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Protein

Conserved oligomeric Golgi complex subunit 4

Gene

COG4

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

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 - 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
Complete GO annotation...

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
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Involvement in diseasei

Congenital disorder of glycosylation 2J1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:613489
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti729 – 7291R → W in CDG2J; severe defects in glycosylation. 2 Publications
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

BgeeiQ9H9E3.
CleanExiHS_COG4.
ExpressionAtlasiQ9H9E3. baseline and differential.
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. 20 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 – 57236Combined sources
Turni573 – 5753Combined sources
Helixi580 – 61536Combined sources
Helixi617 – 6259Combined sources
Helixi626 – 6294Combined sources
Helixi636 – 6449Combined sources
Helixi649 – 66618Combined sources
Helixi669 – 69123Combined sources
Helixi698 – 71619Combined sources
Helixi723 – 7264Combined sources
Helixi728 – 73710Combined sources
Helixi742 – 7476Combined sources
Helixi750 – 7534Combined sources
Helixi762 – 7698Combined sources
Helixi777 – 7826Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00390000003662.
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

        10         20         30         40         50
MADLDSPPKL SGVQQPSEGV GGGRCSEISA ELIRSLTELQ ELEAVYERLC
60 70 80 90 100
GEEKVVEREL DALLEQQNTI ESKMVTLHRM GPNLQLIEGD AKQLAGMITF
110 120 130 140 150
TCNLAENVSS KVRQLDLAKN RLYQAIQRAD DILDLKFCMD GVQTALRSED
160 170 180 190 200
YEQAAAHTHR YLCLDKSVIE LSRQGKEGSM IDANLKLLQE AEQRLKAIVA
210 220 230 240 250
EKFAIATKEG DLPQVERFFK IFPLLGLHEE GLRKFSEYLC KQVASKAEEN
260 270 280 290 300
LLMVLGTDMS DRRAAVIFAD TLTLLFEGIA RIVETHQPIV ETYYGPGRLY
310 320 330 340 350
TLIKYLQVEC DRQVEKVVDK FIKQRDYHQQ FRHVQNNLMR NSTTEKIEPR
360 370 380 390 400
ELDPILTEVT LMNARSELYL RFLKKRISSD FEVGDSMASE EVKQEHQKCL
410 420 430 440 450
DKLLNNCLLS CTMQELIGLY VTMEEYFMRE TVNKAVALDT YEKGQLTSSM
460 470 480 490 500
VDDVFYIVKK CIGRALSSSS IDCLCAMINL ATTELESDFR DVLCNKLRMG
510 520 530 540 550
FPATTFQDIQ RGVTSAVNIM HSSLQQGKFD TKGIESTDEA KMSFLVTLNN
560 570 580 590 600
VEVCSENIST LKKTLESDCT KLFSQGIGGE QAQAKFDSCL SDLAAVSNKF
610 620 630 640 650
RDLLQEGLTE LNSTAIKPQV QPWINSFFSV SHNIEEEEFN DYEANDPWVQ
660 670 680 690 700
QFILNLEQQM AEFKASLSPV IYDSLTGLMT SLVAVELEKV VLKSTFNRLG
710 720 730 740 750
GLQFDKELRS LIAYLTTVTT WTIRDKFARL SQMATILNLE RVTEILDYWG
760 770 780
PNSGPLTWRL TPAEVRQVLA LRIDFRSEDI KRLRL
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.Curated

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. 2 Publications
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:
EMBLi
GenBanki
DDBJi
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

EnsembliENST00000482252; 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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi117365. 20 interactions.
DIPiDIP-32635N.
IntActiQ9H9E3. 13 interactions.
MINTiMINT-3069262.
STRINGi9606.ENSP00000315775.

PTM databases

PhosphoSiteiQ9H9E3.

Polymorphism databases

DMDMi311033464.

Proteomic databases

MaxQBiQ9H9E3.
PaxDbiQ9H9E3.
PRIDEiQ9H9E3.

Protocols and materials databases

DNASUi25839.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000482252; ENSP00000432802; ENSG00000103051. [Q9H9E3-2]
GeneIDi25839.
KEGGihsa:25839.
UCSCiuc002eze.3. human. [Q9H9E3-1]

Organism-specific databases

CTDi25839.
GeneCardsiGC16M070514.
GeneReviewsiCOG4.
H-InvDBHIX0013201.
HGNCiHGNC:18620. COG4.
HPAiHPA040924.
HPA042539.
MIMi606976. gene.
613489. phenotype.
neXtProtiNX_Q9H9E3.
Orphaneti263501. COG4-CDG.
PharmGKBiPA38603.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG321175.
GeneTreeiENSGT00390000003662.
HOVERGENiHBG031403.
InParanoidiQ9H9E3.
PhylomeDBiQ9H9E3.

Miscellaneous databases

ChiTaRSiCOG4. human.
EvolutionaryTraceiQ9H9E3.
GeneWikiiCOG4.
GenomeRNAii25839.
NextBioi47151.
PROiQ9H9E3.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H9E3.
CleanExiHS_COG4.
ExpressionAtlasiQ9H9E3. baseline and differential.
GenevestigatoriQ9H9E3.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  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: February 4, 2015
This is version 124 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

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.