Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9BQQ3 (GORS1_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:
Golgi reassembly-stacking protein 1
Alternative name(s):
Golgi peripheral membrane protein p65
Golgi phosphoprotein 5
Short name=GOLPH5
Golgi reassembly-stacking protein of 65 kDa
Short name=GRASP65
Gene names
Name:GORASP1
Synonyms:GOLPH5, GRASP65
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length440 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Stacking factor involved in the postmitotic assembly of Golgi stacks from mitotic Golgi fragments. Key structural protein required for the maintenance of the Golgi apparatus integrity: its caspase-mediated cleavage is required for fragmentation of the Golgi during apoptosis. Also mediates, via its interaction with GM130, the docking of transport vesicles with the Golgi membranes.

Subunit structure

Homodimer. Forms higher-order oligomers under interphase but not mitotic conditions. Dimers of the protein on one membrane might be able to interact with dimers on another and so stack cisternae. Interacts with the C-terminus of GM130 under both mitotic and non-mitotic conditions. The interaction is critical for the correct targeting of both proteins to the cis-Golgi. The complex binds to the vesicle docking protein p115. Interacts with TMED2 and TMED3 By similarity. Ref.6

Subcellular location

Golgi apparatuscis-Golgi network membrane; Peripheral membrane protein; Cytoplasmic side. Note: Undergoes rapid exchange with the cytosol. Ref.5

Post-translational modification

Phosphorylated by CDC2/B1 and PLK kinases during mitosis. Phosphorylation cycle correlates with the cisternal stacking cycle. Phosphorylation of the homodimer prevents the association of dimers into higher-order oligomers, leading to cisternal unstacking. Ref.6 Ref.7

Target for caspase-3 cleavage during apoptosis. The cleavage contributes to Golgi fragmentation and occurs very early in the execution phase of apoptosis By similarity.

Sequence similarities

Belongs to the GORASP family.

Contains 1 PDZ (DHR) domain.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9BQQ3-1)

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: Q9BQQ3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     176-440: VTVTPNAAWG...DSQAQISTTE → SGMWHWLWVS...FCSTTWCPTT
Note: No experimental confirmation available.
Isoform 3 (identifier: Q9BQQ3-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-73: Missing.
     306-319: GFLDVSGISLLDNS → AMPVCGPACPLPQN
     320-440: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Probable
Chain2 – 440439Golgi reassembly-stacking protein 1
PRO_0000087570

Regions

Domain5 – 7571PDZ
Region190 – 20213Essential for the interaction with GM130 By similarity
Compositional bias203 – 29896Pro-rich
Compositional bias295 – 2984Poly-Pro
Compositional bias348 – 3525Poly-Ser

Amino acid modifications

Modified residue2161Phosphothreonine Ref.8 Ref.9 Ref.10
Modified residue3731Phosphoserine By similarity
Lipidation21N-myristoyl glycine Probable

Natural variations

Alternative sequence1 – 7373Missing in isoform 3.
VSP_011306
Alternative sequence176 – 440265VTVTP…ISTTE → SGMWHWLWVSTPDPNSAPQL PQEATWHPTTFCSTTWCPTT in isoform 2.
VSP_011307
Alternative sequence306 – 31914GFLDV…LLDNS → AMPVCGPACPLPQN in isoform 3.
VSP_011308
Alternative sequence320 – 440121Missing in isoform 3.
VSP_011309
Natural variant4251T → M.
Corresponds to variant rs1109643 [ dbSNP | Ensembl ].
VAR_051016

Experimental info

Sequence conflict2711G → E in BAC03598. Ref.2

Sequences

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

Last modified January 23, 2007. Version 3.
Checksum: 1187C0356E16CE00

FASTA44046,482
        10         20         30         40         50         60 
MGLGVSAEQP AGGAEGFHLH GVQENSPAQQ AGLEPYFDFI ITIGHSRLNK ENDTLKALLK 

        70         80         90        100        110        120 
ANVEKPVKLE VFNMKTMRVR EVEVVPSNMW GGQGLLGASV RFCSFRRASE QVWHVLDVEP 

       130        140        150        160        170        180 
SSPAALAGLR PYTDYVVGSD QILQESEDFF TLIESHEGKP LKLMVYNSKS DSCREVTVTP 

       190        200        210        220        230        240 
NAAWGGEGSL GCGIGYGYLH RIPTQPPSYH KKPPGTPPPS ALPLGAPPPD ALPPGPTPED 

       250        260        270        280        290        300 
SPSLETGSRQ SDYMEALLQA PGSSMEDPLP GPGSPSHSAP DPDGLPHFME TPLQPPPPVQ 

       310        320        330        340        350        360 
RVMDPGFLDV SGISLLDNSN ASVWPSLPSS TELTTTAVST SGPEDICSSS SSHERGGEAT 

       370        380        390        400        410        420 
WSGSEFEVSF LDSPGAQAQA DHLPQLTLPD SLTSAASPED GLSAELLEAQ AEEEPASTEG 

       430        440 
LDTGTEAEGL DSQAQISTTE 

« Hide

Isoform 2 [UniParc].

