Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Golgi phosphoprotein 3

Gene

GOLPH3

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

Functioni

Phosphatidylinositol-4-phosphate-binding protein that links Golgi membranes to the cytoskeleton and may participate in the tensile force required for vesicle budding from the Golgi. Thereby, may play a role in Golgi membrane trafficking and could indirectly give its flattened shape to the Golgi apparatus. May also bind to the coatomer to regulate Golgi membrane trafficking. May play a role in anterograde transport from the Golgi to the plasma membrane and regulate secretion. Has also been involved in the control of the localization of Golgi enzymes through interaction with their cytoplasmic part. May play an indirect role in cell migration. Has also been involved in the modulation of mTOR signaling. May also be involved in the regulation of mitochondrial lipids biosynthesis.7 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei81 – 811PtdIns4PCurated
Binding sitei90 – 901PtdIns4PCurated
Binding sitei171 – 1711PtdIns4PCurated
Binding sitei174 – 1741PtdIns4PCurated

GO - Molecular functioni

  • enzyme binding Source: UniProtKB
  • phosphatidylinositol-4-phosphate binding Source: UniProtKB

GO - Biological processi

  • asymmetric Golgi ribbon formation Source: CACAO
  • cell adhesion molecule production Source: UniProtKB
  • cell migration Source: UniProtKB
  • cell proliferation Source: UniProtKB
  • gene expression Source: UniProtKB
  • glycoprotein biosynthetic process Source: UniProtKB
  • Golgi organization Source: UniProtKB
  • Golgi ribbon formation Source: CACAO
  • Golgi to plasma membrane protein transport Source: UniProtKB
  • Golgi vesicle budding Source: UniProtKB
  • lamellipodium assembly Source: UniProtKB
  • leukocyte tethering or rolling Source: UniProtKB
  • negative regulation of apoptotic process Source: CACAO
  • positive regulation of protein secretion Source: UniProtKB
  • positive regulation of TOR signaling Source: UniProtKB
  • protein retention in Golgi apparatus Source: UniProtKB
  • protein secretion Source: UniProtKB
  • regulation of mitochondrion organization Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Golgi phosphoprotein 3
Alternative name(s):
Coat protein GPP34
Mitochondrial DNA absence factor
Short name:
MIDAS
Gene namesi
Name:GOLPH3
Synonyms:GPP34
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:15452. GOLPH3.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • endosome Source: UniProtKB-SubCell
  • Golgi apparatus Source: CACAO
  • Golgi cisterna Source: UniProtKB
  • Golgi cisterna membrane Source: UniProtKB-SubCell
  • intracellular membrane-bounded organelle Source: HPA
  • mitochondrial intermembrane space Source: UniProtKB-SubCell
  • mitochondrion Source: UniProtKB
  • nucleoplasm Source: HPA
  • plasma membrane Source: UniProtKB-SubCell
  • trans-Golgi network Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endosome, Golgi apparatus, Membrane, Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi7 – 71R → A: Altered binding to coatomer. 1 Publication
Mutagenesisi14 – 152RR → AA: Loss of binding to coatomer. 1 Publication
Mutagenesisi81 – 811W → A: Abolishes phosphoinositide binding and localization to the Golgi apparatus; when associated with A-90. 1 Publication
Mutagenesisi90 – 901R → A: Abolishes phosphoinositide binding and localization to the Golgi apparatus; when associated with A-81. 2 Publications
Mutagenesisi90 – 901R → L: Loss of function in vesicle budding, abolishes phosphoinositide binding and localization to the Golgi apparatus. 2 Publications
Mutagenesisi171 – 1711R → A or L: Abolishes phosphoinositide binding and localization to the Golgi apparatus; when associated with A-174. 2 Publications
Mutagenesisi174 – 1741R → A: Abolishes phosphoinositide binding and localization to the Golgi apparatus; when associated with A-171 or L-171. 2 Publications

Organism-specific databases

PharmGKBiPA28812.

