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Protein

Golgi resident protein GCP60

Gene

ACBD3

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

Functioni

Involved in the maintenance of Golgi structure by interacting with giantin, affecting protein transport between the endoplasmic reticulum and Golgi. Involved in hormone-induced steroid biosynthesis in testicular Leydig cells (By similarity).By similarity1 Publication

GO - Molecular functioni

  • fatty-acyl-CoA binding Source: InterPro
  • protein kinase A regulatory subunit binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis

Enzyme and pathway databases

BioCyciZFISH:G66-32660-MONOMER.
ReactomeiR-HSA-432722. Golgi Associated Vesicle Biogenesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Golgi resident protein GCP60
Alternative name(s):
Acyl-CoA-binding domain-containing protein 3
Golgi complex-associated protein 1
Short name:
GOCAP1
Golgi phosphoprotein 1
Short name:
GOLPH1
PBR- and PKA-associated protein 7
Peripheral benzodiazepine receptor-associated protein PAP7
Cleaved into the following chain:
Gene namesi
Name:ACBD3
Synonyms:GCP60, GOCAP1, GOLPH1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:15453. ACBD3.

Subcellular locationi

GO - Cellular componenti

  • Golgi apparatus Source: HPA
  • Golgi membrane Source: UniProtKB-SubCell
  • integral component of membrane Source: InterPro
  • membrane Source: UniProtKB
  • mitochondrion Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane, Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi243K → A: No effect on PI4KB- and TBC1D22B-binding. 1 Publication1
Mutagenesisi244Q → A: No effect on PI4KB- and TBC1D22B-binding. 1 Publication1
Mutagenesisi245Q → A: No effect on PI4KB- and TBC1D22B-binding. 1 Publication1
Mutagenesisi246I → A: Partial loss of PI4KB- and TBC1D22B-binding. 1 Publication1
Mutagenesisi253Q → A: No effect on PI4KB- and TBC1D22B-binding. 1 Publication1
Mutagenesisi254T → A: No effect on PI4KB- and TBC1D22B-binding. 1 Publication1
Mutagenesisi256 – 258VQF → AAA: Loss of PI4KB-, TBC1D22A- and TBC1D22B-binding. 1 Publication3
Mutagenesisi257Q → A: Partial loss of PI4KB- and TBC1D22B-binding. 1 Publication1
Mutagenesisi258F → A: Differential effect on PI4KB- and TBC1D22B-binding, with PI4KB-binding being much more affected than TBC1D22B-binding. 1 Publication1
Mutagenesisi259Q → A: No effect on PI4KB- and TBC1D22B-binding. 1 Publication1
Mutagenesisi260Q → A: No effect on PI4KB- and TBC1D22B-binding. 1 Publication1
Mutagenesisi261Y → A: No effect on PI4KB- and TBC1D22B-binding. 1 Publication1
Mutagenesisi264 – 266QQY → AAA: No effect on PI4KB-, TBC1D22A- and TBC1D22B-binding. 1 Publication3
Mutagenesisi267 – 269PGN → AAA: Loss of PI4KB-, TBC1D22A- and TBC1D22B-binding. 1 Publication3
Mutagenesisi275I → A: No effect on PI4KB- and TBC1D22B-binding. 1 Publication1
Mutagenesisi276L → A: No effect on PI4KB- and TBC1D22B-binding. 1 Publication1
Mutagenesisi282 – 285EQHY → AAAA: Loss of PI4KB-, TBC1D22A- and TBC1D22B-binding. 1 Publication4
Mutagenesisi284H → A: Almost complete loss of PI4KB- and TBC1D22B-binding. 1 Publication1
Mutagenesisi285Y → A: Differential loss of PI4KB- and TBC1D22B-binding, with PI4KB-binding being much more affected than TBC1D22B-binding. 1 Publication1
Mutagenesisi286Q → A: No effect on PI4KB- and TBC1D22B-binding. 1 Publication1
Mutagenesisi287Q → A: No effect on PI4KB- and TBC1D22B-binding. 1 Publication1
Mutagenesisi288Y → A: Almost complete loss of PI4KB- and TBC1D22B-binding. 1 Publication1
Mutagenesisi344 – 345SS → AA: No effect on PI4KB-, TBC1D22A- and TBC1D22B-binding. 1 Publication2
Mutagenesisi414 – 416SYL → AAA: No effect on PI4KB-, TBC1D22A- and TBC1D22B-binding. 1 Publication3
Mutagenesisi417 – 420FWEF → AAAA: No effect on PI4KB-, TBC1D22A- and TBC1D22B-binding. 1 Publication4
Mutagenesisi433 – 435FEW → AAA: No effect on PI4KB-, TBC1D22A- and TBC1D22B-binding. 1 Publication3
Mutagenesisi494 – 496GSH → AAA: No effect on PI4KB-, TBC1D22A- and TBC1D22B-binding. 1 Publication3
Mutagenesisi511 – 513SYS → AAA: No effect on PI4KB-, TBC1D22A- and TBC1D22B-binding. 1 Publication3
Mutagenesisi511S → A: Partial loss of PI4KB- and TBC1D22B-binding. 1 Publication1

