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P04844

- RPN2_HUMAN

UniProt

P04844 - RPN2_HUMAN

Protein

Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2

Gene

RPN2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 3 (01 Dec 2000)
      Previous versions | rss
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    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

    GO - Molecular functioni

    1. ribosome binding Source: Ensembl
    2. transferase activity, transferring glycosyl groups Source: UniProtKB-KW

    GO - Biological processi

    1. aging Source: Ensembl
    2. cellular protein metabolic process Source: Reactome
    3. cellular protein modification process Source: ProtInc
    4. gene expression Source: Reactome
    5. post-translational protein modification Source: Reactome
    6. protein N-linked glycosylation via asparagine Source: HGNC
    7. response to drug Source: Ensembl
    8. SRP-dependent cotranslational protein targeting to membrane Source: Reactome
    9. translation Source: Reactome

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Enzyme and pathway databases

    ReactomeiREACT_115902. SRP-dependent cotranslational protein targeting to membrane.
    REACT_22426. Asparagine N-linked glycosylation.
    UniPathwayiUPA00378.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2 (EC:2.4.99.18)
    Alternative name(s):
    Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 63 kDa subunit
    RIBIIR
    Ribophorin II
    Short name:
    RPN-II
    Ribophorin-2
    Gene namesi
    Name:RPN2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:10382. RPN2.

    Subcellular locationi

    GO - Cellular componenti

    1. autophagic vacuole membrane Source: Ensembl
    2. endoplasmic reticulum Source: HPA
    3. endoplasmic reticulum membrane Source: Reactome
    4. integral component of membrane Source: UniProtKB-KW
    5. membrane Source: UniProtKB
    6. nucleus Source: HPA
    7. oligosaccharyltransferase complex Source: HGNC
    8. rough endoplasmic reticulum Source: Ensembl

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34778.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 22221 PublicationAdd
    BLAST
    Chaini23 – 631609Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2PRO_0000022244Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi106 – 1061N-linked (GlcNAc...)1 Publication
    Cross-linki154 – 154Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)

    Keywords - PTMi

    Glycoprotein, Isopeptide bond, Ubl conjugation

    Proteomic databases

    MaxQBiP04844.
    PaxDbiP04844.
    PRIDEiP04844.

    PTM databases

    PhosphoSiteiP04844.

    Expressioni

    Tissue specificityi

    Expressed in all tissues tested.

    Gene expression databases

    ArrayExpressiP04844.
    BgeeiP04844.
    CleanExiHS_RPN2.
    GenevestigatoriP04844.

    Organism-specific databases

    HPAiCAB019277.
    HPA008297.
    HPA025922.

    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

    Protein-protein interaction databases

    BioGridi112100. 37 interactions.
    IntActiP04844. 15 interactions.
    MINTiMINT-8247596.
    STRINGi9606.ENSP00000237530.

    Structurei

    3D structure databases

    ProteinModelPortaliP04844.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini23 – 540518LumenalSequence AnalysisAdd
    BLAST
    Topological domaini562 – 57110CytoplasmicSequence Analysis
    Topological domaini593 – 5964LumenalSequence Analysis
    Topological domaini618 – 63114CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei541 – 56121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei572 – 59221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei597 – 61721HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the SWP1 family.Curated

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG258688.
    HOGENOMiHOG000231261.
    HOVERGENiHBG002365.
    InParanoidiP04844.
    KOiK12667.
    OMAiPTHYLTK.
    OrthoDBiEOG78SQHS.
    PhylomeDBiP04844.
    TreeFamiTF106146.

    Family and domain databases

    InterProiIPR008814. Swp1.
    [Graphical view]
    PANTHERiPTHR12640:SF0. PTHR12640:SF0. 1 hit.
    PfamiPF05817. Ribophorin_II. 1 hit.
    [Graphical view]

    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. Align

    Isoform 1 (identifier: P04844-1) [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