Polymorphism and mutation databases

BioMutaiGOLPH3.
DMDMi50400651.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 298298Golgi phosphoprotein 3PRO_0000123819Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei35 – 351PhosphoserineCombined sources
Modified residuei36 – 361PhosphoserineCombined sources
Disulfide bondi84 ↔ 1081 Publication

Post-translational modificationi

Phosphorylated.By similarity

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

EPDiQ9H4A6.
MaxQBiQ9H4A6.
PaxDbiQ9H4A6.
PRIDEiQ9H4A6.

PTM databases

iPTMnetiQ9H4A6.
PhosphoSiteiQ9H4A6.

Expressioni

Tissue specificityi

Detected in muscle fibers of patients with mitochondrial diseases; not detected in normal muscle fibers.

Inductioni

Activated by depletion of mitochondrial DNA.

Gene expression databases

BgeeiQ9H4A6.
CleanExiHS_GOLPH3.
ExpressionAtlasiQ9H4A6. baseline and differential.
GenevisibleiQ9H4A6. HS.

Organism-specific databases

HPAiHPA044564.
HPA055841.

Interactioni

Subunit structurei

Homodimer. Interacts with the coatomer complex. Interacts with MYO18A; the interaction is direct and may link Golgi membranes to the actin cytoskeleton. Interacts with GCNT1; may control its retention in the Golgi. Interacts with VPS35.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ARL6IP1Q150413EBI-2465479,EBI-714543
GCNT1Q027426EBI-2465479,EBI-8766035
MYO18AQ926146EBI-2465479,EBI-949059
vprP125203EBI-2465479,EBI-6164519From a different organism.
XRCC5P130102EBI-2465479,EBI-357997

GO - Molecular functioni

  • enzyme binding Source: UniProtKB

Protein-protein interaction databases

BioGridi122048. 33 interactions.
IntActiQ9H4A6. 9 interactions.
MINTiMINT-5001986.
STRINGi9606.ENSP00000265070.

Structurei

Secondary structure

1
298
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi62 – 698Combined sources
Beta strandi73 – 753Combined sources
Helixi83 – 9917Combined sources
Beta strandi102 – 1054Combined sources
Turni110 – 1123Combined sources
Turni115 – 1173Combined sources
Beta strandi118 – 1236Combined sources
Helixi131 – 14212Combined sources
Helixi149 – 1568Combined sources
Helixi163 – 1664Combined sources
Helixi173 – 18311Combined sources
Beta strandi190 – 1945Combined sources
Beta strandi197 – 2015Combined sources
Helixi207 – 22014Combined sources
Turni221 – 2244Combined sources
Helixi229 – 2313Combined sources
Helixi234 – 24512Combined sources
Helixi250 – 2534Combined sources
Helixi258 – 27316Combined sources
Helixi276 – 2794Combined sources
Beta strandi282 – 2843Combined sources
Helixi287 – 2959Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3KN1X-ray2.90A52-298[»]
ProteinModelPortaliQ9H4A6.
SMRiQ9H4A6. Positions 59-297.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9H4A6.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni190 – 20112Beta-hairpin required for oligomerizationBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi48 – 514Poly-Asp

Sequence similaritiesi

Belongs to the GOLPH3/VPS74 family.Curated

Phylogenomic databases

eggNOGiKOG3983. Eukaryota.
ENOG410XRT6. LUCA.
GeneTreeiENSGT00390000007153.
HOGENOMiHOG000209848.
HOVERGENiHBG059607.
InParanoidiQ9H4A6.
KOiK15620.
OMAiTTHPLND.
OrthoDBiEOG7ZKSBV.
PhylomeDBiQ9H4A6.
TreeFamiTF314360.

