Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Membrane-associated progesterone receptor component 1

Gene

PGRMC1

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

Functioni

Receptor for progesterone.By similarity

GO - Molecular functioni

  1. heme binding Source: GO_Central
  2. steroid binding Source: ProtInc

GO - Biological processi

  1. axon guidance Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Ligandi

Lipid-binding, Steroid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Membrane-associated progesterone receptor component 1
Short name:
mPR
Gene namesi
Name:PGRMC1
Synonyms:HPR6.6, PGRMC
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:16090. PGRMC1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 2423LumenalSequence AnalysisAdd
BLAST
Transmembranei25 – 4319HelicalSequence AnalysisAdd
BLAST
Topological domaini44 – 195152CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: HPA
  2. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  3. extracellular vesicular exosome Source: UniProtKB
  4. integral component of membrane Source: UniProtKB-KW
  5. membrane Source: UniProtKB
  6. nucleolus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33248.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 195194Membrane-associated progesterone receptor component 1PRO_0000121739Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei54 – 541Phosphoserine2 Publications
Modified residuei57 – 571Phosphoserine10 Publications
Modified residuei74 – 741Phosphothreonine1 Publication
Modified residuei181 – 1811Phosphoserine5 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO00264.
PaxDbiO00264.
PeptideAtlasiO00264.
PRIDEiO00264.

2D gel databases

OGPiO00264.

PTM databases

PhosphoSiteiO00264.

Expressioni

Tissue specificityi

Widely expressed, with highest expression in liver and kidney.

Gene expression databases

BgeeiO00264.
CleanExiHS_PGRMC1.
ExpressionAtlasiO00264. baseline and differential.
GenevestigatoriO00264.

Organism-specific databases

HPAiHPA002877.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
CYP2C2P001816EBI-1045534,EBI-4320576From a different organism.
PORP164355EBI-1045534,EBI-726554

Protein-protein interaction databases

BioGridi116068. 37 interactions.
IntActiO00264. 11 interactions.
MINTiMINT-2997519.
STRINGi9606.ENSP00000217971.

Structurei

3D structure databases

ProteinModelPortaliO00264.
SMRiO00264. Positions 72-171.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini72 – 171100Cytochrome b5 heme-bindingAdd
BLAST

Domaini

The cytochrome b5 heme-binding domain lacks the conserved iron-binding His residues at positions 107 and 131.By similarity

Sequence similaritiesi

Belongs to the cytochrome b5 family. MAPR subfamily.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG291734.
GeneTreeiENSGT00730000110959.
HOGENOMiHOG000187840.
HOVERGENiHBG059971.
InParanoidiO00264.
KOiK17278.
OMAiEHDDLSD.
OrthoDBiEOG7KWSKJ.
PhylomeDBiO00264.
TreeFamiTF314562.

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]
SUPFAMiSSF55856. SSF55856. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

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

Isoform 1 (identifier: O00264-1) [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
MAAEDVVATG ADPSDLESGG LLHEIFTSPL NLLLLGLCIF LLYKIVRGDQ
60 70 80 90 100
PAASGDSDDD EPPPLPRLKR RDFTPAELRR FDGVQDPRIL MAINGKVFDV
110 120 130 140 150
TKGRKFYGPE GPYGVFAGRD ASRGLATFCL DKEALKDEYD DLSDLTAAQQ
160 170 180 190
ETLSDWESQF TFKYHHVGKL LKEGEEPTVY SDEEEPKDES ARKND
Length:195
Mass (Da):21,671
Last modified:January 22, 2007 - v3
Checksum:iCCD5E802E1C9E604
GO
Isoform 2 (identifier: O00264-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     110-162: EGPYGVFAGRDASRGLATFCLDKEALKDEYDDLSDLTAAQQETLSDWESQFTF → V

Note: No experimental confirmation available.

Show »
Length:143
Mass (Da):15,879
Checksum:i51538E8883D9E1EC
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei110 – 16253EGPYG…SQFTF → V in isoform 2. 1 PublicationVSP_054710Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y12711 mRNA. Translation: CAA73248.1.
AK293618 mRNA. Translation: BAH11549.1.
AC004835 Genomic DNA. No translation available.
CH471161 Genomic DNA. Translation: EAW89881.1.
BC034238 mRNA. Translation: AAH34238.1.
AJ249131 Genomic DNA. Translation: CAB65109.1.
CCDSiCCDS14576.1. [O00264-1]
CCDS65313.1. [O00264-2]
RefSeqiNP_001269550.1. NM_001282621.1. [O00264-2]
NP_006658.1. NM_006667.4. [O00264-1]
UniGeneiHs.90061.