    MAPPGSSTVF LLALTIIAST WALTPTHYLT KHDVERLKAS LDRPFTNLES    50
    AFYSIVGLSS LGAQVPDAKK ACTYIRSNLD PSNVDSLFYA AQASQALSGC 100
    EISISNETKD LLLAAVSEDS SVTQIYHAVA ALSGFGLPLA SQEALSALTA 150
    RLSKEETVLA TVQALQTASH LSQQADLRSI VEEIEDLVAR LDELGGVYLQ 200
    FEEGLETTAL FVAATYKLMD HVGTEPSIKE DQVIQLMNAI FSKKNFESLS 250
    EAFSVASAAA VLSHNRYHVP VVVVPEGSAS DTHEQAILRL QVTNVLSQPL 300
    TQATVKLEHA KSVASRATVL QKTSFTPVGD VFELNFMNVK FSSGYYDFLV 350
    EVEGDNRYIA NTVELRVKIS TEVGITNVDL STVDKDQSIA PKTTRVTYPA 400
    KAKGTFIADS HQNFALFFQL VDVNTGAELT PHQTFVRLHN QKTGQEVVFV 450
    AEPDNKNVYK FELDTSERKI EFDSASGTYT LYLIIGDATL KNPILWNVAD 500
    VVIKFPEEEA PSTVLSQNLF TPKQEIQHLF REPEKRPPTV VSNTFTALIL 550
    SPLLLLFALW IRIGANVSNF TFAPSTIIFH LGHAAMLGLM YVYWTQLNMF 600
    QTLKYLAILG SVTFLAGNRM LAQQAVKRTA H 631
    Length:631
    Mass (Da):69,284
    Last modified:December 1, 2000 - v3
    Checksum:iE24D7B3565141676
    GO
    Isoform 2 (identifier: P04844-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         70-101: Missing.
         627-627: K → KRIAAEQSSRLAKYRTL

    Note: No experimental confirmation available.

    Show »
    Length:615
    Mass (Da):67,723
    Checksum:iFC967C1FA17A011E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti197 – 1971V → L in CAA68393. (PubMed:3034581)Curated
    Sequence conflicti201 – 2011F → C in CAA68393. (PubMed:3034581)Curated
    Sequence conflicti260 – 2601A → S in CAA68393. (PubMed:3034581)Curated
    Sequence conflicti286 – 2861A → S in CAG33180. 1 PublicationCurated
    Sequence conflicti423 – 4231V → M in CAA68393. (PubMed:3034581)Curated
    Sequence conflicti427 – 4271A → V in CAG33180. 1 PublicationCurated
    Sequence conflicti571 – 5711T → I in AAH13028. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti597 – 5971L → F.
    Corresponds to variant rs34951322 [ dbSNP | Ensembl ].
    VAR_054040

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei70 – 10132Missing in isoform 2. 1 PublicationVSP_043051Add
    BLAST
    Alternative sequencei627 – 6271K → KRIAAEQSSRLAKYRTL in isoform 2. 1 PublicationVSP_043052

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y00282 mRNA. Translation: CAA68393.1.
    AJ237734
    , AJ237735, AJ237733, AJ237736, AJ237737, AJ237738, AJ237739, AJ237740, AJ237741, AJ237742, AJ237743, AJ237744, AJ237745, AJ237746, AJ237747, AJ237748, AJ237749 Genomic DNA. Translation: CAB54801.1.
    AK096243 mRNA. Translation: BAG53237.1.
    CR456899 mRNA. Translation: CAG33180.1.
    AL031659 Genomic DNA. Translation: CAB41763.1.
    AL031659 Genomic DNA. Translation: CAI42668.1.
    CH471077 Genomic DNA. Translation: EAW76073.1.
    BC002380 mRNA. Translation: AAH02380.2.
    BC003560 mRNA. Translation: AAH03560.1.
    BC013028 mRNA. Translation: AAH13028.2.
    BC020222 mRNA. Translation: AAH20222.1.
    CCDSiCCDS13291.1. [P04844-1]
    CCDS46599.1. [P04844-2]
    PIRiB26168.
    RefSeqiNP_001129243.1. NM_001135771.1. [P04844-2]
    NP_002942.2. NM_002951.3. [P04844-1]
    UniGeneiHs.370895.

