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Protein

Golgin subfamily A member 2

Gene

Golga2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Peripheral membrane component of the cis-Golgi stack that acts as a membrane skeleton that maintains the structure of the Golgi apparatus, and as a vesicle thether that facilitates vesicle fusion to the Golgi membrane (PubMed:8557739, PubMed:9150144, PubMed:20197635). Together with p115/USO1 and STX5, involved in vesicle tethering and fusion at the cis-Golgi membrane to maintain the stacked and inter-connected structure of the Golgi apparatus (PubMed:10679020, PubMed:11035033, PubMed:18167358). Plays a central role in mitotic Golgi disassembly: phosphorylation at Ser-37 by CDK1 at the onset of mitosis inhibits the interaction with p115/USO1, preventing tethering of COPI vesicles and thereby inhibiting transport through the Golgi apparatus during mitosis (PubMed:9753325). Also plays a key role in spindle pole assembly and centrosome organization (PubMed:26165940). Promotes the mitotic spindle pole assembly by activating the spindle assembly factor TPX2 to nucleate microtubules around the Golgi and capture them to couple mitotic membranes to the spindle: upon phosphorylation at the onset of mitosis, GOLGA2 interacts with importin-alpha via the nuclear localization signal region, leading to recruit importin-alpha to the Golgi membranes and liberate the spindle assembly factor TPX2 from importin-alpha. TPX2 then activates AURKA kinase and stimulates local microtubule nucleation. Upon filament assembly, nascent microtubules are further captured by GOLGA2, thus linking Golgi membranes to the spindle (By similarity). Regulates the meiotic spindle pole assembly, probably via the same mechanism (By similarity). Also regulates the centrosome organization (By similarity). Also required for the Golgi ribbon formation and glycosylation of membrane and secretory proteins (By similarity).1 PublicationBy similarity7 Publications

GO - Molecular functioni

  • importin-alpha family protein binding Source: UniProtKB
  • microtubule binding Source: UniProtKB
  • protein complex binding Source: RGD
  • protein kinase binding Source: UniProtKB

GO - Biological processi

  • asymmetric cell division Source: UniProtKB
  • centrosome organization Source: UniProtKB
  • ER to Golgi vesicle-mediated transport Source: UniProtKB
  • Golgi disassembly Source: UniProtKB
  • Golgi ribbon formation Source: UniProtKB
  • microtubule nucleation Source: UniProtKB
  • mitotic spindle assembly Source: UniProtKB
  • protein glycosylation Source: UniProtKB
  • protein homotetramerization Source: UniProtKB
  • spindle assembly Source: UniProtKB
  • spindle assembly involved in meiosis Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Enzyme and pathway databases

ReactomeiR-RNO-162658. Golgi Cisternae Pericentriolar Stack Reorganization.
R-RNO-204005. COPII (Coat Protein 2) Mediated Vesicle Transport.
R-RNO-6807878. COPI-mediated anterograde transport.

Names & Taxonomyi

Protein namesi
Recommended name:
Golgin subfamily A member 2Curated
Alternative name(s):
130 kDa cis-Golgi matrix protein1 Publication
Short name:
GM1301 Publication
Gene namesi
Name:Golga2Imported
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi620282. Golga2.

Subcellular locationi

GO - Cellular componenti

  • cis-Golgi network Source: RGD
  • cytoplasm Source: RGD
  • Golgi apparatus Source: MGI
  • Golgi cis cisterna Source: RGD
  • Golgi cisterna membrane Source: UniProtKB
  • Golgi membrane Source: Reactome
  • microtubule Source: UniProtKB-KW
  • mitotic spindle Source: UniProtKB
  • neuronal cell body Source: RGD
  • protein complex Source: RGD
  • spindle pole Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Golgi apparatus, Membrane, Microtubule