Genome annotation databases

EnsembliENST00000217971; ENSP00000217971; ENSG00000101856. [O00264-1]
ENST00000535419; ENSP00000442821; ENSG00000101856. [O00264-2]
GeneIDi10857.
KEGGihsa:10857.
UCSCiuc004erb.3. human. [O00264-1]
uc011mts.2. human.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y12711 mRNA. Translation: CAA73248.1.
AK293618 mRNA. Translation: BAH11549.1.
AC004835 Genomic DNA. No translation available.
CH471161 Genomic DNA. Translation: EAW89881.1.
BC034238 mRNA. Translation: AAH34238.1.
AJ249131 Genomic DNA. Translation: CAB65109.1.
CCDSiCCDS14576.1. [O00264-1]
CCDS65313.1. [O00264-2]
RefSeqiNP_001269550.1. NM_001282621.1. [O00264-2]
NP_006658.1. NM_006667.4. [O00264-1]
UniGeneiHs.90061.

3D structure databases

ProteinModelPortaliO00264.
SMRiO00264. Positions 72-171.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116068. 37 interactions.
IntActiO00264. 11 interactions.
MINTiMINT-2997519.
STRINGi9606.ENSP00000217971.

Chemistry

DrugBankiDB00514. Dextromethorphan.
DB00540. Nortriptyline.

PTM databases

PhosphoSiteiO00264.

2D gel databases

OGPiO00264.

Proteomic databases

MaxQBiO00264.
PaxDbiO00264.
PeptideAtlasiO00264.
PRIDEiO00264.

Protocols and materials databases

DNASUi10857.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000217971; ENSP00000217971; ENSG00000101856. [O00264-1]
ENST00000535419; ENSP00000442821; ENSG00000101856. [O00264-2]
GeneIDi10857.
KEGGihsa:10857.
UCSCiuc004erb.3. human. [O00264-1]
uc011mts.2. human.

Organism-specific databases

CTDi10857.
GeneCardsiGC0XP118370.
HGNCiHGNC:16090. PGRMC1.
HPAiHPA002877.
MIMi300435. gene.
neXtProtiNX_O00264.
PharmGKBiPA33248.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG291734.
GeneTreeiENSGT00730000110959.
HOGENOMiHOG000187840.
HOVERGENiHBG059971.
InParanoidiO00264.
KOiK17278.
OMAiEHDDLSD.
OrthoDBiEOG7KWSKJ.
PhylomeDBiO00264.
TreeFamiTF314562.

Miscellaneous databases

ChiTaRSiPGRMC1. human.
GeneWikiiPGRMC1.
GenomeRNAii10857.
NextBioi35478759.
PROiO00264.
SOURCEiSearch...

Gene expression databases

BgeeiO00264.
CleanExiHS_PGRMC1.
ExpressionAtlasiO00264. baseline and differential.
GenevestigatoriO00264.

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]
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(1997) [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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Cerebellum.
  3. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Ovary.
  6. "The human membrane progesterone receptor gene: genomic structure and promoter analysis."
    Bernauer S., Wehling M., Gerdes D., Falkenstein E.
    DNA Seq. 12:13-25(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-109 (ISOFORM 1).
  7. Bienvenut W.V., Waridel P., Quadroni M.
    Submitted (FEB-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 48-67; 81-88; 105-119; 124-132 AND 173-192, PHOSPHORYLATION AT SER-181, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryonic kidney.
  8. "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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "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(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Prostate cancer.
  10. "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(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "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(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: T-cell.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  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(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54 AND SER-57, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57 AND SER-181, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  19. "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(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57 AND SER-181, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "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(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57 AND SER-181, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "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(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54; SER-57; THR-74 AND SER-181, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiPGRC1_HUMAN
AccessioniPrimary (citable) accession number: O00264
Secondary accession number(s): B7Z1L3, Q9UGJ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2000
Last sequence update: January 22, 2007
Last modified: March 3, 2015
This is version 140 of the entry and version 3 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: 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

External Data

Dasty 3

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 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.