Checksum: 0EC77420BA924801
Show »

FASTA21523,906
Isoform 3 [UniParc].

Checksum: 9EC9AC172F80403D
Show »

FASTA24626,237

References

« Hide 'large scale' references
[1]"Refined physical mapping and genomic structure of a 4-Mb region (AP-20) on human chromosome 3p22-p21.33 implicated in lung and kidney cancerogenesis."
Protopopov A., Kashuba V., Kvasha S., Klein G., Zabarovsky E.
Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Lung.
[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).
Tissue: Brain and Tongue.
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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] (ISOFORMS 1 AND 2).
Tissue: Eye and Placenta.
[5]"Maintenance of Golgi structure and function depends on the integrity of ER export."
Ward T.H., Polishchuk R.S., Caplan S., Hirschberg K., Lippincott-Schwartz J.
J. Cell Biol. 155:557-570(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION IN THE CYTOSOL.
[6]"A direct role for GRASP65 as a mitotically regulated Golgi stacking factor."
Wang Y., Seemann J., Pypaert M., Shorter J., Warren G.
EMBO J. 22:3279-3290(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION, OLIGOMERIZATION.
[7]"Peripheral Golgi protein GRASP65 is a target of mitotic polo-like kinase (Plk) and Cdc2."
Lin C.-Y., Madsen M.L., Yarm F.R., Jang Y.-J., Liu X., Erikson R.L.
Proc. Natl. Acad. Sci. U.S.A. 97:12589-12594(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION.
[8]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-216, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-216, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"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 THR-216, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ409349 mRNA. Translation: CAC35160.1.
AK091168 mRNA. Translation: BAC03598.1.
AK124755 mRNA. Translation: BAG54090.1.
CH471055 Genomic DNA. Translation: EAW64554.1.
BC008928 mRNA. Translation: AAH08928.1.
BC075854 mRNA. Translation: AAH75854.1.
BC103826 mRNA. Translation: AAI03827.1.
BC103827 mRNA. Translation: AAI03828.1.
RefSeqNP_001265718.1. NM_001278789.1.
NP_001265719.1. NM_001278790.1.
NP_114105.1. NM_031899.3.
UniGeneHs.721946.

3D structure databases

ProteinModelPortalQ9BQQ3.
SMRQ9BQQ3. Positions 13-211.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122232. 14 interactions.
IntActQ9BQQ3. 4 interactions.
MINTMINT-1185294.
STRING9606.ENSP00000313869.

PTM databases

PhosphoSiteQ9BQQ3.

Polymorphism databases

DMDM51316077.

Proteomic databases

PaxDbQ9BQQ3.
PRIDEQ9BQQ3.

Protocols and materials databases

DNASU64689.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000319283; ENSP00000313869; ENSG00000114745. [Q9BQQ3-1]
ENST00000431601; ENSP00000403552; ENSG00000114745. [Q9BQQ3-3]
ENST00000452389; ENSP00000403167; ENSG00000114745. [Q9BQQ3-2]
GeneID64689.
KEGGhsa:64689.
UCSCuc003ciw.1. human. [Q9BQQ3-1]

Organism-specific databases

CTD64689.
GeneCardsGC03M039113.
HGNCHGNC:16769. GORASP1.
HPAHPA056283.
MIM606867. gene.
neXtProtNX_Q9BQQ3.
PharmGKBPA28814.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5233.
HOGENOMHOG000054196.
HOVERGENHBG051826.
InParanoidQ9BQQ3.
OMASGPEDVC.
OrthoDBEOG7BS4B1.
PhylomeDBQ9BQQ3.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.

Gene expression databases

ArrayExpressQ9BQQ3.
BgeeQ9BQQ3.
CleanExHS_GORASP1.
GenevestigatorQ9BQQ3.

Family and domain databases

Gene3D2.30.42.10. 1 hit.
InterProIPR024958. GRASP55/65_PDZ.
IPR007583. GRASP55_65.
IPR001478. PDZ.
[Graphical view]
PANTHERPTHR12893. PTHR12893. 1 hit.
PfamPF04495. GRASP55_65. 1 hit.
[Graphical view]
SUPFAMSSF50156. SSF50156. 2 hits.
ProtoNetSearch...

Other

GeneWikiGORASP1.
GenomeRNAi64689.
NextBio66611.
PMAP-CutDBQ9BQQ3.
PROQ9BQQ3.
SOURCESearch...

Entry information

Entry nameGORS1_HUMAN
AccessionPrimary (citable) accession number: Q9BQQ3
Secondary accession number(s): B3KWC8 expand/collapse secondary AC list , Q3SYG7, Q8N272, Q96H42
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
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 3

Human chromosome 3: entries, gene names and cross-references to MIM