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Q9H9E3 (COG4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Conserved oligomeric Golgi complex subunit 4

Short name=COG complex subunit 4
Alternative name(s):
Component of oligomeric Golgi complex 4
Gene names
Name:COG4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length785 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for normal Golgi function. Plays a role in SNARE-pin assembly and Golgi-to-ER retrograde transport via its interaction with SCFD1. Ref.9

Subunit structure

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. Ref.9 Ref.12

Subcellular location

Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side Probable Ref.6.

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.12 Ref.13

Sequence similarities

Belongs to the COG4 family.

Sequence caution

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

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9H9E3-1)

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.
Isoform 2 (identifier: Q9H9E3-2)

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.
Isoform 3 (identifier: Q9H9E3-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-73: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 785784Conserved oligomeric Golgi complex subunit 4
PRO_0000213504

Regions

Region2 – 8483Interacts with SCFD1
Region85 – 15369Interacts with STX5
Region618 – 740123D domain
Region741 – 78545E domain; essential for proper cell surface glycosylation

Amino acid modifications

Modified residue21N-acetylalanine Ref.8 Ref.11

Natural variations

Alternative sequence1 – 7373Missing in isoform 3.
VSP_037551
Alternative sequence331 – 3377FRHVQNN → NFVFSFF in isoform 2.
VSP_001127
Alternative sequence338 – 785448Missing in isoform 2.
VSP_001128
Natural variant1581T → I. Ref.1 Ref.2 Ref.4
Corresponds to variant rs3931036 [ dbSNP | Ensembl ].
VAR_058009
Natural variant7291R → W in CDG2J; severe defects in glycosylation. Ref.12 Ref.13
VAR_063767

Experimental info

Mutagenesis7291R → A: Severe defects in glycosylation. Ref.12
Mutagenesis7641E → A: Severe defects in glycosylation. Ref.12
Sequence conflict1771E → G in BAB14286. Ref.2
Sequence conflict2341K → R in BAB14286. Ref.2
Sequence conflict2851T → A in BAB14286. Ref.2
Sequence conflict4861E → G in BAB15483. Ref.2
Sequence conflict5881S → G in BAB14286. Ref.2
Sequence conflict5881S → G in BAG59950. Ref.2
Sequence conflict6441A → S in AAH06306. Ref.4

Secondary structure

............................. 785
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 2, 2010. Version 3.
Checksum: 93E8597991934AD2

FASTA78589,083
        10         20         30         40         50         60 
MADLDSPPKL SGVQQPSEGV GGGRCSEISA ELIRSLTELQ ELEAVYERLC GEEKVVEREL 

        70         80         90        100        110        120 
DALLEQQNTI ESKMVTLHRM GPNLQLIEGD AKQLAGMITF TCNLAENVSS KVRQLDLAKN 

       130        140        150        160        170        180 
RLYQAIQRAD DILDLKFCMD GVQTALRSED YEQAAAHTHR YLCLDKSVIE LSRQGKEGSM 

       190        200        210        220        230        240 
IDANLKLLQE AEQRLKAIVA EKFAIATKEG DLPQVERFFK IFPLLGLHEE GLRKFSEYLC 

       250        260        270        280        290        300 
KQVASKAEEN LLMVLGTDMS DRRAAVIFAD TLTLLFEGIA RIVETHQPIV ETYYGPGRLY 

       310        320        330        340        350        360 
TLIKYLQVEC DRQVEKVVDK FIKQRDYHQQ FRHVQNNLMR NSTTEKIEPR ELDPILTEVT 

       370        380        390        400        410        420 
LMNARSELYL RFLKKRISSD FEVGDSMASE EVKQEHQKCL DKLLNNCLLS CTMQELIGLY 

       430        440        450        460        470        480 
VTMEEYFMRE TVNKAVALDT YEKGQLTSSM VDDVFYIVKK CIGRALSSSS IDCLCAMINL 

       490        500        510        520        530        540 
ATTELESDFR DVLCNKLRMG FPATTFQDIQ RGVTSAVNIM HSSLQQGKFD TKGIESTDEA 

       550        560        570        580        590        600 
KMSFLVTLNN VEVCSENIST LKKTLESDCT KLFSQGIGGE QAQAKFDSCL SDLAAVSNKF 

       610        620        630        640        650        660 
RDLLQEGLTE LNSTAIKPQV QPWINSFFSV SHNIEEEEFN DYEANDPWVQ QFILNLEQQM 

       670        680        690        700        710        720 
AEFKASLSPV IYDSLTGLMT SLVAVELEKV VLKSTFNRLG GLQFDKELRS LIAYLTTVTT 

       730        740        750        760        770        780 
WTIRDKFARL SQMATILNLE RVTEILDYWG PNSGPLTWRL TPAEVRQVLA LRIDFRSEDI 


KRLRL 

« Hide

Isoform 2 (Cog4S) [UniParc].

Checksum: 3255EF1D38584CC9
Show »

FASTA33738,245
Isoform 3 [UniParc].

Checksum: E6426B98B87E5226
Show »

FASTA71281,098

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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]"An unappreciated role for RNA surveillance."
Hillman R.T., Green R.E., Brenner S.E.
Genome Biol. 5:R8.1-R8.16(2004) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001182068.1. NM_001195139.1.
NP_056201.2. NM_015386.2.
UniGeneHs.208680.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3HR0X-ray1.90A/B525-785[»]
ProteinModelPortalQ9H9E3.
SMRQ9H9E3. Positions 536-785.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117365. 14 interactions.
DIPDIP-32635N.
IntActQ9H9E3. 13 interactions.
MINTMINT-3069262.
STRING9606.ENSP00000315775.

PTM databases

PhosphoSiteQ9H9E3.

Polymorphism databases

DMDM311033464.

Proteomic databases

PaxDbQ9H9E3.
PRIDEQ9H9E3.

Protocols and materials databases

DNASU25839.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000393612; ENSP00000377236; ENSG00000103051. [Q9H9E3-2]
ENST00000482252; ENSP00000432802; ENSG00000103051. [Q9H9E3-2]
GeneID25839.
KEGGhsa:25839.
UCSCuc002eze.3. human. [Q9H9E3-1]

Organism-specific databases

CTD25839.
GeneCardsGC16M070514.
H-InvDBHIX0013201.
HGNCHGNC:18620. COG4.
HPAHPA040924.
HPA042539.
MIM606976. gene.
613489. phenotype.
neXtProtNX_Q9H9E3.
Orphanet263501. COG4-CDG.
PharmGKBPA38603.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG321175.
HOVERGENHBG031403.
InParanoidQ9H9E3.
PhylomeDBQ9H9E3.

Gene expression databases

ArrayExpressQ9H9E3.
BgeeQ9H9E3.
CleanExHS_COG4.
GenevestigatorQ9H9E3.

Family and domain databases

InterProIPR013167. COG_su4.
[Graphical view]
PfamPF08318. COG4. 1 hit.
[Graphical view]
SMARTSM00762. Cog4. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9H9E3.
GeneWikiCOG4.
GenomeRNAi25839.
NextBio47151.
PROQ9H9E3.
SOURCESearch...

Entry information

Entry nameCOG4_HUMAN
AccessionPrimary (citable) accession number: Q9H9E3
Secondary accession number(s): B4DMN8 expand/collapse secondary AC list , C9JS23, Q96D40, Q9BRF0, Q9BVZ2, Q9H5Y4, Q9Y3W3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2002
Last sequence update: November 2, 2010
Last modified: March 19, 2014
This is version 116 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM