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Q9UJY5

- GGA1_HUMAN

UniProt

Q9UJY5 - GGA1_HUMAN

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Protein

ADP-ribosylation factor-binding protein GGA1

Gene

GGA1

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

Functioni

Plays a role in protein sorting and trafficking between the trans-Golgi network (TGN) and endosomes. Mediates the ARF-dependent recruitment of clathrin to the TGN and binds ubiquitinated proteins and membrane cargo molecules with a cytosolic acidic cluster-dileucine (AC-LL) motif.1 Publication

GO - Biological processi

  1. intracellular protein transport Source: UniProtKB
  2. positive regulation of protein catabolic process Source: Ensembl
  3. vesicle-mediated transport Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
ADP-ribosylation factor-binding protein GGA1
Alternative name(s):
Gamma-adaptin-related protein 1
Golgi-localized, gamma ear-containing, ARF-binding protein 1
Gene namesi
Name:GGA1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:17842. GGA1.

Subcellular locationi

GO - Cellular componenti

  1. clathrin adaptor complex Source: InterPro
  2. endosome Source: UniProtKB-KW
  3. Golgi apparatus Source: UniProtKB
  4. intracellular membrane-bounded organelle Source: HPA
  5. membrane Source: UniProtKB
  6. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Endosome, Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi92 – 921N → A: Abolishes interaction with IGF2R. 1 Publication
Mutagenesisi182 – 1821L → A: Abolishes interaction with ARF1, UBC and TSG101. 1 Publication
Mutagenesisi194 – 1941N → A: Abolishes interaction with ARF1 and RABEP1. 1 Publication
Mutagenesisi197 – 1971I → A: Abolishes interaction with ARF1, UBC and TSG101. 1 Publication
Mutagenesisi198 – 1981K → A: Abolishes interaction with ARF1. 1 Publication
Mutagenesisi200 – 2001M → A: Abolishes interaction with ARF1. 1 Publication
Mutagenesisi204 – 2041D → A: Abolishes interaction with ARF1. 1 Publication
Mutagenesisi259 – 2591M → K: Abolishes interaction with RABEP1.
Mutagenesisi260 – 2601R → A: No effect on interaction with RABEP1. 1 Publication
Mutagenesisi260 – 2601R → E: Abolishes interaction with RABEP1 and UBC. 1 Publication
Mutagenesisi264 – 2641F → A: Abolishes interaction with RABEP1. 1 Publication
Mutagenesisi267 – 2671A → D: Abolishes interaction with RABEP1 and UBC. 1 Publication
Mutagenesisi277 – 2771L → A: Abolishes interaction with RABEP1, UBC and TSG101. 1 Publication
Mutagenesisi281 – 2811L → A: Abolishes interaction with RABEP1. 1 Publication
Mutagenesisi284 – 2841N → A: Abolishes interaction with RABEP1. 1 Publication
Mutagenesisi284 – 2841N → S: Abolishes interaction with RABEP1. 1 Publication
Mutagenesisi355 – 3551S → A: Increased interaction with IGF2R. Reduced phosphorylation. 1 Publication
Mutagenesisi355 – 3551S → D: Abolishes interaction with IGF2R. 1 Publication
Mutagenesisi356 – 3605LLDDE → AADAA: Partial loss of clathrin-binding. 1 Publication
Mutagenesisi358 – 3581D → A: Increased interaction with IGF2R. 1 Publication
Mutagenesisi361 – 3622LM → AA: Increased interaction with IGF2R. 1 Publication
Mutagenesisi563 – 5631A → D: Abolishes interaction with CCDC91. 1 Publication
Mutagenesisi564 – 5641V → D: Abolishes interaction with CCDC91. 1 Publication
Mutagenesisi570 – 5701V → E: Abolishes interaction with CCDC91. 1 Publication
Mutagenesisi572 – 5721L → E: Abolishes interaction with CCDC91. 1 Publication

Organism-specific databases

PharmGKBiPA28657.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 639639ADP-ribosylation factor-binding protein GGA1PRO_0000212680Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine2 Publications
Modified residuei355 – 3551Phosphoserine; by CK21 Publication

Post-translational modificationi

Phosphorylated by CK2 and dephosphorylated by PP2A. Phosphorylation of GGA1 allows the internal AC-LL motif to bind the VHS domain and to inhibit the recognition of cargo signals.1 Publication
Ubiquitinated.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9UJY5.
PaxDbiQ9UJY5.
PRIDEiQ9UJY5.

