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Q9NZ52

- GGA3_HUMAN

UniProt

Q9NZ52 - GGA3_HUMAN

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Protein

ADP-ribosylation factor-binding protein GGA3

Gene

GGA3

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 - Molecular functioni

  1. ADP-ribosylation factor binding Source: UniProtKB

GO - Biological processi

  1. intracellular protein transport Source: UniProtKB
  2. 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 GGA3
Alternative name(s):
Golgi-localized, gamma ear-containing, ARF-binding protein 3
Gene namesi
Name:GGA3
Synonyms:KIAA0154
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:17079. GGA3.

Subcellular locationi

Golgi apparatustrans-Golgi network membrane 1 Publication; Peripheral membrane protein 1 Publication. Endosome membrane 1 Publication; Peripheral membrane protein 1 Publication

GO - Cellular componenti

  1. clathrin adaptor complex Source: InterPro
  2. endosome Source: UniProtKB-KW
  3. trans-Golgi network Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endosome, Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi194 – 1941N → A: Loss of interaction with ARF1 and Golgi localization. 1 Publication
Mutagenesisi199 – 1991S → P: Loss of interaction with ARF1 and Golgi localization. 1 Publication
Mutagenesisi217 – 2171T → P: Loss of interaction with ARF1 and Golgi localization. 1 Publication
Mutagenesisi247 – 2471L → P: Loss of UBC-binding and ubiquitination. 1 Publication
Mutagenesisi258 – 2581K → M: No effect. Confers an affinity to RABEP1 identical to GGA1; when associated with N-283. 1 Publication
Mutagenesisi262 – 2621L → S: Loss of UBC-binding and ubiquitination. 1 Publication
Mutagenesisi276 – 2761L → A: Loss of UBC-binding and ubiquitination. 2 Publications
Mutagenesisi276 – 2761L → S: Loss of UBC-binding and ubiquitination. 2 Publications
Mutagenesisi280 – 2801L → R: Loss of UBC-binding and ubiquitination. 1 Publication
Mutagenesisi283 – 2831S → N: Can bind RABEP1. Confers an affinity to RABEP1 identical to GGA1; when associated with M-258. 1 Publication
Mutagenesisi284 – 2841D → G: Loss of UBC-binding and ubiquitination. 1 Publication
Mutagenesisi293 – 2931Y → H: Loss of UBC-binding and ubiquitination. 1 Publication
Mutagenesisi391 – 3955DEELL → AAAAA: Increased binding to IGF2R. 1 Publication

Organism-specific databases

PharmGKBiPA28659.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 723723ADP-ribosylation factor-binding protein GGA3PRO_0000212684Add
BLAST

Post-translational modificationi

Phosphorylated by CK2 and dephosphorylated by PP2A (By similarity). Phosphorylation of GGA3 allows the internal AC-LL motif to bind the VHS domain and to inhibit the recognition of cargo signals.By similarity
Ubiquitinated.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9NZ52.
PaxDbiQ9NZ52.
PRIDEiQ9NZ52.

PTM databases

PhosphoSiteiQ9NZ52.

Expressioni

Tissue specificityi

Ubiquitously expressed.

Gene expression databases

BgeeiQ9NZ52.
CleanExiHS_GGA3.
ExpressionAtlasiQ9NZ52. baseline and differential.
GenevestigatoriQ9NZ52.

Organism-specific databases

HPAiHPA022945.

Interactioni

Subunit structurei

Monomer. Interacts with SORT1, SORL1, LRP3, GGA binding partner (GGABP) and P200 (By similarity). Interacts with GGA1 and GGA2. Binds to clathrin and activated ARFs. Binds RABEP1 and RABGEF1. Interacts with the membrane proteins M6PR/CD-MPR, IGF2R/CI-MPR and BACE1 and the accessory proteins SYNRG, EPN4, NECAP1, NECAP2 and AFTPH/aftiphilin. Interacts with TSG101 and UBC.By similarity13 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PACS1Q6VY075EBI-447404,EBI-2555014
RABEP1Q152764EBI-447404,EBI-447043
UBBP0CG472EBI-447404,EBI-413034

Protein-protein interaction databases

BioGridi116775. 32 interactions.
DIPiDIP-31600N.
IntActiQ9NZ52. 13 interactions.
MINTiMINT-126320.
STRINGi9606.ENSP00000245541.

Structurei

Secondary structure

1
723
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 168
Helixi26 – 3813
Helixi42 – 5413
Helixi59 – 7517
Helixi77 – 848
Helixi87 – 9711
Helixi99 – 1035
Helixi108 – 12417
Helixi129 – 14012
Helixi218 – 23114
Turni232 – 2343
Turni237 – 2393
Helixi242 – 26726
Helixi276 – 29015
Helixi292 – 2954
Turni296 – 2983
Helixi588 – 5903
Beta strandi599 – 6046
Beta strandi607 – 61610
Beta strandi624 – 63310
Beta strandi635 – 6373
Beta strandi639 – 6479
Beta strandi652 – 6565
Beta strandi675 – 6839
Beta strandi692 – 7009
Beta strandi703 – 7119
Helixi717 – 7193

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JPLX-ray2.40A/B/C/D1-166[»]
1JUQX-ray2.20A/B/C/D1-166[»]
1LF8X-ray2.30A/B/C/D1-166[»]
1P4UX-ray2.20A571-723[»]
1WR6X-ray2.60A/B/C/D209-319[»]
1YD8X-ray2.80G/H208-301[»]
ProteinModelPortaliQ9NZ52.
SMRiQ9NZ52. Positions 1-157, 168-304, 579-723.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NZ52.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini16 – 146131VHSPROSITE-ProRule annotationAdd
BLAST
Domaini171 – 298128GATPROSITE-ProRule annotationAdd
BLAST
Domaini594 – 715122GAEPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 313313Binds to ARF1 (in long isoform)Add
BLAST
Regioni299 – 593295Unstructured hingeAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi391 – 3955Autoinhibitory

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi357 – 3604Poly-Pro
Compositional biasi453 – 4575Poly-Ser
Compositional biasi624 – 6296Poly-Val

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 and an 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.
InParanoidiQ9NZ52.
KOiK12404.
OMAiQGSPMKG.
PhylomeDBiQ9NZ52.
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.
IPR027422. GGA3.
IPR002014. VHS.
IPR018205. VHS_subgr.
[Graphical view]
PANTHERiPTHR13856:SF34. PTHR13856:SF34. 1 hit.
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 (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform Long (identifier: Q9NZ52-1) [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
MAEAEGESLE SWLNKATNPS NRQEDWEYII GFCDQINKEL EGPQIAVRLL
60 70 80 90 100
AHKIQSPQEW EALQALTVLE ACMKNCGRRF HNEVGKFRFL NELIKVVSPK
110 120 130 140 150
YLGDRVSEKV KTKVIELLYS WTMALPEEAK IKDAYHMLKR QGIVQSDPPI
160 170 180 190 200
PVDRTLIPSP PPRPKNPVFD DEEKSKLLAK LLKSKNPDDL QEANKLIKSM
210 220 230 240 250
VKEDEARIQK VTKRLHTLEE VNNNVRLLSE MLLHYSQEDS SDGDRELMKE
260 270 280 290 300
LFDQCENKRR TLFKLASETE DNDNSLGDIL QASDNLSRVI NSYKTIIEGQ
310 320 330 340 350
VINGEVATLT LPDSEGNSQC SNQGTLIDLA ELDTTNSLSS VLAPAPTPPS
360 370 380 390 400
SGIPILPPPP QASGPPRSRS SSQAEATLGP SSTSNALSWL DEELLCLGLA
410 420 430 440 450
DPAPNVPPKE SAGNSQWHLL QREQSDLDFF SPRPGTAACG ASDAPLLQPS
460 470 480 490 500
APSSSSSQAP LPPPFPAPVV PASVPAPSAG SSLFSTGVAP ALAPKVEPAV
510 520 530 540 550
PGHHGLALGN SALHHLDALD QLLEEAKVTS GLVKPTTSPL IPTTTPARPL
560 570 580 590 600
LPFSTGPGSP LFQPLSFQSQ GSPPKGPELS LASIHVPLES IKPSSALPVT
610 620 630 640 650
AYDKNGFRIL FHFAKECPPG RPDVLVVVVS MLNTAPLPVK SIVLQAAVPK
660 670 680 690 700
SMKVKLQPPS GTELSPFSPI QPPAAITQVM LLANPLKEKV RLRYKLTFAL
710 720
GEQLSTEVGE VDQFPPVEQW GNL
Length:723
Mass (Da):78,315
Last modified:October 1, 2000 - v1
Checksum:i4F80D6032239168C
GO
Isoform Short (identifier: Q9NZ52-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     68-100: Missing.

Show »
Length:690
Mass (Da):74,470
Checksum:iE3A1C841AB3966C8
GO
Isoform 3 (identifier: Q9NZ52-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-122: Missing.
     688-723: EKVRLRYKLTFALGEQLSTEVGEVDQFPPVEQWGNL → KQVLSFLGKACLQPWGQAILLTTSCLA

Show »
Length:592
Mass (Da):62,921
Checksum:iCACD3268CEE80BBE
GO
Isoform 4 (identifier: Q9NZ52-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-72: Missing.

