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Q9H9E3

- COG4_HUMAN

UniProt

Q9H9E3 - COG4_HUMAN

Protein

Conserved oligomeric Golgi complex subunit 4

Gene

COG4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 3 (02 Nov 2010)
      Previous versions | rss
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    Functioni

    Required for normal Golgi function. Plays a role in SNARE-pin assembly and Golgi-to-ER retrograde transport via its interaction with SCFD1.1 Publication

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. Golgi organization Source: UniProtKB
    2. Golgi vesicle prefusion complex stabilization Source: UniProtKB
    3. protein transport Source: UniProtKB-KW
    4. retrograde vesicle-mediated transport, Golgi to ER Source: UniProtKB

    Keywords - Biological processi

    Protein transport, Transport

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Conserved oligomeric Golgi complex subunit 4
    Short name:
    COG complex subunit 4
    Alternative name(s):
    Component of oligomeric Golgi complex 4
    Gene namesi
    Name:COG4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:18620. COG4.

    Subcellular locationi

    Golgi apparatus membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication

    GO - Cellular componenti

    1. Golgi membrane Source: UniProtKB-SubCell
    2. Golgi transport complex Source: UniProtKB

    Keywords - Cellular componenti

    Golgi apparatus, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Congenital disorder of glycosylation 2J (CDG2J) [MIM:613489]: A multisystem disorder caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N-glycoproteins during embryonic development, differentiation, and maintenance of cell functions.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti729 – 7291R → W in CDG2J; severe defects in glycosylation. 1 Publication
    VAR_063767

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi729 – 7291R → A: Severe defects in glycosylation. 1 Publication
    Mutagenesisi764 – 7641E → A: Severe defects in glycosylation. 1 Publication

    Keywords - Diseasei

    Congenital disorder of glycosylation, Disease mutation

    Organism-specific databases

    MIMi613489. phenotype.
    Orphaneti263501. COG4-CDG.
    PharmGKBiPA38603.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 785784Conserved oligomeric Golgi complex subunit 4PRO_0000213504Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9H9E3.
    PaxDbiQ9H9E3.
    PRIDEiQ9H9E3.

    PTM databases

    PhosphoSiteiQ9H9E3.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9H9E3.
    BgeeiQ9H9E3.
    CleanExiHS_COG4.
    GenevestigatoriQ9H9E3.

    Organism-specific databases

    HPAiHPA040924.
    HPA042539.

    Interactioni

    Subunit structurei

    Monomer. Component of the conserved oligomeric Golgi (COG) complex which is composed of eight different subunits and is required for normal Golgi morphology and localization. Mediates interaction of SCFD1 with the COG complex. Interacts with STX5.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    COG1Q8WTW32EBI-368382,EBI-368371
    COG2Q147462EBI-368382,EBI-389449
    COG5Q9UP832EBI-368382,EBI-389502
    COG7P834364EBI-368382,EBI-389534
    SCFD1Q8WVM810EBI-368382,EBI-722569
    STX5Q131902EBI-368382,EBI-714206

    Protein-protein interaction databases

    BioGridi117365. 14 interactions.
    DIPiDIP-32635N.
    IntActiQ9H9E3. 13 interactions.
    MINTiMINT-3069262.
    STRINGi9606.ENSP00000315775.

    Structurei

    Secondary structure

    1
    785
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi537 – 57236
    Turni573 – 5753
    Helixi580 – 61536
    Helixi617 – 6259
    Helixi626 – 6294
    Helixi636 – 6449
    Helixi649 – 66618
    Helixi669 – 69123
    Helixi698 – 71619
    Helixi723 – 7264
    Helixi728 – 73710
    Helixi742 – 7476
    Helixi750 – 7534
    Helixi762 – 7698
    Helixi777 – 7826

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3HR0X-ray1.90A/B525-785[»]
    ProteinModelPortaliQ9H9E3.
    SMRiQ9H9E3. Positions 536-785.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9H9E3.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 8483Interacts with SCFD1Add
    BLAST
    Regioni85 – 15369Interacts with STX5Add
    BLAST
    Regioni618 – 740123D domainAdd
    BLAST
    Regioni741 – 78545E domain; essential for proper cell surface glycosylationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the COG4 family.Curated

    Phylogenomic databases

    eggNOGiNOG321175.
    HOVERGENiHBG031403.
    InParanoidiQ9H9E3.
    PhylomeDBiQ9H9E3.