PTM databases

PhosphoSiteiQ9UJY5.

Expressioni

Tissue specificityi

Ubiquitously expressed.

Gene expression databases

BgeeiQ9UJY5.
CleanExiHS_GGA1.
ExpressionAtlasiQ9UJY5. baseline and differential.
GenevestigatoriQ9UJY5.

Organism-specific databases

HPAiHPA048280.
HPA051016.

Interactioni

Subunit structurei

Monomer. Interacts with NECAP1. Interacts with CNST (By similarity). Interacts with GGA2 and GGA3. Binds to clathrin and activated ARFs, including ARF1 and ARF6. Interacts with RABEP1 and RABGEF1. Interacts with the type-I membrane proteins SORT1, SORL1, LRP3, M6PR/CD-MPR, IGF2R/CI-MPR and BACE1. Binds CCDC91, P200, SYNRG, EPN4, NECAP2 and AFTPH/aftiphilin. Interacts with TSG101 and UBC. Interacts with RNF11.By similarity19 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Arf6P623312EBI-447141,EBI-988682From a different organism.
IGF2RP117172EBI-447141,EBI-1048580
MON2Q7Z3U72EBI-447141,EBI-358882
RABEP1Q152768EBI-447141,EBI-447043
RABGEF1O189732EBI-447141,EBI-447376From a different organism.
RNF11Q9Y3C53EBI-447141,EBI-396669
SORT1Q995232EBI-447141,EBI-1057058
UBBP0CG473EBI-447141,EBI-413034

Protein-protein interaction databases

BioGridi117540. 43 interactions.
IntActiQ9UJY5. 21 interactions.
MINTiMINT-126174.
STRINGi9606.ENSP00000341344.

Structurei

Secondary structure

1
639
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 53Combined sources
Helixi10 – 178Combined sources
Helixi27 – 3610Combined sources
Helixi37 – 393Combined sources
Beta strandi40 – 423Combined sources
Helixi43 – 5513Combined sources
Helixi60 – 7617Combined sources
Helixi79 – 857Combined sources
Helixi88 – 9811Combined sources
Turni100 – 1034Combined sources
Helixi104 – 1063Combined sources
Helixi109 – 12517Combined sources
Helixi130 – 14112Combined sources
Helixi172 – 18211Combined sources
Helixi187 – 20519Combined sources
Helixi212 – 23322Combined sources
Turni235 – 2384Combined sources
Helixi243 – 26725Combined sources
Helixi274 – 29825Combined sources
Helixi494 – 4974Combined sources
Helixi504 – 5063Combined sources
Beta strandi515 – 5206Combined sources
Beta strandi523 – 5319Combined sources
Beta strandi533 – 5353Combined sources
Beta strandi540 – 54910Combined sources
Beta strandi555 – 5639Combined sources
Beta strandi568 – 5725Combined sources
Beta strandi592 – 5998Combined sources
Beta strandi608 – 6169Combined sources
Beta strandi619 – 6279Combined sources
Turni633 – 6353Combined sources
Helixi636 – 6383Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1J2JX-ray1.60B166-210[»]
1JWFX-ray2.10A1-147[»]
1JWGX-ray2.00A/B1-147[»]
1NA8X-ray2.30A/B494-639[»]
1NAFX-ray2.80A165-314[»]
1NWMX-ray2.40X166-302[»]
1O3XX-ray2.10A166-305[»]
1OM9X-ray2.50A/B494-639[»]
1OXZX-ray2.80A141-326[»]
1PY1X-ray2.60A/B/C/D2-157[»]
1UJJX-ray2.60A/B1-147[»]
1UJKX-ray1.90A/B1-147[»]
1X79X-ray2.41A210-302[»]
2DWXX-ray2.55A/B/C/D507-639[»]
P/Q376-388[»]
2DWYX-ray2.30A/B/C/D507-639[»]
3G2SX-ray1.70A/B1-147[»]
3G2TX-ray2.00A/B1-147[»]
3G2UX-ray2.30A/B1-147[»]
3G2VX-ray2.10A/B1-147[»]
3G2WX-ray2.40A/B1-147[»]
C/D351-364[»]
DisProtiDP00314.
ProteinModelPortaliQ9UJY5.
SMRiQ9UJY5. Positions 2-147, 171-302, 498-639.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UJY5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini17 – 147131VHSPROSITE-ProRule annotationAdd
BLAST
Domaini171 – 299129GATPROSITE-ProRule annotationAdd
BLAST
Domaini510 – 631122GAEPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni114 – 274161Interaction with ARF3Add
BLAST
Regioni300 – 509210Unstructured hingeAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi358 – 3625Autoinhibitory

Domaini

The VHS domain functions as a recognition module for sorting signals composed of an acidic cluster followed by two leucines (AC-LL motif).
The GAT domain is responsible for interaction with ARF-GTP, UBC and RABEP1. Required for recruitment to the TGN it prevents ARF-GTP hydrolysis.
The unstructured hinge region contains clathrin-binding but no autoinhibitory (AC-LL) motifs.
The GAE domain binds accessory proteins regulating GGAs function.

Sequence similaritiesi

Belongs to the GGA protein family.Curated
Contains 1 GAE domain.PROSITE-ProRule annotation
Contains 1 GAT domain.PROSITE-ProRule annotation
Contains 1 VHS domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG321636.
GeneTreeiENSGT00700000104396.
HOGENOMiHOG000231169.
HOVERGENiHBG015945.
InParanoidiQ9UJY5.
KOiK12404.
OrthoDBiEOG7V49Z0.
PhylomeDBiQ9UJY5.
TreeFamiTF318574.

Family and domain databases

Gene3Di1.25.40.90. 1 hit.
2.60.40.1230. 1 hit.
InterProiIPR008152. Clathrin_a/b/g-adaptin_app_Ig.
IPR008153. Clathrin_g-adaptin_app.
IPR013041. Coatomer/clathrin_app_Ig-like.
IPR008942. ENTH_VHS.
IPR004152. GAT.
IPR002014. VHS.
IPR018205. VHS_subgr.
[Graphical view]
PfamiPF02883. Alpha_adaptinC2. 1 hit.
PF03127. GAT. 1 hit.
PF00790. VHS. 1 hit.
[Graphical view]
SMARTiSM00809. Alpha_adaptinC2. 1 hit.
SM00288. VHS. 1 hit.
[Graphical view]
SUPFAMiSSF48464. SSF48464. 1 hit.
SSF49348. SSF49348. 1 hit.
PROSITEiPS50180. GAE. 1 hit.
PS50909. GAT. 1 hit.
PS50179. VHS. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9UJY5-1) [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
MEPAMEPETL EARINRATNP LNKELDWASI NGFCEQLNED FEGPPLATRL
60 70 80 90 100
LAHKIQSPQE WEAIQALTVL ETCMKSCGKR FHDEVGKFRF LNELIKVVSP
110 120 130 140 150
KYLGSRTSEK VKNKILELLY SWTVGLPEEV KIAEAYQMLK KQGIVKSDPK
160 170 180 190 200
LPDDTTFPLP PPRPKNVIFE DEEKSKMLAR LLKSSHPEDL RAANKLIKEM
210 220 230 240 250
VQEDQKRMEK ISKRVNAIEE VNNNVKLLTE MVMSHSQGGA AAGSSEDLMK
260 270 280 290 300
ELYQRCERMR PTLFRLASDT EDNDEALAEI LQANDNLTQV INLYKQLVRG
310 320 330 340 350
EEVNGDATAG SIPGSTSALL DLSGLDLPPA GTTYPAMPTR PGEQASPEQP
360 370 380 390 400
SASVSLLDDE LMSLGLSDPT PPSGPSLDGT GWNSFQSSDA TEPPAPALAQ
410 420 430 440 450
APSMESRPPA QTSLPASSGL DDLDLLGKTL LQQSLPPESQ QVRWEKQQPT
460 470 480 490 500
PRLTLRDLQN KSSSCSSPSS SATSLLHTVS PEPPRPPQQP VPTELSLASI
510 520 530 540 550
TVPLESIKPS NILPVTVYDQ HGFRILFHFA RDPLPGRSDV LVVVVSMLST
560 570 580 590 600
APQPIRNIVF QSAVPKVMKV KLQPPSGTEL PAFNPIVHPS AITQVLLLAN
610 620 630
PQKEKVRLRY KLTFTMGDQT YNEMGDVDQF PPPETWGSL
Length:639
Mass (Da):70,384
Last modified:May 1, 2000 - v1
Checksum:iB0B6F089FA0F7DD5
GO
Isoform 2 (identifier: Q9UJY5-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     69-101: Missing.

