Full text data of RPN1
RPN1
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1; 2.4.99.18 (Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 67 kDa subunit; Ribophorin I; RPN-I; Ribophorin-1; Flags: Precursor)
Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1; 2.4.99.18 (Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 67 kDa subunit; Ribophorin I; RPN-I; Ribophorin-1; Flags: Precursor)
UniProt
P04843
ID RPN1_HUMAN Reviewed; 607 AA.
AC P04843; B2R5Z0; D3DNB6; Q68DT1;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
read moreDT 13-AUG-1987, sequence version 1.
DT 22-JAN-2014, entry version 134.
DE RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1;
DE EC=2.4.99.18;
DE AltName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 67 kDa subunit;
DE AltName: Full=Ribophorin I;
DE Short=RPN-I;
DE AltName: Full=Ribophorin-1;
DE Flags: Precursor;
GN Name=RPN1;
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].
RX PubMed=3034581;
RA Crimaudo C., Hortsch M., Gausepohl H., Meyer D.I.;
RT "Human ribophorins I and II: the primary structure and membrane
RT topology of two highly conserved rough endoplasmic reticulum-specific
RT glycoproteins.";
RL EMBO J. 6:75-82(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Amygdala;
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 [LARGE SCALE MRNA].
RC TISSUE=Uterine endothelium;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cervix;
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 [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RC TISSUE=Melanoma;
RX PubMed=12643545; DOI=10.1021/pr025562r;
RA Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K.,
RA Valencia J., Muller J., Vieira W.D., Watabe H., Shabanowitz J.,
RA Hearing V.J., Hunt D.F., Appella E.;
RT "Proteomic analysis of early melanosomes: identification of novel
RT melanosomal proteins.";
RL J. Proteome Res. 2:69-79(2003).
RN [7]
RP IDENTIFICATION IN THE OLIGOSACCHARYLTRANSFERASE (OST) COMPLEX, AND
RP TISSUE SPECIFICITY.
RX PubMed=12887896; DOI=10.1016/S1097-2765(03)00243-0;
RA Kelleher D.J., Karaoglu D., Mandon E.C., Gilmore R.;
RT "Oligosaccharyltransferase isoforms that contain different catalytic
RT STT3 subunits have distinct enzymatic properties.";
RL Mol. Cell 12:101-111(2003).
RN [8]
RP IDENTIFICATION IN THE OLIGOSACCHARYLTRANSFERASE (OST) COMPLEX.
RX PubMed=15835887; DOI=10.1021/bi047328f;
RA Shibatani T., David L.L., McCormack A.L., Frueh K., Skach W.R.;
RT "Proteomic analysis of mammalian oligosaccharyltransferase reveals
RT multiple subcomplexes that contain Sec61, TRAP, and two potential new
RT subunits.";
RL Biochemistry 44:5982-5992(2005).
RN [9]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
RA Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
RA Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
RA Hunt D.F.;
RT "Proteomic and bioinformatic characterization of the biogenesis and
RT function of melanosomes.";
RL J. Proteome Res. 5:3135-3144(2006).
RN [10]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-299, AND MASS
RP SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of
RT multiple enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-187, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [12]
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).
CC -!- FUNCTION: Essential subunit of the N-oligosaccharyl transferase
CC (OST) complex which catalyzes the transfer of a high mannose
CC oligosaccharide from a lipid-linked oligosaccharide donor to an
CC asparagine residue within an Asn-X-Ser/Thr consensus motif in
CC nascent polypeptide chains.
CC -!- CATALYTIC ACTIVITY: Dolichyl diphosphooligosaccharide + [protein]-
CC L-asparagine = dolichyl diphosphate + a glycoprotein with the
CC oligosaccharide chain attached by N-beta-D-glycosyl linkage to a
CC protein L-asparagine.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex.
CC OST seems to exist in different forms which contain at least RPN1,
CC RPN2, OST48, DAD1, OSTC, KRTCAP2 and either STT3A or STT3B. OST
CC can form stable complexes with the Sec61 complex or with both the
CC Sec61 and TRAP complexes.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC type I membrane protein. Melanosome. Note=Identified by mass
CC spectrometry in melanosome fractions from stage I to stage IV.
CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested.
CC -!- SIMILARITY: Belongs to the OST1 family.
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DR EMBL; Y00281; CAA68392.1; -; mRNA.
DR EMBL; AK312369; BAG35287.1; -; mRNA.
DR EMBL; CR749284; CAH18139.1; -; mRNA.
DR EMBL; CH471052; EAW79306.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79307.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79308.1; -; Genomic_DNA.
DR EMBL; BC010839; AAH10839.1; -; mRNA.
DR PIR; A26168; A26168.
DR RefSeq; NP_002941.1; NM_002950.3.
DR UniGene; Hs.518244; -.
DR UniGene; Hs.603636; -.
DR ProteinModelPortal; P04843; -.
DR IntAct; P04843; 20.
DR MINT; MINT-1152447; -.
DR STRING; 9606.ENSP00000296255; -.
DR PhosphoSite; P04843; -.
DR DMDM; 132559; -.
DR PaxDb; P04843; -.
DR PRIDE; P04843; -.
DR DNASU; 6184; -.
DR Ensembl; ENST00000296255; ENSP00000296255; ENSG00000163902.
DR GeneID; 6184; -.
DR KEGG; hsa:6184; -.
DR UCSC; uc003ekr.1; human.
DR CTD; 6184; -.
DR GeneCards; GC03M128338; -.
DR HGNC; HGNC:10381; RPN1.
DR HPA; CAB009748; -.
DR HPA; HPA026828; -.
DR MIM; 180470; gene.
DR neXtProt; NX_P04843; -.
DR PharmGKB; PA34777; -.
DR eggNOG; NOG292474; -.
DR HOGENOM; HOG000247000; -.
DR HOVERGEN; HBG012864; -.
DR InParanoid; P04843; -.
DR KO; K12666; -.
DR OMA; TFKVHYE; -.
DR OrthoDB; EOG7GFB53; -.
DR PhylomeDB; P04843; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_71; Gene Expression.
DR UniPathway; UPA00378; -.
DR ChiTaRS; RPN1; human.
DR GeneWiki; RPN1; -.
DR GenomeRNAi; 6184; -.
DR NextBio; 24017; -.
DR PRO; PR:P04843; -.
DR ArrayExpress; P04843; -.
DR Bgee; P04843; -.
DR CleanEx; HS_RPN1; -.
DR Genevestigator; P04843; -.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0008250; C:oligosaccharyltransferase complex; TAS:HGNC.
DR GO; GO:0005791; C:rough endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0004579; F:dolichyl-diphosphooligosaccharide-protein glycotransferase activity; IEA:InterPro.
DR GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; TAS:HGNC.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; TAS:Reactome.
DR GO; GO:0006412; P:translation; TAS:Reactome.
DR InterPro; IPR007676; Ribophorin_I.
DR PANTHER; PTHR21049; PTHR21049; 1.
DR Pfam; PF04597; Ribophorin_I; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Endoplasmic reticulum; Glycoprotein;
KW Glycosyltransferase; Membrane; Reference proteome; Signal;
KW Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1 23
FT CHAIN 24 607 Dolichyl-diphosphooligosaccharide--
FT protein glycosyltransferase subunit 1.
FT /FTId=PRO_0000022241.
FT TOPO_DOM 24 438 Lumenal (Potential).
FT TRANSMEM 439 457 Helical; (Potential).
FT TOPO_DOM 458 607 Cytoplasmic (Potential).
FT MOD_RES 187 187 N6-acetyllysine.
FT CARBOHYD 299 299 N-linked (GlcNAc...).