Organism-specific databases

DisGeNETi64746.
OpenTargetsiENSG00000182827.
PharmGKBiPA28803.

Polymorphism and mutation databases

BioMutaiACBD3.
DMDMi51316096.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004364491 – 528Golgi resident protein GCP60Add BLAST528
Initiator methionineiRemoved; alternateCombined sources1 Publication
ChainiPRO_00002140292 – 528Golgi resident protein GCP60, N-terminally processedAdd BLAST527

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanine; in Golgi resident protein GCP60, N-terminally processedCombined sources1
Modified residuei13PhosphoserineCombined sources1
Modified residuei18PhosphothreonineCombined sources1
Modified residuei20PhosphoserineCombined sources1
Modified residuei43PhosphoserineCombined sources1
Modified residuei47PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9H3P7.
MaxQBiQ9H3P7.
PaxDbiQ9H3P7.
PeptideAtlasiQ9H3P7.
PRIDEiQ9H3P7.

PTM databases

iPTMnetiQ9H3P7.
PhosphoSitePlusiQ9H3P7.
SwissPalmiQ9H3P7.

Expressioni

Tissue specificityi

Ubiquitous, with highest expression in testis and ovary.1 Publication

Gene expression databases

BgeeiENSG00000182827.
CleanExiHS_ACBD3.
ExpressionAtlasiQ9H3P7. baseline and differential.
GenevisibleiQ9H3P7. HS.

Organism-specific databases

HPAiHPA015594.

Interactioni

Subunit structurei

Interacts with the C-terminal cytoplasmic domain of giantin/GOLGB1 (PubMed:11590181). Interacts with PBR and PKA regulatory subunit RI-alpha. Does not interact with PKA regulatory subunit RI-beta nor PKA regulatory subunit RII-alpha (By similarity). Interacts with PI4KB, TBC1D22A AND TBC1D22B; interactions with PI4KB and with TBC1D22A and TBC1D22B are mutually exclusive. Interacts with C10ORF76 and RAB11B (PubMed:23572552).By similarity2 Publications
(Microbial infection) Interacts with 3A proteins from various picornaviruses, including hepatitis A virus, human parechovirus 1, and human klassevirus. Kobuviral (Aichi) 3A protein binding may compete the physiological interaction with TBC1D22A, while enteroviral (poliovirus) 3A protein does not seem to interfere.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
O9146421EBI-1791792,EBI-7587528From a different organism.
PI4KBQ9UBF84EBI-1791792,EBI-1053214
Ppm1lQ8BHN03EBI-1791792,EBI-7970002From a different organism.

GO - Molecular functioni

  • protein kinase A regulatory subunit binding Source: UniProtKB

Protein-protein interaction databases

BioGridi122262. 30 interactors.
DIPiDIP-40673N.
IntActiQ9H3P7. 15 interactors.
MINTiMINT-5003562.
STRINGi9606.ENSP00000355777.

Chemistry databases

BindingDBiQ9H3P7.

Structurei

Secondary structure

1528
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi243 – 265Combined sources23
Helixi270 – 304Combined sources35

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2N72NMR-A241-308[»]
2N73NMR-A241-308[»]
ProteinModelPortaliQ9H3P7.
SMRiQ9H3P7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini83 – 174ACBPROSITE-ProRule annotationAdd BLAST92
Domaini384 – 526GOLDPROSITE-ProRule annotationAdd BLAST143

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili174 – 257Sequence analysisAdd BLAST84

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi21 – 60Pro-richAdd BLAST40
Compositional biasi182 – 240Glu-richAdd BLAST59
Compositional biasi196 – 238Arg-richAdd BLAST43
Compositional biasi241 – 308Gln-richAdd BLAST68

Domaini

The GOLD domain is essential for giantin binding.

Sequence similaritiesi

Contains 1 ACB (acyl-CoA-binding) domain.PROSITE-ProRule annotation
Contains 1 GOLD domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG3878. Eukaryota.
ENOG410XS5V. LUCA.
GeneTreeiENSGT00530000063651.
HOVERGENiHBG051712.
InParanoidiQ9H3P7.
OMAiFGVFFEW.
OrthoDBiEOG091G0KJD.
PhylomeDBiQ9H3P7.
TreeFamiTF321667.

Family and domain databases

Gene3Di1.20.80.10. 1 hit.
InterProiIPR022408. Acyl-CoA-binding_prot_CS.
IPR000582. Acyl-CoA-binding_protein.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
IPR009038. GOLD_dom.
[Graphical view]
PfamiPF00887. ACBP. 1 hit.
PF13897. GOLD_2. 1 hit.
[Graphical view]
SUPFAMiSSF101576. SSF101576. 2 hits.
SSF47027. SSF47027. 1 hit.
PROSITEiPS00880. ACB_1. 1 hit.
PS51228. ACB_2. 1 hit.
PS50866. GOLD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9H3P7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAVLNAERL EVSVDGLTLS PDPEERPGAE GAPLLPPPLP PPSPPGSGRG
60 70 80 90 100
PGASGEQPEP GEAAAGGAAE EARRLEQRWG FGLEELYGLA LRFFKEKDGK
110 120 130 140 150
AFHPTYEEKL KLVALHKQVL MGPYNPDTCP EVGFFDVLGN DRRREWAALG
160 170 180 190 200
NMSKEDAMVE FVKLLNRCCH LFSTYVASHK IEKEEQEKKR KEEEERRRRE
210 220 230 240 250
EEERERLQKE EEKRRREEEE RLRREEEERR RIEEERLRLE QQKQQIMAAL
260 270 280 290 300
NSQTAVQFQQ YAAQQYPGNY EQQQILIRQL QEQHYQQYMQ QLYQVQLAQQ
310 320 330 340 350
QAALQKQQEV VVAGSSLPTS SKVNATVPSN MMSVNGQAKT HTDSSEKELE
360 370 380 390 400
PEAAEEALEN GPKESLPVIA APSMWTRPQI KDFKEKIQQD ADSVITVGRG
410 420 430 440 450
EVVTVRVPTH EEGSYLFWEF ATDNYDIGFG VYFEWTDSPN TAVSVHVSES
460 470 480 490 500
SDDDEEEEEN IGCEEKAKKN ANKPLLDEIV PVYRRDCHEE VYAGSHQYPG
510 520
RGVYLLKFDN SYSLWRSKSV YYRVYYTR
Length:528
Mass (Da):60,593
Last modified:January 23, 2007 - v4
Checksum:iB36EC550F8268FC2
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti93F → L in AAN60219 (Ref. 2) Curated1
Sequence conflicti230R → I in AAN60219 (Ref. 2) Curated1
Sequence conflicti265Q → R in AAN60219 (Ref. 2) Curated1
Sequence conflicti333S → P in AAN60219 (Ref. 2) Curated1
Sequence conflicti384 – 397KEKIQ…SVITV → QREDSAGCRFRDYS (Ref. 2) CuratedAdd BLAST14
Sequence conflicti425Y → C in AAN60219 (Ref. 2) Curated1
Sequence conflicti473K → R in AAH60792 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_019615187E → D.2 PublicationsCorresponds to variant rs2306120dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB043587 mRNA. Translation: BAB20592.2.
AY150218 mRNA. Translation: AAN60219.1.
AK025520 mRNA. Translation: BAB15159.1.
AK314468 mRNA. Translation: BAG37076.1.
AL592045 Genomic DNA. Translation: CAH71922.1.
CH471098 Genomic DNA. Translation: EAW69775.1.
BC034563 mRNA. Translation: AAH34563.2.
BC045533 mRNA. Translation: AAH45533.1.
BC060792 mRNA. Translation: AAH60792.1.
CCDSiCCDS1551.1.
RefSeqiNP_073572.2. NM_022735.3.
UniGeneiHs.520207.

