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Protein

Golgi reassembly-stacking protein 1

Gene

GORASP1

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

Functioni

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.

GO - Biological processi

  • Golgi organization Source: UniProtKB
  • mitotic cell cycle Source: Reactome
  • negative regulation of dendrite morphogenesis Source: UniProtKB
  • protein transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Enzyme and pathway databases

ReactomeiREACT_1100. Golgi Cisternae Pericentriolar Stack Reorganization.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:GORASP1
Synonyms:GOLPH5, GRASP65
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:16769. GORASP1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28814.

Polymorphism and mutation databases

BioMutaiGORASP1.
DMDMi51316077.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedCurated
Chaini2 – 440439Golgi reassembly-stacking protein 1PRO_0000087570Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycineCurated
Modified residuei216 – 2161Phosphothreonine3 Publications
Modified residuei373 – 3731PhosphoserineBy similarity

Post-translational modificationi

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.2 Publications
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).By similarity

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

MaxQBiQ9BQQ3.
PaxDbiQ9BQQ3.
PRIDEiQ9BQQ3.

PTM databases

PhosphoSiteiQ9BQQ3.

Miscellaneous databases

PMAP-CutDBQ9BQQ3.

Expressioni

Gene expression databases

BgeeiQ9BQQ3.
CleanExiHS_GORASP1.
ExpressionAtlasiQ9BQQ3. baseline.
GenevestigatoriQ9BQQ3.

Organism-specific databases

HPAiHPA056283.

Interactioni

Subunit structurei

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).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
AGPSO001163EBI-2561458,EBI-2838732
LONRF1Q17RB83EBI-2561458,EBI-2341787
SCRN1Q127653EBI-2561458,EBI-2690712

Protein-protein interaction databases

BioGridi122232. 25 interactions.
IntActiQ9BQQ3. 8 interactions.
MINTiMINT-1185294.
STRINGi9606.ENSP00000313869.

Structurei

3D structure databases

ProteinModelPortaliQ9BQQ3.
SMRiQ9BQQ3. Positions 13-211.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 7571PDZAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni190 – 20213Essential for the interaction with GM130By similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi203 – 29896Pro-richAdd
BLAST
Compositional biasi295 – 2984Poly-Pro
Compositional biasi348 – 3525Poly-Ser

Sequence similaritiesi

Belongs to the GORASP family.Curated
Contains 1 PDZ (DHR) domain.Curated

Phylogenomic databases

eggNOGiCOG5233.
GeneTreeiENSGT00390000008686.
HOGENOMiHOG000054196.
HOVERGENiHBG051826.
InParanoidiQ9BQQ3.
OMAiSGPEDVC.
OrthoDBiEOG7BS4B1.
PhylomeDBiQ9BQQ3.

Family and domain databases

Gene3Di2.30.42.10. 1 hit.
InterProiIPR024958. GRASP55/65_PDZ.
IPR007583. GRASP55_65.
IPR001478. PDZ.
[Graphical view]
PANTHERiPTHR12893. PTHR12893. 1 hit.
PfamiPF04495. GRASP55_65. 1 hit.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 2 hits.

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. AlignAdd to basket

Isoform 1 (identifier: Q9BQQ3-1) [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
MGLGVSAEQP AGGAEGFHLH GVQENSPAQQ AGLEPYFDFI ITIGHSRLNK
60 70 80 90 100
ENDTLKALLK ANVEKPVKLE VFNMKTMRVR EVEVVPSNMW GGQGLLGASV
110 120 130 140 150
RFCSFRRASE QVWHVLDVEP SSPAALAGLR PYTDYVVGSD QILQESEDFF
160 170 180 190 200
TLIESHEGKP LKLMVYNSKS DSCREVTVTP NAAWGGEGSL GCGIGYGYLH
210 220 230 240 250
RIPTQPPSYH KKPPGTPPPS ALPLGAPPPD ALPPGPTPED SPSLETGSRQ
260 270 280 290 300
SDYMEALLQA PGSSMEDPLP GPGSPSHSAP DPDGLPHFME TPLQPPPPVQ
310 320 330 340 350
RVMDPGFLDV SGISLLDNSN ASVWPSLPSS TELTTTAVST SGPEDICSSS
360 370 380 390 400
SSHERGGEAT WSGSEFEVSF LDSPGAQAQA DHLPQLTLPD SLTSAASPED
410 420 430 440
GLSAELLEAQ AEEEPASTEG LDTGTEAEGL DSQAQISTTE
Length:440
Mass (Da):46,482
Last modified:January 23, 2007 - v3
Checksum:i1187C0356E16CE00
GO
Isoform 2 (identifier: Q9BQQ3-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     176-440: VTVTPNAAWG...DSQAQISTTE → SGMWHWLWVS...FCSTTWCPTT

Note: No experimental confirmation available.