SQ SEQUENCE 607 AA; 68569 MW; A2351A9CFABAEB6C CRC64;
MEAPAAGLFL LLLLGTWAPA PGSASSEAPP LINEDVKRTV DLSSHLAKVT AEVVLAHLGG
GSTSRATSFL LALEPELEAR LAHLGVQVKG EDEEENNLEV RETKIKGKSG RFFTVKLPVA
LDPGAKISVI VETVYTHVLH PYPTQITQSE KQFVVFEGNH YFYSPYPTKT QTMRVKLASR
NVESYTKLGN PTRSEDLLDY GPFRDVPAYS QDTFKVHYEN NSPFLTITSM TRVIEVSHWG
NIAVEENVDL KHTGAVLKGP FSRYDYQRQP DSGISSIRSF KTILPAAAQD VYYRDEIGNV
STSHLLILDD SVEMEIRPRF PLFGGWKTHY IVGYNLPSYE YLYNLGDQYA LKMRFVDHVF
DEQVIDSLTV KIILPEGAKN IEIDSPYEIS RAPDELHYTY LDTFGRPVIV AYKKNLVEQH
IQDIVVHYTF NKVLMLQEPL LVVAAFYILF FTVIIYVRLD FSITKDPAAE ARMKVACITE
QVLTLVNKRI GLYRHFDETV NRYKQSRDIS TLNSGKKSLE TEHKALTSEI ALLQSRLKTE
GSDLCDRVSE MQKLDAQVKE LVLKSAVEAE RLVAGKLKKD TYIENEKLIS GKRQELVTKI
DHILDAL
//
ID RPN1_HUMAN Reviewed; 607 AA.
AC P04843; B2R5Z0; D3DNB6; Q68DT1;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
read moreDT 13-AUG-1987, sequence version 1.
DT 22-JAN-2014, entry version 134.
DE RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1;
DE EC=2.4.99.18;
DE AltName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 67 kDa subunit;
DE AltName: Full=Ribophorin I;
DE Short=RPN-I;
DE AltName: Full=Ribophorin-1;
DE Flags: Precursor;
GN Name=RPN1;
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].
RX PubMed=3034581;
RA Crimaudo C., Hortsch M., Gausepohl H., Meyer D.I.;
RT "Human ribophorins I and II: the primary structure and membrane
RT topology of two highly conserved rough endoplasmic reticulum-specific
RT glycoproteins.";
RL EMBO J. 6:75-82(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Amygdala;
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 [LARGE SCALE MRNA].
RC TISSUE=Uterine endothelium;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cervix;
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 [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RC TISSUE=Melanoma;
RX PubMed=12643545; DOI=10.1021/pr025562r;
RA Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K.,
RA Valencia J., Muller J., Vieira W.D., Watabe H., Shabanowitz J.,
RA Hearing V.J., Hunt D.F., Appella E.;
RT "Proteomic analysis of early melanosomes: identification of novel
RT melanosomal proteins.";
RL J. Proteome Res. 2:69-79(2003).
RN [7]
RP IDENTIFICATION IN THE OLIGOSACCHARYLTRANSFERASE (OST) COMPLEX, AND
RP TISSUE SPECIFICITY.
RX PubMed=12887896; DOI=10.1016/S1097-2765(03)00243-0;
RA Kelleher D.J., Karaoglu D., Mandon E.C., Gilmore R.;
RT "Oligosaccharyltransferase isoforms that contain different catalytic
RT STT3 subunits have distinct enzymatic properties.";
RL Mol. Cell 12:101-111(2003).
RN [8]
RP IDENTIFICATION IN THE OLIGOSACCHARYLTRANSFERASE (OST) COMPLEX.
RX PubMed=15835887; DOI=10.1021/bi047328f;
RA Shibatani T., David L.L., McCormack A.L., Frueh K., Skach W.R.;
RT "Proteomic analysis of mammalian oligosaccharyltransferase reveals
RT multiple subcomplexes that contain Sec61, TRAP, and two potential new
RT subunits.";
RL Biochemistry 44:5982-5992(2005).
RN [9]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
RA Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
RA Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
RA Hunt D.F.;
RT "Proteomic and bioinformatic characterization of the biogenesis and
RT function of melanosomes.";
RL J. Proteome Res. 5:3135-3144(2006).
RN [10]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-299, AND MASS
RP SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of
RT multiple enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-187, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [12]
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).
CC -!- FUNCTION: Essential subunit of the N-oligosaccharyl transferase
CC (OST) complex which catalyzes the transfer of a high mannose
CC oligosaccharide from a lipid-linked oligosaccharide donor to an
CC asparagine residue within an Asn-X-Ser/Thr consensus motif in
CC nascent polypeptide chains.