Genome annotation databases

EnsembliENST00000366812; ENSP00000355777; ENSG00000182827.
GeneIDi64746.
KEGGihsa:64746.
UCSCiuc001hpy.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB043587 mRNA. Translation: BAB20592.2.
AY150218 mRNA. Translation: AAN60219.1.
AK025520 mRNA. Translation: BAB15159.1.
AK314468 mRNA. Translation: BAG37076.1.
AL592045 Genomic DNA. Translation: CAH71922.1.
CH471098 Genomic DNA. Translation: EAW69775.1.
BC034563 mRNA. Translation: AAH34563.2.
BC045533 mRNA. Translation: AAH45533.1.
BC060792 mRNA. Translation: AAH60792.1.
CCDSiCCDS1551.1.
RefSeqiNP_073572.2. NM_022735.3.
UniGeneiHs.520207.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2N72NMR-A241-308[»]
2N73NMR-A241-308[»]
ProteinModelPortaliQ9H3P7.
SMRiQ9H3P7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122262. 30 interactors.
DIPiDIP-40673N.
IntActiQ9H3P7. 15 interactors.
MINTiMINT-5003562.
STRINGi9606.ENSP00000355777.

Chemistry databases

BindingDBiQ9H3P7.

PTM databases

iPTMnetiQ9H3P7.
PhosphoSitePlusiQ9H3P7.
SwissPalmiQ9H3P7.

Polymorphism and mutation databases

BioMutaiACBD3.
DMDMi51316096.

Proteomic databases

EPDiQ9H3P7.
MaxQBiQ9H3P7.
PaxDbiQ9H3P7.
PeptideAtlasiQ9H3P7.
PRIDEiQ9H3P7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000366812; ENSP00000355777; ENSG00000182827.
GeneIDi64746.
KEGGihsa:64746.
UCSCiuc001hpy.4. human.

Organism-specific databases

CTDi64746.
DisGeNETi64746.
GeneCardsiACBD3.
H-InvDBHIX0159664.
HGNCiHGNC:15453. ACBD3.
HPAiHPA015594.
MIMi606809. gene.
neXtProtiNX_Q9H3P7.
OpenTargetsiENSG00000182827.
PharmGKBiPA28803.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3878. Eukaryota.
ENOG410XS5V. LUCA.
GeneTreeiENSGT00530000063651.
HOVERGENiHBG051712.
InParanoidiQ9H3P7.
OMAiFGVFFEW.
OrthoDBiEOG091G0KJD.
PhylomeDBiQ9H3P7.
TreeFamiTF321667.

Enzyme and pathway databases

BioCyciZFISH:G66-32660-MONOMER.
ReactomeiR-HSA-432722. Golgi Associated Vesicle Biogenesis.

Miscellaneous databases

ChiTaRSiACBD3. human.
GeneWikiiACBD3.
GenomeRNAii64746.
PROiQ9H3P7.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000182827.
CleanExiHS_ACBD3.
ExpressionAtlasiQ9H3P7. baseline and differential.
GenevisibleiQ9H3P7. HS.

Family and domain databases

Gene3Di1.20.80.10. 1 hit.
InterProiIPR022408. Acyl-CoA-binding_prot_CS.
IPR000582. Acyl-CoA-binding_protein.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
IPR009038. GOLD_dom.
[Graphical view]
PfamiPF00887. ACBP. 1 hit.
PF13897. GOLD_2. 1 hit.
[Graphical view]
SUPFAMiSSF101576. SSF101576. 2 hits.
SSF47027. SSF47027. 1 hit.
PROSITEiPS00880. ACB_1. 1 hit.
PS51228. ACB_2. 1 hit.
PS50866. GOLD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGCP60_HUMAN
AccessioniPrimary (citable) accession number: Q9H3P7
Secondary accession number(s): B2RB29
, Q5VTJ0, Q6P9F1, Q8IZC5, Q8N4D6, Q9H6U3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 136 of the entry and version 4 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

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

Documents

  1. Human chromosome 1
    Human chromosome 1: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.