Note: No experimental confirmation available.

Show »
Length:606
Mass (Da):66,563
Checksum:i6231A20CC57997B1
GO
Isoform 3 (identifier: Q9UJY5-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-73: Missing.

Show »
Length:566
Mass (Da):62,138
Checksum:iF96825C24B633E03
GO
Isoform 4 (identifier: Q9UJY5-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     277-363: Missing.

Show »
Length:552
Mass (Da):61,379
Checksum:iAC507C9F975A32C3
GO
Isoform 5 (identifier: Q9UJY5-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     70-89: LETCMKSCGKRFHDEVGKFR → RRGEATIRPPPCDDTKGGQD
     90-639: Missing.

Show »
Length:89
Mass (Da):9,969
Checksum:iF209D7D764D4CA7E
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti239 – 2391G → S in a breast cancer sample; somatic mutation. 1 Publication
VAR_036522
Natural varianti484 – 4841P → A in a breast cancer sample; somatic mutation. 1 Publication
VAR_036523

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7373Missing in isoform 3. 1 PublicationVSP_042806Add
BLAST
Alternative sequencei69 – 10133Missing in isoform 2. CuratedVSP_001744Add
BLAST
Alternative sequencei70 – 8920LETCM…VGKFR → RRGEATIRPPPCDDTKGGQD in isoform 5. 1 PublicationVSP_042807Add
BLAST
Alternative sequencei90 – 639550Missing in isoform 5. 1 PublicationVSP_042808Add
BLAST
Alternative sequencei277 – 36387Missing in isoform 4. 1 PublicationVSP_042809Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF190862 mRNA. Translation: AAF05707.1.
AF218584 mRNA. Translation: AAF42847.1.
AF233521 mRNA. Translation: AAF35393.1.
AK075256 mRNA. Translation: BAC11501.1.
AK122898 mRNA. Translation: BAG53788.1.
AK290548 mRNA. Translation: BAF83237.1.
AL035496, Z83844 Genomic DNA. Translation: CAI20951.1.
Z83844, AL035496 Genomic DNA. Translation: CAI20369.1.
AL035496, Z83844 Genomic DNA. Translation: CAQ08834.1.
Z83844, AL035496 Genomic DNA. Translation: CAQ09781.1.
CH471095 Genomic DNA. Translation: EAW60169.1.
BC000538 mRNA. Translation: AAH00538.2.
BC010917 mRNA. Translation: AAH10917.1.
BC029388 mRNA. Translation: AAH29388.1.
BC044629 mRNA. Translation: AAH44629.1.
AL110219 mRNA. Translation: CAB53679.1.
CCDSiCCDS13951.1. [Q9UJY5-1]
CCDS33643.1. [Q9UJY5-4]
CCDS54526.1. [Q9UJY5-3]
PIRiT14759.
RefSeqiNP_001001560.1. NM_001001560.2. [Q9UJY5-4]
NP_001001561.1. NM_001001561.2. [Q9UJY5-5]
NP_001166158.1. NM_001172687.1.
NP_001166159.1. NM_001172688.1. [Q9UJY5-3]
NP_037497.1. NM_013365.4. [Q9UJY5-1]
XP_005261577.1. XM_005261520.1. [Q9UJY5-3]
XP_006724292.1. XM_006724229.1. [Q9UJY5-3]
UniGeneiHs.499158.