CC -!- CATALYTIC ACTIVITY: Dolichyl diphosphooligosaccharide + [protein]-
CC L-asparagine = dolichyl diphosphate + a glycoprotein with the
CC oligosaccharide chain attached by N-beta-D-glycosyl linkage to a
CC protein L-asparagine.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex.
CC OST seems to exist in different forms which contain at least RPN1,
CC RPN2, OST48, DAD1, OSTC, KRTCAP2 and either STT3A or STT3B. OST
CC can form stable complexes with the Sec61 complex or with both the
CC Sec61 and TRAP complexes.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC type I membrane protein. Melanosome. Note=Identified by mass
CC spectrometry in melanosome fractions from stage I to stage IV.
CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested.
CC -!- SIMILARITY: Belongs to the OST1 family.
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DR EMBL; Y00281; CAA68392.1; -; mRNA.
DR EMBL; AK312369; BAG35287.1; -; mRNA.
DR EMBL; CR749284; CAH18139.1; -; mRNA.
DR EMBL; CH471052; EAW79306.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79307.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79308.1; -; Genomic_DNA.
DR EMBL; BC010839; AAH10839.1; -; mRNA.
DR PIR; A26168; A26168.
DR RefSeq; NP_002941.1; NM_002950.3.
DR UniGene; Hs.518244; -.
DR UniGene; Hs.603636; -.
DR ProteinModelPortal; P04843; -.
DR IntAct; P04843; 20.
DR MINT; MINT-1152447; -.
DR STRING; 9606.ENSP00000296255; -.
DR PhosphoSite; P04843; -.
DR DMDM; 132559; -.
DR PaxDb; P04843; -.
DR PRIDE; P04843; -.
DR DNASU; 6184; -.
DR Ensembl; ENST00000296255; ENSP00000296255; ENSG00000163902.
DR GeneID; 6184; -.
DR KEGG; hsa:6184; -.
DR UCSC; uc003ekr.1; human.
DR CTD; 6184; -.
DR GeneCards; GC03M128338; -.
DR HGNC; HGNC:10381; RPN1.
DR HPA; CAB009748; -.
DR HPA; HPA026828; -.
DR MIM; 180470; gene.
DR neXtProt; NX_P04843; -.
DR PharmGKB; PA34777; -.
DR eggNOG; NOG292474; -.
DR HOGENOM; HOG000247000; -.
DR HOVERGEN; HBG012864; -.
DR InParanoid; P04843; -.
DR KO; K12666; -.
DR OMA; TFKVHYE; -.
DR OrthoDB; EOG7GFB53; -.
DR PhylomeDB; P04843; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_71; Gene Expression.
DR UniPathway; UPA00378; -.
DR ChiTaRS; RPN1; human.
DR GeneWiki; RPN1; -.
DR GenomeRNAi; 6184; -.
DR NextBio; 24017; -.
DR PRO; PR:P04843; -.
DR ArrayExpress; P04843; -.
DR Bgee; P04843; -.
DR CleanEx; HS_RPN1; -.
DR Genevestigator; P04843; -.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0008250; C:oligosaccharyltransferase complex; TAS:HGNC.
DR GO; GO:0005791; C:rough endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0004579; F:dolichyl-diphosphooligosaccharide-protein glycotransferase activity; IEA:InterPro.
DR GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; TAS:HGNC.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; TAS:Reactome.
DR GO; GO:0006412; P:translation; TAS:Reactome.
DR InterPro; IPR007676; Ribophorin_I.
DR PANTHER; PTHR21049; PTHR21049; 1.
DR Pfam; PF04597; Ribophorin_I; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Endoplasmic reticulum; Glycoprotein;
KW Glycosyltransferase; Membrane; Reference proteome; Signal;
KW Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1 23
FT CHAIN 24 607 Dolichyl-diphosphooligosaccharide--
FT protein glycosyltransferase subunit 1.
FT /FTId=PRO_0000022241.
FT TOPO_DOM 24 438 Lumenal (Potential).
FT TRANSMEM 439 457 Helical; (Potential).
FT TOPO_DOM 458 607 Cytoplasmic (Potential).
FT MOD_RES 187 187 N6-acetyllysine.
FT CARBOHYD 299 299 N-linked (GlcNAc...).
