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Protein

Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1

Gene

RPN1

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

Functioni

Essential subunit of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains.

Catalytic activityi

Dolichyl diphosphooligosaccharide + [protein]-L-asparagine = dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine.

Pathwayi: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

ReactomeiR-HSA-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-HSA-446203. Asparagine N-linked glycosylation.
UniPathwayiUPA00378.

Names & Taxonomyi

Protein namesi
Recommended name:
Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1 (EC:2.4.99.18)
Alternative name(s):
Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 67 kDa subunit
Ribophorin I
Short name:
RPN-I
Ribophorin-1
Gene namesi
Name:RPN1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:10381. RPN1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini24 – 438415LumenalSequence analysisAdd
BLAST
Transmembranei439 – 45719HelicalSequence analysisAdd
BLAST
Topological domaini458 – 607150CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • endoplasmic reticulum membrane Source: Reactome
  • integral component of membrane Source: UniProtKB-KW
  • melanosome Source: UniProtKB-SubCell
  • membrane Source: UniProtKB
  • oligosaccharyltransferase complex Source: HGNC
  • rough endoplasmic reticulum Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Organism-specific databases

MalaCardsiRPN1.
Orphaneti402020. 'Acute myeloid leukemia with inv3(p21;q26.2) or t(3;3)(p21;q26.2)'.
PharmGKBiPA34777.

Polymorphism and mutation databases

BioMutaiRPN1.
DMDMi132559.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Add
BLAST
Chaini24 – 607584Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1PRO_0000022241Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei187 – 1871N6-acetyllysineCombined sources
Glycosylationi299 – 2991N-linked (GlcNAc...)1 Publication
Modified residuei538 – 5381N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Glycoprotein

Proteomic databases

EPDiP04843.
MaxQBiP04843.
PaxDbiP04843.
PRIDEiP04843.
TopDownProteomicsiP04843.

PTM databases

iPTMnetiP04843.
PhosphoSiteiP04843.
SwissPalmiP04843.

Expressioni

Tissue specificityi

Expressed in all tissues tested.1 Publication

Gene expression databases

BgeeiP04843.
CleanExiHS_RPN1.
ExpressionAtlasiP04843. baseline and differential.
GenevisibleiP04843. HS.

Organism-specific databases

HPAiCAB009748.
HPA026828.

Interactioni

Subunit structurei

Component of the oligosaccharyltransferase (OST) complex. OST seems to exist in different forms which contain at least RPN1, RPN2, OST48, DAD1, OSTC, KRTCAP2 and either STT3A or STT3B. OST can form stable complexes with the Sec61 complex or with both the Sec61 and TRAP complexes. Also identified as part of a complex which includes CANX, DERL1, DERL2, DDOST/OST48, RPN1, RPN2, SELK, VIMP, STT3A AND VCP. This contains known members of the OST complex and may be a form of this complex.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SGTAO437653EBI-355963,EBI-347996
UBQLN1Q9UMX03EBI-355963,EBI-741480
UBQLN1Q9UMX0-23EBI-355963,EBI-10173939

Protein-protein interaction databases

BioGridi112099. 143 interactions.
DIPiDIP-38152N.
IntActiP04843. 37 interactions.
MINTiMINT-1152447.
STRINGi9606.ENSP00000296255.

Structurei

3D structure databases

ProteinModelPortaliP04843.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the OST1 family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2291. Eukaryota.
ENOG410XQVZ. LUCA.
GeneTreeiENSGT00390000009630.
HOGENOMiHOG000247000.
HOVERGENiHBG012864.
InParanoidiP04843.
KOiK12666.
OMAiPYPTHIT.
OrthoDBiEOG7GFB53.
PhylomeDBiP04843.
TreeFamiTF312988.

Family and domain databases

InterProiIPR007676. Ribophorin_I.
[Graphical view]
PANTHERiPTHR21049. PTHR21049. 1 hit.
PfamiPF04597. Ribophorin_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P04843-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEAPAAGLFL LLLLGTWAPA PGSASSEAPP LINEDVKRTV DLSSHLAKVT
60 70 80 90 100
AEVVLAHLGG GSTSRATSFL LALEPELEAR LAHLGVQVKG EDEEENNLEV
110 120 130 140 150
RETKIKGKSG RFFTVKLPVA LDPGAKISVI VETVYTHVLH PYPTQITQSE
160 170 180 190 200
KQFVVFEGNH YFYSPYPTKT QTMRVKLASR NVESYTKLGN PTRSEDLLDY
210 220 230 240 250
GPFRDVPAYS QDTFKVHYEN NSPFLTITSM TRVIEVSHWG NIAVEENVDL
260 270 280 290 300
KHTGAVLKGP FSRYDYQRQP DSGISSIRSF KTILPAAAQD VYYRDEIGNV
310 320 330 340 350
STSHLLILDD SVEMEIRPRF PLFGGWKTHY IVGYNLPSYE YLYNLGDQYA
360 370 380 390 400
LKMRFVDHVF DEQVIDSLTV KIILPEGAKN IEIDSPYEIS RAPDELHYTY
410 420 430 440 450
LDTFGRPVIV AYKKNLVEQH IQDIVVHYTF NKVLMLQEPL LVVAAFYILF
460 470 480 490 500
FTVIIYVRLD FSITKDPAAE ARMKVACITE QVLTLVNKRI GLYRHFDETV
510 520 530 540 550
NRYKQSRDIS TLNSGKKSLE TEHKALTSEI ALLQSRLKTE GSDLCDRVSE
560 570 580 590 600
MQKLDAQVKE LVLKSAVEAE RLVAGKLKKD TYIENEKLIS GKRQELVTKI

DHILDAL
Length:607
Mass (Da):68,569
Last modified:August 13, 1987 - v1
Checksum:iA2351A9CFABAEB6C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00281 mRNA. Translation: CAA68392.1.
AK312369 mRNA. Translation: BAG35287.1.
CR749284 mRNA. Translation: CAH18139.1.
CH471052 Genomic DNA. Translation: EAW79306.1.
CH471052 Genomic DNA. Translation: EAW79307.1.
CH471052 Genomic DNA. Translation: EAW79308.1.
BC010839 mRNA. Translation: AAH10839.1.
CCDSiCCDS3051.1.
PIRiA26168.
RefSeqiNP_002941.1. NM_002950.3.
UniGeneiHs.518244.
Hs.603636.