    Family and domain databases

    InterProiIPR013167. COG_su4.
    [Graphical view]
    PfamiPF08318. COG4. 1 hit.
    [Graphical view]
    SMARTiSM00762. Cog4. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9H9E3-1) [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

    MADLDSPPKL SGVQQPSEGV GGGRCSEISA ELIRSLTELQ ELEAVYERLC    50
    GEEKVVEREL DALLEQQNTI ESKMVTLHRM GPNLQLIEGD AKQLAGMITF 100
    TCNLAENVSS KVRQLDLAKN RLYQAIQRAD DILDLKFCMD GVQTALRSED 150
    YEQAAAHTHR YLCLDKSVIE LSRQGKEGSM IDANLKLLQE AEQRLKAIVA 200
    EKFAIATKEG DLPQVERFFK IFPLLGLHEE GLRKFSEYLC KQVASKAEEN 250
    LLMVLGTDMS DRRAAVIFAD TLTLLFEGIA RIVETHQPIV ETYYGPGRLY 300
    TLIKYLQVEC DRQVEKVVDK FIKQRDYHQQ FRHVQNNLMR NSTTEKIEPR 350
    ELDPILTEVT LMNARSELYL RFLKKRISSD FEVGDSMASE EVKQEHQKCL 400
    DKLLNNCLLS CTMQELIGLY VTMEEYFMRE TVNKAVALDT YEKGQLTSSM 450
    VDDVFYIVKK CIGRALSSSS IDCLCAMINL ATTELESDFR DVLCNKLRMG 500
    FPATTFQDIQ RGVTSAVNIM HSSLQQGKFD TKGIESTDEA KMSFLVTLNN 550
    VEVCSENIST LKKTLESDCT KLFSQGIGGE QAQAKFDSCL SDLAAVSNKF 600
    RDLLQEGLTE LNSTAIKPQV QPWINSFFSV SHNIEEEEFN DYEANDPWVQ 650
    QFILNLEQQM AEFKASLSPV IYDSLTGLMT SLVAVELEKV VLKSTFNRLG 700
    GLQFDKELRS LIAYLTTVTT WTIRDKFARL SQMATILNLE RVTEILDYWG 750
    PNSGPLTWRL TPAEVRQVLA LRIDFRSEDI KRLRL 785
    Length:785
    Mass (Da):89,083
    Last modified:November 2, 2010 - v3
    Checksum:i93E8597991934AD2
    GO
    Isoform 2 (identifier: Q9H9E3-2) [UniParc]FASTAAdd to Basket

    Also known as: Cog4S

    The sequence of this isoform differs from the canonical sequence as follows:
         331-337: FRHVQNN → NFVFSFF
         338-785: Missing.

    Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

    Show »
    Length:337
    Mass (Da):38,245
    Checksum:i3255EF1D38584CC9
    GO
    Isoform 3 (identifier: Q9H9E3-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-73: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:712
    Mass (Da):81,098
    Checksum:iE6426B98B87E5226
    GO

    Sequence cautioni

    The sequence BAB15483.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti177 – 1771E → G in BAB14286. (PubMed:14702039)Curated
    Sequence conflicti234 – 2341K → R in BAB14286. (PubMed:14702039)Curated
    Sequence conflicti285 – 2851T → A in BAB14286. (PubMed:14702039)Curated
    Sequence conflicti486 – 4861E → G in BAB15483. (PubMed:14702039)Curated
    Sequence conflicti588 – 5881S → G in BAB14286. (PubMed:14702039)Curated
    Sequence conflicti588 – 5881S → G in BAG59950. (PubMed:14702039)Curated
    Sequence conflicti644 – 6441A → S in AAH06306. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti158 – 1581T → I.3 Publications
    Corresponds to variant rs3931036 [ dbSNP | Ensembl ].
    VAR_058009
    Natural varianti729 – 7291R → W in CDG2J; severe defects in glycosylation. 1 Publication
    VAR_063767

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 7373Missing in isoform 3. 1 PublicationVSP_037551Add
    BLAST
    Alternative sequencei331 – 3377FRHVQNN → NFVFSFF in isoform 2. 1 PublicationVSP_001127
    Alternative sequencei338 – 785448Missing in isoform 2. 1 PublicationVSP_001128Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB088369 mRNA. Translation: BAC05682.1.
    AK022874 mRNA. Translation: BAB14286.1.
    AK026435 mRNA. Translation: BAB15483.1. Different initiation.
    AK297557 mRNA. Translation: BAG59950.1.
    AC106804 Genomic DNA. No translation available.
    BC000796 mRNA. Translation: AAH00796.1.
    BC006306 mRNA. Translation: AAH06306.2.
    BC013347 mRNA. Translation: AAH13347.2.
    BC072438 mRNA. Translation: AAH72438.1.
    AL050101 mRNA. Translation: CAB43272.1.
    RefSeqiNP_001182068.1. NM_001195139.1.
    NP_056201.2. NM_015386.2.
    UniGeneiHs.208680.