SQ SEQUENCE 607 AA; 68569 MW; A2351A9CFABAEB6C CRC64;
MEAPAAGLFL LLLLGTWAPA PGSASSEAPP LINEDVKRTV DLSSHLAKVT AEVVLAHLGG
GSTSRATSFL LALEPELEAR LAHLGVQVKG EDEEENNLEV RETKIKGKSG RFFTVKLPVA
LDPGAKISVI VETVYTHVLH PYPTQITQSE KQFVVFEGNH YFYSPYPTKT QTMRVKLASR
NVESYTKLGN PTRSEDLLDY GPFRDVPAYS QDTFKVHYEN NSPFLTITSM TRVIEVSHWG
NIAVEENVDL KHTGAVLKGP FSRYDYQRQP DSGISSIRSF KTILPAAAQD VYYRDEIGNV
STSHLLILDD SVEMEIRPRF PLFGGWKTHY IVGYNLPSYE YLYNLGDQYA LKMRFVDHVF
DEQVIDSLTV KIILPEGAKN IEIDSPYEIS RAPDELHYTY LDTFGRPVIV AYKKNLVEQH
IQDIVVHYTF NKVLMLQEPL LVVAAFYILF FTVIIYVRLD FSITKDPAAE ARMKVACITE
QVLTLVNKRI GLYRHFDETV NRYKQSRDIS TLNSGKKSLE TEHKALTSEI ALLQSRLKTE
GSDLCDRVSE MQKLDAQVKE LVLKSAVEAE RLVAGKLKKD TYIENEKLIS GKRQELVTKI
DHILDAL
//
MIM
180470
*RECORD*
*FIELD* NO
180470
*FIELD* TI
*180470 RIBOPHORIN I; RPN1
*FIELD* TX
DESCRIPTION
Ribophorins I and II (180490) represent proteins that appear to be
read moreinvolved in ribosome binding. They are abundant, highly conserved
glycoproteins located exclusively in the membranes of the rough
endoplasmic reticulum.
CLONING
Using probes derived from a human liver expression library, Crimaudo et
al. (1987) isolated and sequenced full-length human cDNA clones encoding
ribophorins I and II. The cDNA clones hybridize to mRNA species of 2.5
kb and encode polypeptides of 68.5 and 69.3 kD, respectively. Sequence
comparisons and immunoblotting with specific antibodies showed both
proteins to be highly conserved throughout a variety of species.
However, no relationship between the 2 proteins could be deduced from
their primary sequences.
GENE FUNCTION
Kelleher et al. (1992) reported that mammalian oligosaccharyltransferase
activity is associated with a protein complex composed of ribophorin I,
ribophorin II, and a 48-kD oligosaccharyltransferase protein (602202).
Rpn1 is a component of the proteasome base. Using in vitro binding
assays with purified yeast proteasomes, Elsasser et al. (2002) found
that the ubiquitin-like (UBL) domain of recombinant Rad23 (see 600061)
interacted with proteasomes through the leucine-rich repeat domain of
Rpn1. Yeast Dsk2 (see 300264) also contains a UBL domain, and it
competed with Rad23 for proteasome binding.
MAPPING
Using cDNA clones, Barton et al. (1987) mapped the RPN1 gene to
chromosome 3 in somatic cell hybrids.
*FIELD* RF
1. Barton, D. E.; Crimaudo, C.; Hortsch, M.; Francke, U.: The genes
for ribophorins I and II are on human chromosomes 3q and 20 and mouse
chromosomes 6 and 12, respectively. (Abstract) Cytogenet. Cell Genet. 46:
577 only, 1987.
2. Crimaudo, C.; Hortsch, M.; Gausepohl, H.; Meyer, D. I.: Human
ribophorins I and II: the primary structure and membrane topology
of two highly conserved round endoplasmic reticulum-specific glycoproteins. EMBO
J. 6: 75-82, 1987.
3. Elsasser, S.; Gali, R. R.; Schwickart, M.; Larsen, C. N.; Leggett,
D. S.; Muller, B.; Feng, M. T.; Tubing, F.; Dittmar, G. A. G.; Finley,
D.: Proteasome subunit Rpn1 binds ubiquitin-like protein domains. Nature
Cell Biol. 4: 725-730, 2002.