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi37 – 371S → A: Constitutive interaction with p115/USO1; under mitotic as well as interphase conditions. 1 Publication
Mutagenesisi37 – 371S → D: Phosphomimetic mutant that strongly reduces interaction with p115/USO1. 1 Publication
Mutagenesisi55 – 551S → A: Does not affect interaction with p115/USO1. 1 Publication
Mutagenesisi94 – 941S → A: Does not affect interaction with p115/USO1. 1 Publication
Mutagenesisi988 – 9881D → A: Does not affect with GORASP1/GRASP65. 1 Publication
Mutagenesisi989 – 9891E → A: Does not affect with GORASP1/GRASP65. 1 Publication
Mutagenesisi990 – 9901N → A: Strongly impairs interaction with GORASP1/GRASP65. 1 Publication
Mutagenesisi991 – 9911D → A: Strongly impairs interaction with GORASP1/GRASP65. 1 Publication
Mutagenesisi992 – 9921E → A: Does not affect with GORASP1/GRASP65. 1 Publication
Mutagenesisi993 – 9931V → A: Does not affect with GORASP1/GRASP65. 1 Publication
Mutagenesisi994 – 9941K → A: Does not affect with GORASP1/GRASP65. 1 Publication
Mutagenesisi995 – 9951I → A: Strongly impairs interaction with GORASP1/GRASP65. 1 Publication
Mutagenesisi996 – 9961M → A: Strongly impairs interaction with GORASP1/GRASP65. 1 Publication
Mutagenesisi997 – 9971V → A: Impairs interaction with GORASP1/GRASP65. 1 Publication
Mutagenesisi998 – 9981I → A: Impairs interaction with GORASP1/GRASP65. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 998998Golgin subfamily A member 2PRO_0000190056Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei18 – 181Omega-N-methylated arginineBy similarity
Modified residuei30 – 301Dimethylated arginineBy similarity
Modified residuei37 – 371Phosphoserine; by CDK13 Publications
Modified residuei273 – 2731PhosphoserineBy similarity
Modified residuei438 – 4381PhosphoserineBy similarity
Modified residuei697 – 6971PhosphoserineBy similarity
Modified residuei933 – 9331PhosphoserineBy similarity
Modified residuei977 – 9771PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated at Ser-37 by CDK1 at the onset of mitosis, inhibiting the interaction with p115/USO1 and triggering Golgi disassembly (PubMed:9150144, PubMed:9753325). A report however suggests that Golgi disassembly is independent of phosphorylation at Ser-37 (PubMed:20699666). Phosphorylated at Ser-37 in prophase as the Golgi complex starts to break down, and remains phosphorylated during further breakdown and partitioning of the Golgi fragments in metaphase and anaphase. In telophase, GM130 is dephosphorylated by PP2A as the Golgi fragments start to reassemble (PubMed:10769027).4 Publications
Cleaved by caspases at the onset of apoptosis.By similarity
Methylation by PRMT5 is required for Golgi ribbon formation.By similarity

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

PaxDbiQ62839.
PRIDEiQ62839.

PTM databases

iPTMnetiQ62839.
PhosphoSiteiQ62839.

Interactioni

Subunit structurei

Homotetramer; forms a parallel homotetramer with a flexible rod-like structure with I- and Y-shaped conformations (PubMed:25787021). Interacts with RAB1B that has been activated by GTP-binding (PubMed:18167358). Interacts with p115/USO1; interaction with p115/USO1 inhibits interaction with STX5 and/or RAB1B (PubMed:9150144, PubMed:9753325, PubMed:10744704, PubMed:10769027, PubMed:18167358). Interacts with GORASP1/GRASP65 (PubMed:9346242, PubMed:9628863). Interacts with STX5 (PubMed:18167358). Interacts with ZFPL1 (By similarity). Interacts with AKAP450/AKAP9; leading to recruit AKAP450/AKAP9 to the cis-Golgi (By similarity).By similarity8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Gorasp1O352542EBI-618335,EBI-4422879
STK25O005062EBI-618335,EBI-618295From a different organism.
Zfpl1Q9DB4314EBI-618335,EBI-7836139From a different organism.

GO - Molecular functioni

  • importin-alpha family protein binding Source: UniProtKB
  • microtubule binding Source: UniProtKB
  • protein complex binding Source: RGD
  • protein kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi249112. 1 interaction.
IntActiQ62839. 20 interactions.
MINTiMINT-4568392.
STRINGi10116.ENSRNOP00000016341.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 8686Interaction with p115/USO11 PublicationAdd
BLAST
Regioni988 – 99811Interaction with GORASP1/GRASP651 PublicationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili147 – 894748Sequence analysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi26 – 4924Nuclear localization signalBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi45 – 517Poly-Lys
Compositional biasi350 – 695346Gln-richAdd
BLAST
Compositional biasi449 – 4557Poly-Pro

Domaini

Extended rod-like protein with coiled-coil domains.1 Publication
The nuclear localization signal (cNLS) mediates interaction with importin-alpha, recruiting importin-alpha to the Golgi membrane and liberating TPX2.By similarity

Sequence similaritiesi

Belongs to the GOLGA2 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410INYK. Eukaryota.
ENOG4111MFD. LUCA.
HOGENOMiHOG000218631.
HOVERGENiHBG051752.
InParanoidiQ62839.
OrthoDBiEOG71P29T.