Genome annotation databases

EnsembliENST00000325180; ENSP00000321288; ENSG00000100083. [Q9UJY5-4]
ENST00000343632; ENSP00000341344; ENSG00000100083. [Q9UJY5-1]
ENST00000406772; ENSP00000385287; ENSG00000100083. [Q9UJY5-3]
GeneIDi26088.
KEGGihsa:26088.
UCSCiuc003atb.3. human. [Q9UJY5-5]
uc003atc.3. human. [Q9UJY5-1]
uc003atd.3. human. [Q9UJY5-4]

Polymorphism databases

DMDMi14548066.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF190862 mRNA. Translation: AAF05707.1 .
AF218584 mRNA. Translation: AAF42847.1 .
AF233521 mRNA. Translation: AAF35393.1 .
AK075256 mRNA. Translation: BAC11501.1 .
AK122898 mRNA. Translation: BAG53788.1 .
AK290548 mRNA. Translation: BAF83237.1 .
AL035496 , Z83844 Genomic DNA. Translation: CAI20951.1 .
Z83844 , AL035496 Genomic DNA. Translation: CAI20369.1 .
AL035496 , Z83844 Genomic DNA. Translation: CAQ08834.1 .
Z83844 , AL035496 Genomic DNA. Translation: CAQ09781.1 .
CH471095 Genomic DNA. Translation: EAW60169.1 .
BC000538 mRNA. Translation: AAH00538.2 .
BC010917 mRNA. Translation: AAH10917.1 .
BC029388 mRNA. Translation: AAH29388.1 .
BC044629 mRNA. Translation: AAH44629.1 .
AL110219 mRNA. Translation: CAB53679.1 .
CCDSi CCDS13951.1. [Q9UJY5-1 ]
CCDS33643.1. [Q9UJY5-4 ]
CCDS54526.1. [Q9UJY5-3 ]
PIRi T14759.
RefSeqi NP_001001560.1. NM_001001560.2. [Q9UJY5-4 ]
NP_001001561.1. NM_001001561.2. [Q9UJY5-5 ]
NP_001166158.1. NM_001172687.1.
NP_001166159.1. NM_001172688.1. [Q9UJY5-3 ]
NP_037497.1. NM_013365.4. [Q9UJY5-1 ]
XP_005261577.1. XM_005261520.1. [Q9UJY5-3 ]
XP_006724292.1. XM_006724229.1. [Q9UJY5-3 ]
UniGenei Hs.499158.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1J2J X-ray 1.60 B 166-210 [» ]
1JWF X-ray 2.10 A 1-147 [» ]
1JWG X-ray 2.00 A/B 1-147 [» ]
1NA8 X-ray 2.30 A/B 494-639 [» ]
1NAF X-ray 2.80 A 165-314 [» ]
1NWM X-ray 2.40 X 166-302 [» ]
1O3X X-ray 2.10 A 166-305 [» ]
1OM9 X-ray 2.50 A/B 494-639 [» ]
1OXZ X-ray 2.80 A 141-326 [» ]
1PY1 X-ray 2.60 A/B/C/D 2-157 [» ]
1UJJ X-ray 2.60 A/B 1-147 [» ]
1UJK X-ray 1.90 A/B 1-147 [» ]
1X79 X-ray 2.41 A 210-302 [» ]
2DWX X-ray 2.55 A/B/C/D 507-639 [» ]
P/Q 376-388 [» ]
2DWY X-ray 2.30 A/B/C/D 507-639 [» ]
3G2S X-ray 1.70 A/B 1-147 [» ]
3G2T X-ray 2.00 A/B 1-147 [» ]
3G2U X-ray 2.30 A/B 1-147 [» ]
3G2V X-ray 2.10 A/B 1-147 [» ]
3G2W X-ray 2.40 A/B 1-147 [» ]
C/D 351-364 [» ]
DisProti DP00314.
ProteinModelPortali Q9UJY5.
SMRi Q9UJY5. Positions 2-147, 171-302, 498-639.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 117540. 43 interactions.
IntActi Q9UJY5. 21 interactions.
MINTi MINT-126174.
STRINGi 9606.ENSP00000341344.