Show »
Length:215
Mass (Da):23,906
Checksum:i0EC77420BA924801
GO
Isoform 3 (identifier: Q9BQQ3-3) [UniParc]FASTAAdd to basket

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.

Show »
Length:246
Mass (Da):26,237
Checksum:i9EC9AC172F80403D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti271 – 2711G → E in BAC03598 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti425 – 4251T → M.
Corresponds to variant rs1109643 [ dbSNP | Ensembl ].
VAR_051016

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7373Missing in isoform 3. 1 PublicationVSP_011306Add
BLAST
Alternative sequencei176 – 440265VTVTP…ISTTE → SGMWHWLWVSTPDPNSAPQL PQEATWHPTTFCSTTWCPTT in isoform 2. 1 PublicationVSP_011307Add
BLAST
Alternative sequencei306 – 31914GFLDV…LLDNS → AMPVCGPACPLPQN in isoform 3. 1 PublicationVSP_011308Add
BLAST
Alternative sequencei320 – 440121Missing in isoform 3. 1 PublicationVSP_011309Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS2681.1. [Q9BQQ3-1]
RefSeqiNP_001265718.1. NM_001278789.1.
NP_001265719.1. NM_001278790.1.
NP_114105.1. NM_031899.3. [Q9BQQ3-1]
UniGeneiHs.721946.

Genome annotation databases

EnsembliENST00000319283; ENSP00000313869; ENSG00000114745. [Q9BQQ3-1]
ENST00000431601; ENSP00000403552; ENSG00000114745. [Q9BQQ3-3]
ENST00000452389; ENSP00000403167; ENSG00000114745. [Q9BQQ3-2]
GeneIDi64689.
KEGGihsa:64689.
UCSCiuc003ciw.1. human. [Q9BQQ3-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS2681.1. [Q9BQQ3-1]
RefSeqiNP_001265718.1. NM_001278789.1.
NP_001265719.1. NM_001278790.1.
NP_114105.1. NM_031899.3. [Q9BQQ3-1]
UniGeneiHs.721946.

3D structure databases

ProteinModelPortaliQ9BQQ3.
SMRiQ9BQQ3. Positions 13-211.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122232. 25 interactions.
IntActiQ9BQQ3. 8 interactions.
MINTiMINT-1185294.
STRINGi9606.ENSP00000313869.

PTM databases

PhosphoSiteiQ9BQQ3.

Polymorphism and mutation databases

BioMutaiGORASP1.
DMDMi51316077.

Proteomic databases

MaxQBiQ9BQQ3.
PaxDbiQ9BQQ3.
PRIDEiQ9BQQ3.

Protocols and materials databases

DNASUi64689.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000319283; ENSP00000313869; ENSG00000114745. [Q9BQQ3-1]
ENST00000431601; ENSP00000403552; ENSG00000114745. [Q9BQQ3-3]
ENST00000452389; ENSP00000403167; ENSG00000114745. [Q9BQQ3-2]
GeneIDi64689.
KEGGihsa:64689.
UCSCiuc003ciw.1. human. [Q9BQQ3-1]

Organism-specific databases

CTDi64689.
GeneCardsiGC03M039113.
HGNCiHGNC:16769. GORASP1.
HPAiHPA056283.
MIMi606867. gene.
neXtProtiNX_Q9BQQ3.
PharmGKBiPA28814.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5233.
GeneTreeiENSGT00390000008686.
HOGENOMiHOG000054196.
HOVERGENiHBG051826.
InParanoidiQ9BQQ3.
OMAiSGPEDVC.
OrthoDBiEOG7BS4B1.
PhylomeDBiQ9BQQ3.

Enzyme and pathway databases

ReactomeiREACT_1100. Golgi Cisternae Pericentriolar Stack Reorganization.

Miscellaneous databases

ChiTaRSiGORASP1. human.
GeneWikiiGORASP1.
GenomeRNAii64689.
NextBioi66611.
PMAP-CutDBQ9BQQ3.
PROiQ9BQQ3.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BQQ3.
CleanExiHS_GORASP1.
ExpressionAtlasiQ9BQQ3. baseline.
GenevestigatoriQ9BQQ3.

Family and domain databases

Gene3Di2.30.42.10. 1 hit.
InterProiIPR024958. GRASP55/65_PDZ.
IPR007583. GRASP55_65.
IPR001478. PDZ.
[Graphical view]
PANTHERiPTHR12893. PTHR12893. 1 hit.
PfamiPF04495. GRASP55_65. 1 hit.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-216, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. 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.
  11. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiGORS1_HUMAN
AccessioniPrimary (citable) accession number: Q9BQQ3
Secondary accession number(s): B3KWC8
, Q3SYG7, Q8N272, Q96H42
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: January 23, 2007
Last modified: April 29, 2015
This is version 114 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: 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. 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.