Family and domain databases

InterProiIPR024858. Golgin_A.
[Graphical view]
PfamiPF15070. GOLGA2L5. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q62839-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWPPRFPPPR PGMSEETRQS KLAAAKKKLR EYQQKNSPGV PAGAKKKKKI
60 70 80 90 100
KNGHSPERTS ASDCQSAENV PTDHTAPAPP STAAATMFLG VVPSPDADLI
110 120 130 140 150
QSHDAGNCSN LMEETKTFSS TESLRQLSQQ LNGLVSESTS YINGEGLTSS
160 170 180 190 200
NMKELESRYQ ELAVALDSSY VTNKQLSSTI EELKQQNQDT LDQLEKEKKD
210 220 230 240 250
YQQKLAKEQG ALREQLQVHI QTIGILVSEK AELQTALAHT QQAARQKAGE
260 270 280 290 300
SEDLASRLQS SRQRVGELER TLSTVSTQQK QADRYNKDLT KERDALKLEL
310 320 330 340 350
YKNGKSNEDL RQQNSELEEK LRVLVAEKAA AQLGAEELQK KLEMSELLLQ
360 370 380 390 400
QFSSQSEASG SNEQLQQAME ERAQLESHVG QLMESLKQLQ VERDQYAENL
410 420 430 440 450
KGESAMWQQR VQQMAEQVHA LKEEKEQRES QVQELEASLA ELRSQMEEPP
460 470 480 490 500
PPEPPTGPSE AEERLQGEVE QLQKELEGLT GQLRAQVQDN ESLSHLNREQ
510 520 530 540 550
EGRLLELERE AQHWSEQAEE RKQILESMQS DRTTISRALS QNRELKEQLA
560 570 580 590 600
ELQNGFVRLT NENMEITSAL QSEQHVKKEL ARKLGELQER LGELKETVEL
610 620 630 640 650
KSQEAQGLQE QRDQCLSHLQ QYAAAYQQHL TAYEQLTSEK EALHKQLLLQ
660 670 680 690 700
TQLMDQLQHE EVQGKMAAEM ARQELQEAQE RLKASSQENQ QLQAQLSLLV
710 720 730 740 750
LPGEDMDQEE QDEEVPQPSL TIPEDLVSRE AMVAFCNAAI ARAEEEQARL
760 770 780 790 800
RVQLREQKAR CRSLAHLAAP VQSKLEKEAV VPRDMGDSVS EESNQALHVA
810 820 830 840 850
MEKLQNRFLE VMQEKVELKE RVEELEHCCI QLSGETDTIG EYIALYQNQR
860 870 880 890 900
AVLKARHLEK EEYISRLAQD KEEMKVKLLE LQELVLRLVN ERNEWQGKFL
910 920 930 940 950
AVSQNPADVP APVPTGSQEF GAADQQGDLR EVSLADDTEP AQGEAGVPAP
960 970 980 990
QENPTAQQIM QLLREIQNPQ ERPGLGSNPC IPFFYRADEN DEVKIMVI
Length:998
Mass (Da):112,872
Last modified:October 14, 2015 - v4
Checksum:i3AA8CBC61F98A6A4
GO

Sequence cautioni

The sequence AAB53335.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti112 – 1121M → L in AAB53335 (PubMed:8557739).Curated
Sequence conflicti504 – 5041L → M in AAB53335 (PubMed:8557739).Curated
Sequence conflicti806 – 8061N → S in AAB53335 (PubMed:8557739).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U35022 mRNA. Translation: AAB53335.2. Different initiation.
AABR07051438 Genomic DNA. No translation available.
AABR07051439 Genomic DNA. No translation available.
PIRiT10754.
RefSeqiNP_072118.2. NM_022596.2.
XP_006234060.1. XM_006233998.2.
UniGeneiRn.6165.

Genome annotation databases

GeneIDi64528.
KEGGirno:64528.
UCSCiRGD:620282. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U35022 mRNA. Translation: AAB53335.2. Different initiation.
AABR07051438 Genomic DNA. No translation available.
AABR07051439 Genomic DNA. No translation available.
PIRiT10754.
RefSeqiNP_072118.2. NM_022596.2.
XP_006234060.1. XM_006233998.2.
UniGeneiRn.6165.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi249112. 1 interaction.
IntActiQ62839. 20 interactions.
MINTiMINT-4568392.
STRINGi10116.ENSRNOP00000016341.

PTM databases

iPTMnetiQ62839.
PhosphoSiteiQ62839.

Proteomic databases

PaxDbiQ62839.
PRIDEiQ62839.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi64528.
KEGGirno:64528.
UCSCiRGD:620282. rat.

Organism-specific databases

CTDi2801.
RGDi620282. Golga2.

Phylogenomic databases

eggNOGiENOG410INYK. Eukaryota.
ENOG4111MFD. LUCA.
HOGENOMiHOG000218631.
HOVERGENiHBG051752.
InParanoidiQ62839.
OrthoDBiEOG71P29T.

Enzyme and pathway databases

ReactomeiR-RNO-162658. Golgi Cisternae Pericentriolar Stack Reorganization.
R-RNO-204005. COPII (Coat Protein 2) Mediated Vesicle Transport.
R-RNO-6807878. COPI-mediated anterograde transport.