Family and domain databases

InterProiIPR008628. GPP34.
[Graphical view]
PfamiPF05719. GPP34. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9H4A6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTSLTQRSSG LVQRRTEASR NAADKERAAG GGAGSSEDDA QSRRDEQDDD
60 70 80 90 100
DKGDSKETRL TLMEEVLLLG LKDREGYTSF WNDCISSGLR GCMLIELALR
110 120 130 140 150
GRLQLEACGM RRKSLLTRKV ICKSDAPTGD VLLDEALKHV KETQPPETVQ
160 170 180 190 200
NWIELLSGET WNPLKLHYQL RNVRERLAKN LVEKGVLTTE KQNFLLFDMT
210 220 230 240 250
THPLTNNNIK QRLIKKVQEA VLDKWVNDPH RMDRRLLALI YLAHASDVLE
260 270 280 290
NAFAPLLDEQ YDLATKRVRQ LLDLDPEVEC LKANTNEVLW AVVAAFTK
Length:298
Mass (Da):33,811
Last modified:March 1, 2001 - v1
Checksum:i34FAD78155CC214A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ296152 mRNA. Translation: CAC13124.1.
AK075156 mRNA. Translation: BAC11438.1.
AL356292 Genomic DNA. No translation available.
AL356356 Genomic DNA. No translation available.
BC012123 mRNA. Translation: AAH12123.1.
BC033725 mRNA. Translation: AAH33725.1.
BC063586 mRNA. Translation: AAH63586.1.
AL133078 mRNA. Translation: CAB61398.1.
CCDSiCCDS3896.1.
PIRiT42677.
RefSeqiNP_071413.1. NM_022130.3.
UniGeneiHs.408909.

Genome annotation databases

EnsembliENST00000265070; ENSP00000265070; ENSG00000113384.
GeneIDi64083.
KEGGihsa:64083.
UCSCiuc003jhp.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ296152 mRNA. Translation: CAC13124.1.
AK075156 mRNA. Translation: BAC11438.1.
AL356292 Genomic DNA. No translation available.
AL356356 Genomic DNA. No translation available.
BC012123 mRNA. Translation: AAH12123.1.
BC033725 mRNA. Translation: AAH33725.1.
BC063586 mRNA. Translation: AAH63586.1.
AL133078 mRNA. Translation: CAB61398.1.
CCDSiCCDS3896.1.
PIRiT42677.
RefSeqiNP_071413.1. NM_022130.3.
UniGeneiHs.408909.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3KN1X-ray2.90A52-298[»]
ProteinModelPortaliQ9H4A6.
SMRiQ9H4A6. Positions 59-297.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122048. 33 interactions.
IntActiQ9H4A6. 9 interactions.
MINTiMINT-5001986.
STRINGi9606.ENSP00000265070.

PTM databases

iPTMnetiQ9H4A6.
PhosphoSiteiQ9H4A6.

Polymorphism and mutation databases

BioMutaiGOLPH3.
DMDMi50400651.

Proteomic databases

EPDiQ9H4A6.
MaxQBiQ9H4A6.
PaxDbiQ9H4A6.
PRIDEiQ9H4A6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000265070; ENSP00000265070; ENSG00000113384.
GeneIDi64083.
KEGGihsa:64083.
UCSCiuc003jhp.2. human.

Organism-specific databases

CTDi64083.
GeneCardsiGOLPH3.
H-InvDBHIX0032097.
HGNCiHGNC:15452. GOLPH3.
HPAiHPA044564.
HPA055841.
MIMi612207. gene.
neXtProtiNX_Q9H4A6.
PharmGKBiPA28812.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3983. Eukaryota.
ENOG410XRT6. LUCA.
GeneTreeiENSGT00390000007153.
HOGENOMiHOG000209848.
HOVERGENiHBG059607.
InParanoidiQ9H4A6.
KOiK15620.
OMAiTTHPLND.
OrthoDBiEOG7ZKSBV.
PhylomeDBiQ9H4A6.
TreeFamiTF314360.

Miscellaneous databases

ChiTaRSiGOLPH3. human.
EvolutionaryTraceiQ9H4A6.
GenomeRNAii64083.
NextBioi65876.
PROiQ9H4A6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H4A6.
CleanExiHS_GOLPH3.
ExpressionAtlasiQ9H4A6. baseline and differential.
GenevisibleiQ9H4A6. HS.