    Genome annotation databases

    EnsembliENST00000237530; ENSP00000237530; ENSG00000118705. [P04844-1]
    ENST00000373622; ENSP00000362724; ENSG00000118705. [P04844-2]
    GeneIDi6185.
    KEGGihsa:6185.
    UCSCiuc002xgp.3. human. [P04844-1]
    uc002xgq.3. human. [P04844-2]

    Polymorphism databases

    DMDMi9297108.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y00282 mRNA. Translation: CAA68393.1 .
    AJ237734
    , AJ237735 , AJ237733 , AJ237736 , AJ237737 , AJ237738 , AJ237739 , AJ237740 , AJ237741 , AJ237742 , AJ237743 , AJ237744 , AJ237745 , AJ237746 , AJ237747 , AJ237748 , AJ237749 Genomic DNA. Translation: CAB54801.1 .
    AK096243 mRNA. Translation: BAG53237.1 .
    CR456899 mRNA. Translation: CAG33180.1 .
    AL031659 Genomic DNA. Translation: CAB41763.1 .
    AL031659 Genomic DNA. Translation: CAI42668.1 .
    CH471077 Genomic DNA. Translation: EAW76073.1 .
    BC002380 mRNA. Translation: AAH02380.2 .
    BC003560 mRNA. Translation: AAH03560.1 .
    BC013028 mRNA. Translation: AAH13028.2 .
    BC020222 mRNA. Translation: AAH20222.1 .
    CCDSi CCDS13291.1. [P04844-1 ]
    CCDS46599.1. [P04844-2 ]
    PIRi B26168.
    RefSeqi NP_001129243.1. NM_001135771.1. [P04844-2 ]
    NP_002942.2. NM_002951.3. [P04844-1 ]
    UniGenei Hs.370895.

    3D structure databases

    ProteinModelPortali P04844.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112100. 37 interactions.
    IntActi P04844. 15 interactions.
    MINTi MINT-8247596.
    STRINGi 9606.ENSP00000237530.

    PTM databases

    PhosphoSitei P04844.

    Polymorphism databases

    DMDMi 9297108.

    Proteomic databases

    MaxQBi P04844.
    PaxDbi P04844.
    PRIDEi P04844.

    Protocols and materials databases

    DNASUi 6185.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000237530 ; ENSP00000237530 ; ENSG00000118705 . [P04844-1 ]
    ENST00000373622 ; ENSP00000362724 ; ENSG00000118705 . [P04844-2 ]
    GeneIDi 6185.
    KEGGi hsa:6185.
    UCSCi uc002xgp.3. human. [P04844-1 ]
    uc002xgq.3. human. [P04844-2 ]

    Organism-specific databases

    CTDi 6185.
    GeneCardsi GC20P035806.
    HGNCi HGNC:10382. RPN2.
    HPAi CAB019277.
    HPA008297.
    HPA025922.
    MIMi 180490. gene.
    neXtProti NX_P04844.
    PharmGKBi PA34778.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG258688.
    HOGENOMi HOG000231261.
    HOVERGENi HBG002365.
    InParanoidi P04844.
    KOi K12667.
    OMAi PTHYLTK.
    OrthoDBi EOG78SQHS.
    PhylomeDBi P04844.
    TreeFami TF106146.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .
    Reactomei REACT_115902. SRP-dependent cotranslational protein targeting to membrane.
    REACT_22426. Asparagine N-linked glycosylation.

    Miscellaneous databases

    ChiTaRSi RPN2. human.
    GeneWikii RPN2.
    GenomeRNAii 6185.
    NextBioi 24021.
    PROi P04844.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P04844.
    Bgeei P04844.
    CleanExi HS_RPN2.
    Genevestigatori P04844.

    Family and domain databases

    InterProi IPR008814. Swp1.
    [Graphical view ]
    PANTHERi PTHR12640:SF0. PTHR12640:SF0. 1 hit.
    Pfami PF05817. Ribophorin_II. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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] (ISOFORM 1).
    2. "Genomic structure of human ribophorin II gene."
      Iolascon A., Totaro A., Gasparini P.
      Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    5. "The DNA sequence and comparative analysis of human chromosome 20."
      Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
      , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
      Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Muscle, Pancreas and Placenta.
    8. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 23-36.
      Tissue: Platelet.
    9. "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.
    10. "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.
    11. "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-106.
      Tissue: Liver.
    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; RPN1; SELK; STT3A; VCP AND VIMP.

    Entry informationi

    Entry nameiRPN2_HUMAN
    AccessioniPrimary (citable) accession number: P04844
    Secondary accession number(s): Q5JYR6
    , Q6IBA5, Q96E21, Q9BUQ3, Q9UBE1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: December 1, 2000
    Last modified: October 1, 2014
    This is version 147 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 20
      Human chromosome 20: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

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