PTM databases

PhosphoSitei Q9UJY5.

Polymorphism databases

DMDMi 14548066.

Proteomic databases

MaxQBi Q9UJY5.
PaxDbi Q9UJY5.
PRIDEi Q9UJY5.

Protocols and materials databases

DNASUi 26088.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000325180 ; ENSP00000321288 ; ENSG00000100083 . [Q9UJY5-4 ]
ENST00000343632 ; ENSP00000341344 ; ENSG00000100083 . [Q9UJY5-1 ]
ENST00000406772 ; ENSP00000385287 ; ENSG00000100083 . [Q9UJY5-3 ]
GeneIDi 26088.
KEGGi hsa:26088.
UCSCi uc003atb.3. human. [Q9UJY5-5 ]
uc003atc.3. human. [Q9UJY5-1 ]
uc003atd.3. human. [Q9UJY5-4 ]

Organism-specific databases

CTDi 26088.
GeneCardsi GC22P038004.
HGNCi HGNC:17842. GGA1.
HPAi HPA048280.
HPA051016.
MIMi 606004. gene.
neXtProti NX_Q9UJY5.
PharmGKBi PA28657.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG321636.
GeneTreei ENSGT00700000104396.
HOGENOMi HOG000231169.
HOVERGENi HBG015945.
InParanoidi Q9UJY5.
KOi K12404.
OrthoDBi EOG7V49Z0.
PhylomeDBi Q9UJY5.
TreeFami TF318574.

Miscellaneous databases

ChiTaRSi GGA1. human.
EvolutionaryTracei Q9UJY5.
GeneWikii GGA1.
GenomeRNAii 26088.
NextBioi 48013.
PROi Q9UJY5.
SOURCEi Search...

Gene expression databases

Bgeei Q9UJY5.
CleanExi HS_GGA1.
ExpressionAtlasi Q9UJY5. baseline and differential.
Genevestigatori Q9UJY5.

Family and domain databases

Gene3Di 1.25.40.90. 1 hit.
2.60.40.1230. 1 hit.
InterProi IPR008152. Clathrin_a/b/g-adaptin_app_Ig.
IPR008153. Clathrin_g-adaptin_app.
IPR013041. Coatomer/clathrin_app_Ig-like.
IPR008942. ENTH_VHS.
IPR004152. GAT.
IPR002014. VHS.
IPR018205. VHS_subgr.
[Graphical view ]
Pfami PF02883. Alpha_adaptinC2. 1 hit.
PF03127. GAT. 1 hit.
PF00790. VHS. 1 hit.
[Graphical view ]
SMARTi SM00809. Alpha_adaptinC2. 1 hit.
SM00288. VHS. 1 hit.
[Graphical view ]
SUPFAMi SSF48464. SSF48464. 1 hit.
SSF49348. SSF49348. 1 hit.
PROSITEi PS50180. GAE. 1 hit.
PS50909. GAT. 1 hit.
PS50179. VHS. 1 hit.
[Graphical view ]
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Publicationsi