    Genome annotation databases

    EnsembliENST00000393612; ENSP00000377236; ENSG00000103051. [Q9H9E3-2]
    ENST00000482252; ENSP00000432802; ENSG00000103051. [Q9H9E3-2]
    GeneIDi25839.
    KEGGihsa:25839.
    UCSCiuc002eze.3. human. [Q9H9E3-1]

    Polymorphism databases

    DMDMi311033464.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB088369 mRNA. Translation: BAC05682.1 .
    AK022874 mRNA. Translation: BAB14286.1 .
    AK026435 mRNA. Translation: BAB15483.1 . Different initiation.
    AK297557 mRNA. Translation: BAG59950.1 .
    AC106804 Genomic DNA. No translation available.
    BC000796 mRNA. Translation: AAH00796.1 .
    BC006306 mRNA. Translation: AAH06306.2 .
    BC013347 mRNA. Translation: AAH13347.2 .
    BC072438 mRNA. Translation: AAH72438.1 .
    AL050101 mRNA. Translation: CAB43272.1 .
    RefSeqi NP_001182068.1. NM_001195139.1.
    NP_056201.2. NM_015386.2.
    UniGenei Hs.208680.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3HR0 X-ray 1.90 A/B 525-785 [» ]
    ProteinModelPortali Q9H9E3.
    SMRi Q9H9E3. Positions 536-785.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117365. 14 interactions.
    DIPi DIP-32635N.
    IntActi Q9H9E3. 13 interactions.
    MINTi MINT-3069262.
    STRINGi 9606.ENSP00000315775.

    PTM databases

    PhosphoSitei Q9H9E3.

    Polymorphism databases

    DMDMi 311033464.

    Proteomic databases

    MaxQBi Q9H9E3.
    PaxDbi Q9H9E3.
    PRIDEi Q9H9E3.

    Protocols and materials databases

    DNASUi 25839.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000393612 ; ENSP00000377236 ; ENSG00000103051 . [Q9H9E3-2 ]
    ENST00000482252 ; ENSP00000432802 ; ENSG00000103051 . [Q9H9E3-2 ]
    GeneIDi 25839.
    KEGGi hsa:25839.
    UCSCi uc002eze.3. human. [Q9H9E3-1 ]

    Organism-specific databases

    CTDi 25839.
    GeneCardsi GC16M070514.
    GeneReviewsi COG4.
    H-InvDB HIX0013201.
    HGNCi HGNC:18620. COG4.
    HPAi HPA040924.
    HPA042539.
    MIMi 606976. gene.
    613489. phenotype.
    neXtProti NX_Q9H9E3.
    Orphaneti 263501. COG4-CDG.
    PharmGKBi PA38603.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG321175.
    HOVERGENi HBG031403.
    InParanoidi Q9H9E3.
    PhylomeDBi Q9H9E3.

    Miscellaneous databases

    EvolutionaryTracei Q9H9E3.
    GeneWikii COG4.
    GenomeRNAii 25839.
    NextBioi 47151.
    PROi Q9H9E3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9H9E3.
    Bgeei Q9H9E3.
    CleanExi HS_COG4.
    Genevestigatori Q9H9E3.

    Family and domain databases

    InterProi IPR013167. COG_su4.
    [Graphical view ]
    Pfami PF08318. COG4. 1 hit.
    [Graphical view ]
    SMARTi SM00762. Cog4. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cog4S, a splicing variant of Cog4."
      Ariga H.
      Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT ILE-158.
      Tissue: T-cell.
    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] (ISOFORMS 1 AND 3), VARIANT ILE-158.
      Tissue: Brain, Ileal mucosa and Testis.
    3. "The sequence and analysis of duplication-rich human chromosome 16."
      Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
      , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
      Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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), VARIANT ILE-158.
      Tissue: Muscle, Placenta, Skin and Testis.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 229-785 (ISOFORM 1).
      Tissue: Uterus.
    6. "The Sec34/35 Golgi transport complex is related to the exocyst, defining a family of complexes involved in multiple steps of membrane traffic."
      Whyte J.R., Munro S.
      Dev. Cell 1:527-537(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    7. Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
    8. "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(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    9. "Direct interaction between the COG complex and the SM protein, Sly1, is required for Golgi SNARE pairing."
      Laufman O., Kedan A., Hong W., Lev S.
      EMBO J. 28:2006-2017(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SCFD1 AND STX5.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Structural basis for a human glycosylation disorder caused by mutation of the COG4 gene."
      Richardson B.C., Smith R.D., Ungar D., Nakamura A., Jeffrey P.D., Lupashin V.V., Hughson F.M.
      Proc. Natl. Acad. Sci. U.S.A. 106:13329-13334(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 525-785, SUBUNIT, IDENTIFICATION OF DOMAINS D AND E, CHARACTERIZATION OF VARIANT CDG2J TRP-729, MUTAGENESIS OF ARG-729 AND GLU-764.
    13. "Golgi function and dysfunction in the first COG4-deficient CDG type II patient."
      Reynders E., Foulquier F., Leao Teles E., Quelhas D., Morelle W., Rabouille C., Annaert W., Matthijs G.
      Hum. Mol. Genet. 18:3244-3256(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CDG2J TRP-729.

    Entry informationi

    Entry nameiCOG4_HUMAN
    AccessioniPrimary (citable) accession number: Q9H9E3
    Secondary accession number(s): B4DMN8
    , C9JS23, Q96D40, Q9BRF0, Q9BVZ2, Q9H5Y4, Q9Y3W3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 30, 2002
    Last sequence update: November 2, 2010
    Last modified: October 1, 2014
    This is version 120 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

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