Miscellaneous databases

NextBioi35577170.
PROiQ62839.

Family and domain databases

InterProiIPR024858. Golgin_A.
[Graphical view]
PfamiPF15070. GOLGA2L5. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 87-998, FUNCTION, SUBCELLULAR LOCATION, DOMAIN.
    Strain: Sprague-Dawley.
  2. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], IDENTIFICATION.
    Strain: Brown Norway.
  3. "The vesicle docking protein p115 binds GM130, a cis-Golgi matrix protein, in a mitotically regulated manner."
    Nakamura N., Lowe M., Levine T.P., Rabouille C., Warren G.
    Cell 89:445-455(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH USO1, PHOSPHORYLATION.
    Strain: Sprague-Dawley.
  4. Lubec G., Kang S.U., Lubec S.
    Submitted (SEP-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 175-184 AND 199-207, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain.
  5. "GRASP65, a protein involved in the stacking of Golgi cisternae."
    Barr F.A., Puype M., Vandekerckhove J., Warren G.
    Cell 91:253-262(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GORASP1.
  6. "Cdc2 kinase directly phosphorylates the cis-Golgi matrix protein GM130 and is required for Golgi fragmentation in mitosis."
    Lowe M., Rabouille C., Nakamura N., Watson R., Jackman M., Jamsa E., Rahman D., Pappin D.J.C., Warren G.
    Cell 94:783-793(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT SER-37, INTERACTION WITH USO1, MUTAGENESIS OF SER-37; SER-55 AND SER-94.
  7. "Mapping the interaction between GRASP65 and GM130, components of a protein complex involved in the stacking of Golgi cisternae."
    Barr F.A., Nakamura N., Warren G.
    EMBO J. 17:3258-3268(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GORASP1, MUTAGENESIS OF ASP-988; GLU-989; ASN-990; ASP-991; GLU-992; VAL-993; LYS-994; ILE-995; MET-996; VAL-997 AND ILE-998.
  8. "Binding relationships of membrane tethering components. The giantin N terminus and the GM130 N terminus compete for binding to the p115 C terminus."
    Linstedt A.D., Jesch S.A., Mehta A., Lee T.H., Garcia-Mata R., Nelson D.S., Sztul E.
    J. Biol. Chem. 275:10196-10201(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH USO1.
  9. "The mitotic phosphorylation cycle of the cis-Golgi matrix protein GM130."
    Lowe M., Gonatas N.K., Warren G.
    J. Cell Biol. 149:341-356(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH USO1, PHOSPHORYLATION AT SER-37.
  10. "The role of the tethering proteins p115 and GM130 in transport through the Golgi apparatus in vivo."
    Seemann J., Jokitalo E.J., Warren G.
    Mol. Biol. Cell 11:635-645(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "The p115-interactive proteins GM130 and giantin participate in endoplasmic reticulum-Golgi traffic."
    Alvarez C., Garcia-Mata R., Hauri H.P., Sztul E.
    J. Biol. Chem. 276:2693-2700(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "Countercurrent distribution of two distinct SNARE complexes mediating transport within the Golgi stack."
    Volchuk A., Ravazzola M., Perrelet A., Eng W.S., Di Liberto M., Varlamov O., Fukasawa M., Engel T., Sollner T.H., Rothman J.E., Orci L.
    Mol. Biol. Cell 15:1506-1518(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  13. "Coordination of golgin tethering and SNARE assembly: GM130 binds syntaxin 5 in a p115-regulated manner."
    Diao A., Frost L., Morohashi Y., Lowe M.
    J. Biol. Chem. 283:6957-6967(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH STX5; USO1 AND RAB1B.
  14. "Mitotic Golgi vesiculation involves mechanisms independent of Ser25 phosphorylation of GM130."
    Sundaramoorthy S., Goh J.B., Rafee S., Murata-Hori M.
    Cell Cycle 9:3100-3105(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-37.
  15. "Emerging new roles of GM130, a cis-Golgi matrix protein, in higher order cell functions."
    Nakamura N.
    J. Pharmacol. Sci. 112:255-264(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  16. "GM130 is a parallel tetramer with a flexible rod-like structure and N-terminally open (Y-shaped) and closed (I-shaped) conformations."
    Ishida R., Yamamoto A., Nakayama K., Sohda M., Misumi Y., Yasunaga T., Nakamura N.
    FEBS J. 282:2232-2244(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  17. "GM130 regulates Golgi-derived spindle assembly by activating TPX2 and capturing microtubules."
    Wei J.H., Zhang Z.C., Wynn R.M., Seemann J.
    Cell 162:287-299(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiGOGA2_RAT
AccessioniPrimary (citable) accession number: Q62839
Secondary accession number(s): F1LSS0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 14, 2015
Last modified: April 13, 2016
This is version 119 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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 one 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.