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Q96JB2 (COG3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Conserved oligomeric Golgi complex subunit 3

Short name=COG complex subunit 3
Alternative name(s):
Component of oligomeric Golgi complex 3
Vesicle-docking protein SEC34 homolog
p94
Gene names
Name:COG3
Synonyms:SEC34
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length828 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in ER-Golgi transport. Ref.2

Subunit structure

Component of the conserved oligomeric Golgi complex which is composed of eight different subunits and is required for normal Golgi morphology and localization By similarity.

Subcellular location

Golgi apparatusGolgi stack membrane; Peripheral membrane protein. Note: Associated with the peripheral membrane of cis/medial cisternae. Ref.1

Tissue specificity

Widely expressed with highest levels in pancreas and testis and lowest levels in lung. Ref.1

Sequence similarities

Belongs to the COG3 family.

Ontologies

Keywords
   Biological processProtein transport
Transport
   Cellular componentGolgi apparatus
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processER to Golgi vesicle-mediated transport

Inferred from direct assay Ref.2. Source: UniProtKB

intra-Golgi vesicle-mediated transport

Inferred from direct assay Ref.2. Source: UniProtKB

intracellular protein transport

Inferred from electronic annotation. Source: InterPro

protein glycosylation

Inferred from mutant phenotype PubMed 16420527. Source: UniProtKB

protein localization to organelle

Inferred from mutant phenotype PubMed 16420527. Source: UniProtKB

protein stabilization

Inferred from mutant phenotype PubMed 16420527. Source: UniProtKB

retrograde vesicle-mediated transport, Golgi to ER

Inferred from mutant phenotype PubMed 16420527. Source: UniProtKB

   Cellular_componentGolgi apparatus

Inferred from direct assay PubMed 11980916. Source: UniProtKB

Golgi cisterna membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

Golgi transport complex

Inferred from direct assay Ref.1PubMed 15047703. Source: UniProtKB

cis-Golgi network

Inferred from electronic annotation. Source: InterPro

cytoplasm

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay. Source: HPA

plasma membrane

Inferred from direct assay. Source: HPA

   Molecular_functionprotein transporter activity

Inferred from direct assay Ref.2. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q96JB2-1)

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: Q96JB2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     443-444: AE → GK
     445-828: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 828827Conserved oligomeric Golgi complex subunit 3
PRO_0000213500

Amino acid modifications

Modified residue21N-acetylalanine Ref.6 Ref.11 Ref.12
Modified residue6631Phosphoserine Ref.7 Ref.8 Ref.9

Natural variations

Alternative sequence443 – 4442AE → GK in isoform 2.
VSP_013652
Alternative sequence445 – 828384Missing in isoform 2.
VSP_013653
Natural variant6201R → C in a breast cancer sample; somatic mutation. Ref.13
VAR_036454
Natural variant7471N → S. Ref.2
Corresponds to variant rs2274285 [ dbSNP | Ensembl ].
VAR_055663

Experimental info

Sequence conflict106 – 1072QQ → HE in AAK66974. Ref.1
Sequence conflict8251L → S in AAK66974. Ref.1
Sequence conflict8251L → S in AAK06848. Ref.2
Sequence conflict8251L → S in BAG37012. Ref.3

Sequences

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

Last modified January 23, 2007. Version 3.
Checksum: B3DCF03FD4DC6A60

FASTA82894,096
        10         20         30         40         50         60 
MAEAALLLLP EAAAERDARE KLALWDRRPD TTAPLTDRQT DSVLELKAAA ENLPVPAELP 

        70         80         90        100        110        120 
IEDLCSLTSQ SLPIELTSVV PESTEDILLK GFTSLGMEEE RIETAQQFFS WFAKLQTQMD 

       130        140        150        160        170        180 
QDEGTKYRQM RDYLSGFQEQ CDAILNDVNS ALQHLESLQK QYLFVSNKTG TLHEACEQLL 

       190        200        210        220        230        240 
KEQSELVDLA ENIQQKLSYF NELETINTKL NSPTLSVNSD GFIPMLAKLD DCITYISSHP 

       250        260        270        280        290        300 
NFKDYPIYLL KFKQCLSKAL HLMKTYTVNT LQTLTSQLLK RDPSSVPNAD NAFTLFYVKF 

       310        320        330        340        350        360 
RAAAPKVRTL IEQIELRSEK IPEYQQLLND IHQCYLDQRE LLLGPSIACT VAELTSQNNR 

       370        380        390        400        410        420 
DHCALVRSGC AFMVHVCQDE HQLYNEFFTK PTSKLDELLE KLCVSLYDVF RPLIIHVIHL 