4. Kelleher, D. J.; Kreibich, G.; Gilmore, R.: Oligosaccharyltransferase
activity is associated with a protein complex composed of ribophorins
I and II and a 48 kd protein. Cell 69: 55-65, 1992.
*FIELD* CN
Patricia A. Hartz - updated: 10/28/2002
Jennifer P. Macke - updated: 4/15/1998
*FIELD* CD
Victor A. McKusick: 3/26/1987
*FIELD* ED
mgross: 10/28/2002
dholmes: 5/8/1998
dholmes: 4/15/1998
dholmes: 4/7/1998
supermim: 3/16/1992
supermim: 3/20/1990
ddp: 10/27/1989
root: 6/20/1988
marie: 3/25/1988
carol: 9/1/1987
*RECORD*
*FIELD* NO
180470
*FIELD* TI
*180470 RIBOPHORIN I; RPN1
*FIELD* TX
DESCRIPTION
Ribophorins I and II (180490) represent proteins that appear to be
read moreinvolved in ribosome binding. They are abundant, highly conserved
glycoproteins located exclusively in the membranes of the rough
endoplasmic reticulum.
CLONING
Using probes derived from a human liver expression library, Crimaudo et
al. (1987) isolated and sequenced full-length human cDNA clones encoding
ribophorins I and II. The cDNA clones hybridize to mRNA species of 2.5
kb and encode polypeptides of 68.5 and 69.3 kD, respectively. Sequence
comparisons and immunoblotting with specific antibodies showed both
proteins to be highly conserved throughout a variety of species.
However, no relationship between the 2 proteins could be deduced from
their primary sequences.
GENE FUNCTION
Kelleher et al. (1992) reported that mammalian oligosaccharyltransferase
activity is associated with a protein complex composed of ribophorin I,
ribophorin II, and a 48-kD oligosaccharyltransferase protein (602202).
Rpn1 is a component of the proteasome base. Using in vitro binding
assays with purified yeast proteasomes, Elsasser et al. (2002) found
that the ubiquitin-like (UBL) domain of recombinant Rad23 (see 600061)
interacted with proteasomes through the leucine-rich repeat domain of
Rpn1. Yeast Dsk2 (see 300264) also contains a UBL domain, and it
competed with Rad23 for proteasome binding.
MAPPING
Using cDNA clones, Barton et al. (1987) mapped the RPN1 gene to
chromosome 3 in somatic cell hybrids.
*FIELD* RF
1. Barton, D. E.; Crimaudo, C.; Hortsch, M.; Francke, U.: The genes
for ribophorins I and II are on human chromosomes 3q and 20 and mouse
chromosomes 6 and 12, respectively. (Abstract) Cytogenet. Cell Genet. 46:
577 only, 1987.
2. Crimaudo, C.; Hortsch, M.; Gausepohl, H.; Meyer, D. I.: Human
ribophorins I and II: the primary structure and membrane topology
of two highly conserved round endoplasmic reticulum-specific glycoproteins. EMBO
J. 6: 75-82, 1987.
3. Elsasser, S.; Gali, R. R.; Schwickart, M.; Larsen, C. N.; Leggett,
D. S.; Muller, B.; Feng, M. T.; Tubing, F.; Dittmar, G. A. G.; Finley,
D.: Proteasome subunit Rpn1 binds ubiquitin-like protein domains. Nature
Cell Biol. 4: 725-730, 2002.
4. Kelleher, D. J.; Kreibich, G.; Gilmore, R.: Oligosaccharyltransferase
activity is associated with a protein complex composed of ribophorins
I and II and a 48 kd protein. Cell 69: 55-65, 1992.
*FIELD* CN
Patricia A. Hartz - updated: 10/28/2002
Jennifer P. Macke - updated: 4/15/1998
*FIELD* CD
Victor A. McKusick: 3/26/1987
*FIELD* ED
mgross: 10/28/2002
dholmes: 5/8/1998
dholmes: 4/15/1998
dholmes: 4/7/1998
supermim: 3/16/1992
supermim: 3/20/1990
ddp: 10/27/1989
root: 6/20/1988
marie: 3/25/1988
carol: 9/1/1987