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Protein

Golgi reassembly-stacking protein 1

Gene

Gorasp1

Organism
Rattus norvegicus (Rat)
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 GOLGA2/GM130, the docking of transport vesicles with the Golgi membranes.2 Publications

GO - Biological processi

  • Golgi organization Source: RGD
  • negative regulation of dendrite morphogenesis Source: UniProtKB
  • protein N-linked glycosylation Source: RGD
  • protein transport Source: UniProtKB-KW

Keywordsi

Biological processProtein transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Golgi reassembly-stacking protein 1
Alternative name(s):
Golgi peripheral membrane protein p65
Golgi reassembly-stacking protein of 65 kDa1 Publication
Short name:
GRASP651 Publication
Gene namesi
Name:Gorasp1
Synonyms:Grasp651 Publication
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi621122. Gorasp1.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi320D → A: Blocks the caspase-mediated cleavage. 1 Publication1
Mutagenesisi375D → A: Blocks the caspase-mediated cleavage. 1 Publication1
Mutagenesisi393D → A: Blocks the caspase-mediated cleavage. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000875722 – 451Golgi reassembly-stacking protein 1Add BLAST450

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi2N-myristoyl glycine1 Publication1
Modified residuei216PhosphoserineCombined sources1
Modified residuei220PhosphothreonineCombined sources1
Modified residuei224PhosphothreonineBy similarity1
Modified residuei365PhosphoserineCombined sources1
Modified residuei367PhosphoserineCombined sources1
Modified residuei376PhosphoserineBy similarity1

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

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

PaxDbiO35254.
PRIDEiO35254.

PTM databases

iPTMnetiO35254.
PhosphoSitePlusiO35254.

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 GOLGA2/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/USO1. Interacts with TMED2 and TMED3.3 Publications

Binary interactionsi

Show more details

Protein-protein interaction databases

CORUMiO35254.
DIPiDIP-60188N.
ELMiO35254.
IntActiO35254. 5 interactors.
MINTiMINT-4578765.
STRINGi10116.ENSRNOP00000024408.

Structurei

Secondary structure

1451
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi16 – 21Combined sources6
Helixi26 – 29Combined sources4
Turni34 – 36Combined sources3
Beta strandi37 – 42Combined sources6
Beta strandi49 – 52Combined sources4
Helixi53 – 60Combined sources8
Turni61 – 63Combined sources3
Beta strandi66 – 72Combined sources7
Turni73 – 75Combined sources3
Beta strandi78 – 83Combined sources6
Beta strandi89 – 95Combined sources7
Beta strandi97 – 101Combined sources5
Helixi104 – 109Combined sources6
Beta strandi112 – 117Combined sources6
Helixi122 – 126Combined sources5
Turni130 – 132Combined sources3
Beta strandi133 – 139Combined sources7
Helixi148 – 154Combined sources7
Turni155 – 157Combined sources3
Beta strandi160 – 166Combined sources7
Turni167 – 170Combined sources4
Beta strandi171 – 177Combined sources7
Beta strandi183 – 189Combined sources7
Beta strandi191 – 194Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4KFVX-ray2.20A1-210[»]
SMRiO35254.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini5 – 74PDZAdd BLAST70

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni189 – 201Essential for interaction with GOLGA2/GM130Add BLAST13

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi298 – 301Poly-Pro4
Compositional biasi314 – 355Ser-richAdd BLAST42
Compositional biasi351 – 355Poly-Ser5

Sequence similaritiesi

Belongs to the GORASP family.Curated

Phylogenomic databases

eggNOGiKOG3834. Eukaryota.
COG5233. LUCA.
HOGENOMiHOG000054196.
HOVERGENiHBG051826.
InParanoidiO35254.
PhylomeDBiO35254.

Family and domain databases

InterProiView protein in InterPro
IPR024958. GRASP55/65_PDZ.
IPR007583. GRASP55_65.
IPR036034. PDZ_sf.
PANTHERiPTHR12893. PTHR12893. 1 hit.
PfamiView protein in Pfam
PF04495. GRASP55_65. 1 hit.
SUPFAMiSSF50156. SSF50156. 2 hits.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O35254-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGLGASSEQP AGGEGFHLHG VQENSPAQQA GLEPYFDFII TIGHSRLNKE
60 70 80 90 100
NDTLKALLKA NVEKPVKLEV FNMKTMRVRE VEVVPSNMWG GQGLLGASVR
110 120 130 140 150
FCSFRRASEH VWHVLDVEPS SPAALAGLRP YTDYIVGSDQ ILQESEDFFT
160 170 180 190 200
LIESHEGKPL KLMVYNSESD SCREVTVTPN AAWGGEGSLG CGIGYGYLHR
210 220 230 240 250
IPTQPSSQYK KPPSASSPGT PAKTPQPNAF PLGAPPPWPI PQDSSGPELG
260 270 280 290 300
SRQSDYMEAL PQVPGGFMEE QLPGPGSPGH GTADYGGCLH SMEIPLQPPP
310 320 330 340 350
PVQRVMDPGF LDVSGMSLLD SNNTSVCPSL SSSSLLTPTA VSALGPEDIG
360 370 380 390 400
SSSSSHERGG EATWSGSEFE ISFPDSPGSQ AQVDHLPRLT LPDGLTSAAS
410 420 430 440 450
PEEGLSAELL EAQTEEPAHT ASLDCMAQTE GPAGQVQAAP DPEPGLCEGP

W
Length:451
Mass (Da):47,673
Last modified:January 23, 2007 - v4
Checksum:i5B38FADF2E255EA3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF015264 mRNA. Translation: AAB81355.2.
UniGeneiRn.144458.

Genome annotation databases

UCSCiRGD:621122. rat.

Similar proteinsi

Entry informationi

Entry nameiGORS1_RAT
AccessioniPrimary (citable) accession number: O35254
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: January 23, 2007
Last modified: November 22, 2017
This is version 117 of the entry and version 4 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families