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  1. "A family of ADP-ribosylation factor effectors that can alter transport through the trans-Golgi."
    Boman A.L., Zhang C.-J., Zhu X., Kahn R.A.
    Mol. Biol. Cell 11:1241-1255(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "GGAs: a family of ADP ribosylation factor-binding proteins related to adaptors and associated with the Golgi complex."
    Dell'Angelica E.C., Puertollano R., Mullins C., Aguilar R.C., Vargas J.D., Hartnell L.M., Bonifacino J.S.
    J. Cell Biol. 149:81-94(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Heart.
  3. "A family of proteins with gamma-adaptin and VHS domains that facilitate trafficking between the trans-Golgi network and the vacuole/lysosome."
    Hirst J., Lui W.W.Y., Bright N.A., Totty N., Seaman M.N.J., Robinson M.S.
    J. Cell Biol. 149:67-80(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "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.
  5. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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 4 AND 5), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 275-639 (ISOFORMS 1/2/3).
    Tissue: Brain.
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 31-639 (ISOFORM 1).
    Tissue: Testis.
  9. "Adaptor gamma ear homology domain conserved in gamma-adaptin and GGA proteins that interact with gamma-synergin."
    Takatsu H., Yoshino K., Nakayama K.
    Biochem. Biophys. Res. Commun. 271:719-725(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SYNRG.
  10. "The GGAs promote ARF-dependent recruitment of clathrin to the TGN."
    Puertollano R., Randazzo P.A., Presley J.F., Hartnell L.M., Bonifacino J.S.
    Cell 105:93-102(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CLATHRIN, FUNCTION, MUTAGENESIS OF 356-LEU--GLU-360.
  11. "Golgi-localizing, gamma-adaptin ear homology domain, ADP-ribosylation factor-binding (GGA) proteins interact with acidic dileucine sequences within the cytoplasmic domains of sorting receptors through their Vps27p/Hrs/STAM (VHS) domains."
    Takatsu H., Katoh Y., Shiba Y., Nakayama K.
    J. Biol. Chem. 276:28541-28545(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SORT1; LRP3 AND IGF2R.
  12. "Sorting of mannose 6-phosphate receptors mediated by the GGAs."
    Puertollano R., Aguilar R.C., Gorshkova I., Crouch R.J., Bonifacino J.S.
    Science 292:1712-1716(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH M6PR AND IGF2R.
  13. "GGA proteins associate with Golgi membranes through interaction between their GGAH domains and ADP-ribosylation factors."
    Takatsu H., Yoshino K., Toda K., Nakayama K.
    Biochem. J. 365:369-378(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ARF1; ARF5 AND ARF6.
  14. "The sorLA cytoplasmic domain interacts with GGA1 and -2 and defines minimum requirements for GGA binding."
    Jacobsen L., Madsen P., Nielsen M.S., Geraerts W.P.M., Gliemann J., Smit A.B., Petersen C.M.
    FEBS Lett. 511:155-158(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SORT1 AND SORL1.
  15. "Autoinhibition of the ligand-binding site of GGA1/3 VHS domains by an internal acidic cluster-dileucine motif."
    Doray B., Bruns K., Ghosh P., Kornfeld S.A.
    Proc. Natl. Acad. Sci. U.S.A. 99:8072-8077(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ASN-92; SER-355; ASP-358 AND 361-LEU-MET-362, PHOSPHORYLATION AT SER-355, INTERACTION WITH IGF2R.
  16. "Biochemical and structural characterization of the interaction of memapsin 2 (beta-secretase) cytosolic domain with the VHS domain of GGA proteins."
    He X., Zhu G., Koelsch G., Rodgers K.K., Zhang X.C., Tang J.
    Biochemistry 42:12174-12180(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BACE1.
  17. "Divalent interaction of the GGAs with the Rabaptin-5-Rabex-5 complex."
    Mattera R., Arighi C.N., Lodge R., Zerial M., Bonifacino J.S.
    EMBO J. 22:78-88(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RABEP1 AND RABGEF1.
  18. "Phosphorylation-induced conformational changes regulate GGAs 1 and 3 function at the trans-Golgi network."
    Ghosh P., Kornfeld S.
    J. Biol. Chem. 278:14543-14549(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: REGULATION BY PHOSPHORYLATION, DEPHOSPHORYLATION BY PP2A.
