DR ArrayExpress; O15173; -.
DR Bgee; O15173; -.
DR CleanEx; HS_PGRMC2; -.
DR Genevestigator; O15173; -.
DR GO; GO:0016021; C:integral to membrane; TAS:ProtInc.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005496; F:steroid binding; TAS:ProtInc.
DR GO; GO:0003707; F:steroid hormone receptor activity; TAS:ProtInc.
DR Gene3D; 3.10.120.10; -; 1.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR Pfam; PF00173; Cyt-b5; 1.
DR SUPFAM; SSF55856; SSF55856; 1.
DR PROSITE; PS00191; CYTOCHROME_B5_1; FALSE_NEG.
DR PROSITE; PS50255; CYTOCHROME_B5_2; FALSE_NEG.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Lipid-binding; Membrane;
KW Phosphoprotein; Receptor; Reference proteome; Steroid-binding;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1 223 Membrane-associated progesterone receptor
FT component 2.
FT /FTId=PRO_0000121743.
FT TRANSMEM 42 66 Helical; (Potential).
FT DOMAIN 102 201 Cytochrome b5 heme-binding.
FT MOD_RES 90 90 Phosphoserine.
FT MOD_RES 208 208 Phosphoserine (By similarity).
FT MOD_RES 210 210 Phosphotyrosine.
FT MOD_RES 211 211 Phosphothreonine.
FT VAR_SEQ 1 1 M -> MGGAGRGVGEGRGRGGGGRRWRAVM (in
FT isoform 2).
FT /FTId=VSP_053500.
SQ SEQUENCE 223 AA; 23818 MW; BE36229EDF0FF3AD CRC64;
MAAGDGDVKL GTLGSGSESS NDGGSESPGD AGAAAEGGGW AAAALALLTG GGEMLLNVAL
VALVLLGAYR LWVRWGRRGL GAGAGAGEES PATSLPRMKK RDFSLEQLRQ YDGSRNPRIL
LAVNGKVFDV TKGSKFYGPA GPYGIFAGRD ASRGLATFCL DKDALRDEYD DLSDLNAVQM
ESVREWEMQF KEKYDYVGRL LKPGEEPSEY TDEEDTKDHN KQD
//
MIM
607735
*RECORD*
*FIELD* NO
607735
*FIELD* TI
*607735 PROGESTERONE RECEPTOR MEMBRANE COMPONENT 2; PGRMC2
*FIELD* TX
CLONING
Using the sequence of a porcine progesterone receptor as probe, Gerdes
read moreet al. (1998) cloned PGRMC2, which they designated DG6. The deduced
protein contains 223 amino acids and has an N-terminal hydrophobic
region. It has no N-glycosylation site. PGRMC2 shares about 50% identity
overall with PGRMC1 (300435), and they share 68% identity in their C
termini, including a highly conserved 58-amino acid sequence. Northern
blot analysis revealed expression of 2.0-kb transcripts in all tissues
examined, with highest expression in placenta. Transcripts of 3.0 and
5.0 kb were also detected.
MAPPING
By genomic sequence analysis, Gerdes et al. (1998) mapped the PGRMC2
gene to chromosome 4q26.
*FIELD* RF
1. Gerdes, D.; Wehling, M.; Leube, B.; Falkenstein, E.: Cloning and
tissue expression of two putative steroid membrane receptors. Biol.
Chem. 379: 907-911, 1998.
*FIELD* CD
Patricia A. Hartz: 4/30/2003
*FIELD* ED
mgross: 04/30/2003
*RECORD*
*FIELD* NO
607735
*FIELD* TI
*607735 PROGESTERONE RECEPTOR MEMBRANE COMPONENT 2; PGRMC2
*FIELD* TX
CLONING
Using the sequence of a porcine progesterone receptor as probe, Gerdes
read moreet al. (1998) cloned PGRMC2, which they designated DG6. The deduced
protein contains 223 amino acids and has an N-terminal hydrophobic
region. It has no N-glycosylation site. PGRMC2 shares about 50% identity
overall with PGRMC1 (300435), and they share 68% identity in their C
termini, including a highly conserved 58-amino acid sequence. Northern
blot analysis revealed expression of 2.0-kb transcripts in all tissues
examined, with highest expression in placenta. Transcripts of 3.0 and
5.0 kb were also detected.
MAPPING
By genomic sequence analysis, Gerdes et al. (1998) mapped the PGRMC2
gene to chromosome 4q26.
*FIELD* RF
1. Gerdes, D.; Wehling, M.; Leube, B.; Falkenstein, E.: Cloning and
tissue expression of two putative steroid membrane receptors. Biol.
Chem. 379: 907-911, 1998.
*FIELD* CD
Patricia A. Hartz: 4/30/2003
*FIELD* ED
mgross: 04/30/2003