Family and domain databases

InterProiIPR008628. GPP34.
[Graphical view]
PfamiPF05719. GPP34. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
  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].
    Tissue: Placenta.
  3. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    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].
    Tissue: Eye, Placenta and Prostate.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 91-298.
    Tissue: Testis.
  6. "MIDAS/GPP34, a nuclear gene product, regulates total mitochondrial mass in response to mitochondrial dysfunction."
    Nakashima-Kamimura N., Asoh S., Ishibashi Y., Mukai Y., Shidara Y., Oda H., Munakata K., Goto Y., Ohta S.
    J. Cell Sci. 118:5357-5367(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  7. "GOLPH3 bridges phosphatidylinositol-4- phosphate and actomyosin to stretch and shape the Golgi to promote budding."
    Dippold H.C., Ng M.M., Farber-Katz S.E., Lee S.K., Kerr M.L., Peterman M.C., Sim R., Wiharto P.A., Galbraith K.A., Madhavarapu S., Fuchs G.J., Meerloo T., Farquhar M.G., Zhou H., Field S.J.
    Cell 139:337-351(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN GOLGI MEMBRANE BUDDING, INTERACTION WITH MYO18A, LIPID-BINDING, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-90; ARG-171 AND ARG-174.
  8. Cited for: FUNCTION IN MTOR SIGNALING, SUBCELLULAR LOCATION, INTERACTION WITH VPS35.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Role of phosphatidylinositol 4-phosphate (PI4P) and its binding protein GOLPH3 in hepatitis C virus secretion."
    Bishe B., Syed G.H., Field S.J., Siddiqui A.
    J. Biol. Chem. 287:27637-27647(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN SECRETION.
  12. "Golgi phosphoprotein 3 determines cell binding properties under dynamic flow by controlling Golgi localization of core 2 N-acetylglucosaminyltransferase 1."
    Ali M.F., Chachadi V.B., Petrosyan A., Cheng P.W.
    J. Biol. Chem. 287:39564-39577(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH GCNT1, SUBCELLULAR LOCATION.
  13. "A conserved N-terminal arginine-motif in GOLPH3-family proteins mediates binding to coatomer."
    Tu L., Chen L., Banfield D.K.
    Traffic 13:1496-1507(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ARG-7 AND 14-ARG--ARG-15, COATOMER-BINDING.
  14. "GOLPH3 regulates the migration and invasion of glioma cells though RhoA."
    Zhou X., Zhan W., Bian W., Hua L., Shi Q., Xie S., Yang D., Li Y., Zhang X., Liu G., Yu R.
    Biochem. Biophys. Res. Commun. 433:338-344(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CELL MIGRATION.
  15. "Functional Characterization of Human Myosin-18A and its Interaction with F-actin and GOLPH3."
    Taft M.H., Behrmann E., Munske-Weidemann L.C., Thiel C., Raunser S., Manstein D.J.
    J. Biol. Chem. 288:30029-30041(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MYO18A.
  16. "GOLPH3L antagonizes GOLPH3 to determine Golgi morphology."
    Ng M.M., Dippold H.C., Buschman M.D., Noakes C.J., Field S.J.
    Mol. Biol. Cell 24:796-808(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MYO18A, SUBCELLULAR LOCATION, LIPID-BINDING.
  17. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35 AND SER-36, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "PtdIns4P recognition by Vps74/GOLPH3 links PtdIns 4-kinase signaling to retrograde Golgi trafficking."
    Wood C.S., Schmitz K.R., Bessman N.J., Setty T.G., Ferguson K.M., Burd C.G.
    J. Cell Biol. 187:967-975(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 52-298, LIPID-BINDING, OLIGOMERIZATION, DISULFIDE BOND, MUTAGENESIS OF TRP-81; ARG-90; ARG-171 AND ARG-174.

Entry informationi

Entry nameiGOLP3_HUMAN
AccessioniPrimary (citable) accession number: Q9H4A6
Secondary accession number(s): Q9UIW5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: March 1, 2001
Last modified: April 13, 2016
This is version 110 of the entry and version 1 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

Miscellaneous

Modulates sensitivity to rapamycin. Tumors expressing this protein are more sensitive to rapamycin in vivo.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.