  19. Cited for: INTERACTION WITH EPN4.
  20. "Mammalian GGAs act together to sort mannose 6-phosphate receptors."
    Ghosh P., Griffith J., Geuze H.J., Kornfeld S.
    J. Cell Biol. 163:755-766(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GGA2 AND GGA3, SUBCELLULAR LOCATION.
  21. "Binding partners for the COOH-terminal appendage domains of the GGAs and gamma-adaptin."
    Lui W.W.Y., Collins B.M., Hirst J., Motley A., Millar C., Schu P., Owen D.J., Robinson M.S.
    Mol. Biol. Cell 14:2385-2398(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CCDC91; P200 AND SYNRG, MUTAGENESIS OF ALA-563; VAL-564; VAL-570 AND LEU-572.
  22. "GAT (GGA and Tom1) domain responsible for ubiquitin binding and ubiquitination."
    Shiba Y., Katoh Y., Shiba T., Yoshino K., Takatsu H., Kobayashi H., Shin H.-W., Wakatsuki S., Nakayama K.
    J. Biol. Chem. 279:7105-7111(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH UBC.
  23. "Definition of the consensus motif recognized by gamma-adaptin ear domains."
    Mattera R., Ritter B., Sidhu S.S., McPherson P.S., Bonifacino J.S.
    J. Biol. Chem. 279:8018-8028(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NECAP2 AND AFTPH.
  24. "The trihelical bundle subdomain of the GGA proteins interacts with multiple partners through overlapping but distinct sites."
    Mattera R., Puertollano R., Smith W.J., Bonifacino J.S.
    J. Biol. Chem. 279:31409-31418(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ARF1; RABEP1; UBC AND TSG101, MUTAGENESIS OF LEU-182; ASN-194; ILE-197; LYS-198; MET-200; ASP-204; ARG-260; PHE-264; ALA-267; LEU-277; LEU-281 AND ASN-284.
  25. "Interactions of GGA3 with the ubiquitin sorting machinery."
    Puertollano R., Bonifacino J.S.
    Nat. Cell Biol. 6:244-251(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  26. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  27. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  28. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  29. "Multiple modification and protein interaction signals drive the Ring finger protein 11 (RNF11) E3 ligase to the endosomal compartment."
    Santonico E., Belleudi F., Panni S., Torrisi M.R., Cesareni G., Castagnoli L.
    Oncogene 29:5604-5618(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RNF11.
  30. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  31. "Structural basis for Arf6-MKLP1 complex formation on the Flemming body responsible for cytokinesis."
    Makyio H., Ohgi M., Takei T., Takahashi S., Takatsu H., Katoh Y., Hanai A., Ueda T., Kanaho Y., Xie Y., Shin H.W., Kamikubo H., Kataoka M., Kawasaki M., Kato R., Wakatsuki S., Nakayama K.
    EMBO J. 31:2590-2603(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ARF6.
  32. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  33. "Structural basis for recognition of acidic-cluster dileucine sequence by GGA1."
    Shiba T., Takatsu H., Nogi T., Matsugaki N., Kawasaki M., Igarashi N., Suzuki M., Kato R., Earnest T., Nakayama K., Wakatsuki S.
    Nature 415:937-941(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-147.
  34. "Molecular mechanism of membrane recruitment of GGA by ARF in lysosomal protein transport."
    Shiba T., Kawasaki M., Takatsu H., Nogi T., Matsugaki N., Igarashi N., Suzuki M., Kato R., Nakayama K., Wakatsuki S.
    Nat. Struct. Biol. 10:386-393(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 168-208 IN COMPLEX WITH MOUSE ARF1.
  35. "Structural basis for binding of accessory proteins by the appendage domain of GGAs."
    Collins B.M., Praefcke G.J., Robinson M.S., Owen D.J.
    Nat. Struct. Biol. 10:607-613(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2-16 IN COMPLEX WITH CCDC91.
  36. Cited for: VARIANTS [LARGE SCALE ANALYSIS] SER-239 AND ALA-484.

Entry informationi

Entry nameiGGA1_HUMAN
AccessioniPrimary (citable) accession number: Q9UJY5
Secondary accession number(s): A8K3D3
, B0QYR7, Q5TG07, Q86YA9, Q8NCS6, Q9BW94, Q9UG00, Q9UGW0, Q9UGW1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: May 1, 2000
Last modified: October 29, 2014
This is version 158 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: 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

External Data

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