Genome annotation databases

EnsembliENST00000296255; ENSP00000296255; ENSG00000163902.
GeneIDi6184.
KEGGihsa:6184.
UCSCiuc003ekr.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00281 mRNA. Translation: CAA68392.1.
AK312369 mRNA. Translation: BAG35287.1.
CR749284 mRNA. Translation: CAH18139.1.
CH471052 Genomic DNA. Translation: EAW79306.1.
CH471052 Genomic DNA. Translation: EAW79307.1.
CH471052 Genomic DNA. Translation: EAW79308.1.
BC010839 mRNA. Translation: AAH10839.1.
CCDSiCCDS3051.1.
PIRiA26168.
RefSeqiNP_002941.1. NM_002950.3.
UniGeneiHs.518244.
Hs.603636.

3D structure databases

ProteinModelPortaliP04843.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112099. 143 interactions.
DIPiDIP-38152N.
IntActiP04843. 37 interactions.
MINTiMINT-1152447.
STRINGi9606.ENSP00000296255.

PTM databases

iPTMnetiP04843.
PhosphoSiteiP04843.
SwissPalmiP04843.

Polymorphism and mutation databases

BioMutaiRPN1.
DMDMi132559.

Proteomic databases

EPDiP04843.
MaxQBiP04843.
PaxDbiP04843.
PRIDEiP04843.
TopDownProteomicsiP04843.

Protocols and materials databases

DNASUi6184.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000296255; ENSP00000296255; ENSG00000163902.
GeneIDi6184.
KEGGihsa:6184.
UCSCiuc003ekr.2. human.

Organism-specific databases

CTDi6184.
GeneCardsiRPN1.
HGNCiHGNC:10381. RPN1.
HPAiCAB009748.
HPA026828.
MalaCardsiRPN1.
MIMi180470. gene.
neXtProtiNX_P04843.
Orphaneti402020. 'Acute myeloid leukemia with inv3(p21;q26.2) or t(3;3)(p21;q26.2)'.
PharmGKBiPA34777.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2291. Eukaryota.
ENOG410XQVZ. LUCA.
GeneTreeiENSGT00390000009630.
HOGENOMiHOG000247000.
HOVERGENiHBG012864.
InParanoidiP04843.
KOiK12666.
OMAiPYPTHIT.
OrthoDBiEOG7GFB53.
PhylomeDBiP04843.
TreeFamiTF312988.

Enzyme and pathway databases

UniPathwayiUPA00378.
ReactomeiR-HSA-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-HSA-446203. Asparagine N-linked glycosylation.

Miscellaneous databases

ChiTaRSiRPN1. human.
GeneWikiiRPN1.
GenomeRNAii6184.
NextBioi24017.
PROiP04843.
SOURCEiSearch...

Gene expression databases

BgeeiP04843.
CleanExiHS_RPN1.
ExpressionAtlasiP04843. baseline and differential.
GenevisibleiP04843. HS.

Family and domain databases

InterProiIPR007676. Ribophorin_I.
[Graphical view]
PANTHERiPTHR21049. PTHR21049. 1 hit.
PfamiPF04597. Ribophorin_I. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Human ribophorins I and II: the primary structure and membrane topology of two highly conserved rough endoplasmic reticulum-specific glycoproteins."
    Crimaudo C., Hortsch M., Gausepohl H., Meyer D.I.
    EMBO J. 6:75-82(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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].
    Tissue: Amygdala.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Uterine endothelium.
  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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Cervix.
  6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Melanoma.
  7. "Oligosaccharyltransferase isoforms that contain different catalytic STT3 subunits have distinct enzymatic properties."
    Kelleher D.J., Karaoglu D., Mandon E.C., Gilmore R.
    Mol. Cell 12:101-111(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE OLIGOSACCHARYLTRANSFERASE (OST) COMPLEX, TISSUE SPECIFICITY.
  8. "Proteomic analysis of mammalian oligosaccharyltransferase reveals multiple subcomplexes that contain Sec61, TRAP, and two potential new subunits."
    Shibatani T., David L.L., McCormack A.L., Frueh K., Skach W.R.
    Biochemistry 44:5982-5992(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE OLIGOSACCHARYLTRANSFERASE (OST) COMPLEX.
  9. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Melanoma.
  10. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-299.
    Tissue: Liver.
  11. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-187, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Selenoprotein K binds multiprotein complexes and is involved in the regulation of endoplasmic reticulum homeostasis."
    Shchedrina V.A., Everley R.A., Zhang Y., Gygi S.P., Hatfield D.L., Gladyshev V.N.
    J. Biol. Chem. 286:42937-42948(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH CANX; DERL1; DERL2; DDOST; RPN2; SELK; STT3A; VCP AND VIMP.
  14. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRPN1_HUMAN
AccessioniPrimary (citable) accession number: P04843
Secondary accession number(s): B2R5Z0, D3DNB6, Q68DT1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: May 11, 2016
This is version 159 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 3
    Human chromosome 3: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. 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.