       430        440        450        460        470        480 
ETLSELCGIL KNEVLEDHVQ NNAEQLGAFA AGVKQMLEDV QERLVYRTHI YIQTDITGYK 

       490        500        510        520        530        540 
PAPGDLAYPD KLVMMEQIAQ SLKDEQKKVP SEASFSDVHL EEGESNSLTK SGSTESLNPR 

       550        560        570        580        590        600 
PQTTISPADL HGMWYPTVRR TLVCLSKLYR CIDRAVFQGL SQEALSACIQ SLLGASESIS 

       610        620        630        640        650        660 
KNKTQIDGQL FLIKHLLILR EQIAPFHTEF TIKEISLDLK KTRDAAFKIL NPMTVPRFFR 

       670        680        690        700        710        720 
LNSNNALIEF LLEGTPEIRE HYLDSKKDVD RHLKSACEQF IQQQTKLFVE QLEEFMTKVS 

       730        740        750        760        770        780 
ALKTMASQGG PKYTLSQQPW AQPAKVNDLA ATAYKTIKTK LPVTLRSMSL YLSNKDTEFI 

       790        800        810        820 
LFKPVRNNIQ QVFQKFHALL KEEFSPEDIQ IIACPSMEQL SLLLLVSK 

« Hide

Isoform 2 [UniParc].

Checksum: 55874C370679512F
Show »

FASTA44450,540

References

« Hide 'large scale' references
[1]"Identification of a human ortholog of Sec34p as a component of the cis-Golgi vesicle tethering machinery."
Suvorova E.S., Kurten R.C., Lupashin V.V.
J. Biol. Chem. 276:22810-22818(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Fetal brain.
[2]"Sec34 is implicated in traffic from the endoplasmic reticulum to the Golgi and exists in a complex with GTC-90 and ldlBp."
Loh E., Hong W.
J. Biol. Chem. 277:21955-21961(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, VARIANT SER-747.
[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. 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] (ISOFORM 1).
Tissue: Placenta.
[4]"The DNA sequence and analysis of human chromosome 13."
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
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] (ISOFORM 2).
Tissue: Leukocyte.
[6]"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 2-16, ACETYLATION AT ALA-2.
Tissue: Platelet.
[7]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-663, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-663, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[9]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-663, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[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]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"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].
[13]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] CYS-620.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF349676 mRNA. Translation: AAK66974.1.
AF332595 mRNA. Translation: AAK06848.1.
AK314387 mRNA. Translation: BAG37012.1.
AL139326, AL606514 Genomic DNA. Translation: CAH72888.1.
BC038953 mRNA. Translation: AAH38953.1.
RefSeqNP_113619.2. NM_031431.3.
UniGeneHs.507948.

3D structure databases

ProteinModelPortalQ96JB2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123680. 17 interactions.
IntActQ96JB2. 9 interactions.
MINTMINT-3054332.
STRING9606.ENSP00000258654.

PTM databases

PhosphoSiteQ96JB2.

Polymorphism databases

DMDM85701302.

Proteomic databases

PaxDbQ96JB2.
PRIDEQ96JB2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000349995; ENSP00000258654; ENSG00000136152. [Q96JB2-1]
GeneID83548.
KEGGhsa:83548.
UCSCuc001vai.3. human. [Q96JB2-2]
uc001vak.3. human. [Q96JB2-1]

Organism-specific databases

CTD83548.
GeneCardsGC13P046039.
H-InvDBHIX0011290.
HGNCHGNC:18619. COG3.
HPAHPA040353.
MIM606975. gene.
neXtProtNX_Q96JB2.
PharmGKBPA38602.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG300871.
HOGENOMHOG000264596.
HOVERGENHBG051062.
InParanoidQ96JB2.
OMAKIPEYQQ.
OrthoDBEOG7NGQ9R.
PhylomeDBQ96JB2.
TreeFamTF314200.

Gene expression databases

BgeeQ96JB2.
CleanExHS_COG3.
GenevestigatorQ96JB2.

Family and domain databases

InterProIPR007265. COG_su3.
[Graphical view]
PANTHERPTHR13302. PTHR13302. 1 hit.
PfamPF04136. Sec34. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiCOG3.
GenomeRNAi83548.
NextBio72485.
PROQ96JB2.
SOURCESearch...

Entry information

Entry nameCOG3_HUMAN
AccessionPrimary (citable) accession number: Q96JB2
Secondary accession number(s): B2RAW5 expand/collapse secondary AC list , Q5VT70, Q8IXX4, Q9BZ92
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2002
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 104 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

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 13

Human chromosome 13: entries, gene names and cross-references to MIM