Note: No experimental confirmation available.

Show »
Length:651
Mass (Da):70,148
Checksum:i416484203E34542A
GO

Sequence cautioni

The sequence BAA09926.1 differs from that shown. Reason: Erroneous initiation.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti448 – 4481Q → K in AAH70044. (PubMed:15489334)Curated
Sequence conflicti562 – 5621F → S in BAH13665. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti574 – 5741P → L in a breast cancer sample; somatic mutation. 1 Publication
VAR_036524

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 122122Missing in isoform 3. 1 PublicationVSP_045133Add
BLAST
Alternative sequencei1 – 7272Missing in isoform 4. 1 PublicationVSP_046868Add
BLAST
Alternative sequencei68 – 10033Missing in isoform Short. 4 PublicationsVSP_001745Add
BLAST
Alternative sequencei688 – 72336EKVRL…QWGNL → KQVLSFLGKACLQPWGQAIL LTTSCLA in isoform 3. 1 PublicationVSP_045134Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF219138 mRNA. Translation: AAF42848.1.
AF190864 mRNA. Translation: AAF05709.1.
AF219139 mRNA. Translation: AAF42849.1.
D63876 mRNA. Translation: BAA09926.1. Different initiation.
AK301895 mRNA. Translation: BAH13578.1.
AK302278 mRNA. Translation: BAH13665.1.
AC022211 Genomic DNA. No translation available.
CH471099 Genomic DNA. Translation: EAW89258.1.
BC070044 mRNA. Translation: AAH70044.1.
CCDSiCCDS11716.1. [Q9NZ52-2]
CCDS11717.1. [Q9NZ52-1]
CCDS54164.1. [Q9NZ52-4]
CCDS58597.1. [Q9NZ52-3]
RefSeqiNP_001166174.1. NM_001172703.2. [Q9NZ52-4]
NP_001166175.1. NM_001172704.2. [Q9NZ52-3]
NP_001278570.1. NM_001291641.1. [Q9NZ52-4]
NP_001278571.1. NM_001291642.1.
NP_054720.1. NM_014001.4. [Q9NZ52-2]
NP_619525.1. NM_138619.3. [Q9NZ52-1]
UniGeneiHs.87726.

Genome annotation databases

EnsembliENST00000537686; ENSP00000438085; ENSG00000125447. [Q9NZ52-1]
ENST00000538886; ENSP00000446421; ENSG00000125447. [Q9NZ52-2]
ENST00000578348; ENSP00000463288; ENSG00000125447. [Q9NZ52-3]
ENST00000582717; ENSP00000462081; ENSG00000125447. [Q9NZ52-4]
GeneIDi23163.
KEGGihsa:23163.
UCSCiuc002jni.2. human. [Q9NZ52-1]
uc002jnj.2. human. [Q9NZ52-2]
uc010wrw.2. human.

Polymorphism databases

DMDMi14548064.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF219138 mRNA. Translation: AAF42848.1 .
AF190864 mRNA. Translation: AAF05709.1 .
AF219139 mRNA. Translation: AAF42849.1 .
D63876 mRNA. Translation: BAA09926.1 . Different initiation.
AK301895 mRNA. Translation: BAH13578.1 .
AK302278 mRNA. Translation: BAH13665.1 .
AC022211 Genomic DNA. No translation available.
CH471099 Genomic DNA. Translation: EAW89258.1 .
BC070044 mRNA. Translation: AAH70044.1 .
CCDSi CCDS11716.1. [Q9NZ52-2 ]
CCDS11717.1. [Q9NZ52-1 ]
CCDS54164.1. [Q9NZ52-4 ]
CCDS58597.1. [Q9NZ52-3 ]
RefSeqi NP_001166174.1. NM_001172703.2. [Q9NZ52-4 ]
NP_001166175.1. NM_001172704.2. [Q9NZ52-3 ]
NP_001278570.1. NM_001291641.1. [Q9NZ52-4 ]
NP_001278571.1. NM_001291642.1.
NP_054720.1. NM_014001.4. [Q9NZ52-2 ]
NP_619525.1. NM_138619.3. [Q9NZ52-1 ]
UniGenei Hs.87726.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1JPL X-ray 2.40 A/B/C/D 1-166 [» ]
1JUQ X-ray 2.20 A/B/C/D 1-166 [» ]
1LF8 X-ray 2.30 A/B/C/D 1-166 [» ]
1P4U X-ray 2.20 A 571-723 [» ]
1WR6 X-ray 2.60 A/B/C/D 209-319 [» ]
1YD8 X-ray 2.80 G/H 208-301 [» ]
ProteinModelPortali Q9NZ52.
SMRi Q9NZ52. Positions 1-157, 168-304, 579-723.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116775. 32 interactions.
DIPi DIP-31600N.
IntActi Q9NZ52. 13 interactions.
MINTi MINT-126320.
STRINGi 9606.ENSP00000245541.

PTM databases

PhosphoSitei Q9NZ52.

Polymorphism databases

DMDMi 14548064.

Proteomic databases

MaxQBi Q9NZ52.
PaxDbi Q9NZ52.
PRIDEi Q9NZ52.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000537686 ; ENSP00000438085 ; ENSG00000125447 . [Q9NZ52-1 ]
ENST00000538886 ; ENSP00000446421 ; ENSG00000125447 . [Q9NZ52-2 ]
ENST00000578348 ; ENSP00000463288 ; ENSG00000125447 . [Q9NZ52-3 ]
ENST00000582717 ; ENSP00000462081 ; ENSG00000125447 . [Q9NZ52-4 ]
GeneIDi 23163.
KEGGi hsa:23163.
UCSCi uc002jni.2. human. [Q9NZ52-1 ]
uc002jnj.2. human. [Q9NZ52-2 ]
uc010wrw.2. human.

Organism-specific databases

CTDi 23163.
GeneCardsi GC17M073229.
HGNCi HGNC:17079. GGA3.
HPAi HPA022945.
MIMi 606006. gene.
neXtProti NX_Q9NZ52.
PharmGKBi PA28659.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG321636.
GeneTreei ENSGT00700000104396.
HOGENOMi HOG000231169.
HOVERGENi HBG015945.
InParanoidi Q9NZ52.
KOi K12404.
OMAi QGSPMKG.
PhylomeDBi Q9NZ52.
TreeFami TF318574.

Miscellaneous databases

EvolutionaryTracei Q9NZ52.
GeneWikii GGA3.
GenomeRNAii 23163.
NextBioi 35535625.
PROi Q9NZ52.
SOURCEi Search...

Gene expression databases

Bgeei Q9NZ52.
CleanExi HS_GGA3.
ExpressionAtlasi Q9NZ52. baseline and differential.
Genevestigatori Q9NZ52.

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.
IPR027422. GGA3.
IPR002014. VHS.
IPR018205. VHS_subgr.
[Graphical view ]
PANTHERi PTHR13856:SF34. PTHR13856:SF34. 1 hit.
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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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] (ISOFORMS LONG AND SHORT).
    Tissue: Heart.
  2. "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 SHORT).
  3. "Prediction of the coding sequences of unidentified human genes. IV. The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of cDNA clones from human cell line KG-1."
    Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.
    DNA Res. 2:167-174(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT).
    Tissue: Bone marrow.
  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 3 AND 4).
    Tissue: Testis.
  5. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [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] (ISOFORM SHORT).
    Tissue: Brain.
  8. "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.
  9. "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: MUTAGENESIS OF ASN-194; SER-199 AND THR-217, INTERACTION WITH ARF1 AND CLATHRIN, FUNCTION.
  10. "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.
  11. "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.
  12. "Enthoprotin: a novel clathrin-associated protein identified through subcellular proteomics."
    Wasiak S., Legendre-Guillemin V., Puertollano R., Blondeau F., Girard M., de Heuvel E., Boismenu D., Bell A.W., Bonifacino J.S., McPherson P.S.
    J. Cell Biol. 158:855-862(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EPN4.
  13. "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 391-ASP--LEU-395, INTERACTION WITH IGF2R, AUTOINHIBITION.
  14. "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.
  15. "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.
  16. "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 GGA1 AND GGA2.
  17. "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: MUTAGENESIS OF LEU-247; LEU-262; LEU-276; LEU-280; ASP-284 AND TYR-293, INTERACTION WITH UBC, UBIQUITINATION.
  18. "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 NECAP1; NECAP2 AND AFTPH.
  19. "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: MUTAGENESIS OF LYS-258 AND SER-283, INTERACTION WITH RABEP1.
  20. "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, MUTAGENESIS OF LEU-276, INTERACTION WITH UBC AND TSG101.
  21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "Phosphoregulation of sorting signal-VHS domain interactions by a direct electrostatic mechanism."
    Kato Y., Misra S., Puertollano R., Hurley J.H., Bonifacino J.S.
    Nat. Struct. Biol. 9:532-536(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-166.
  23. Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-574.

Entry informationi

Entry nameiGGA3_HUMAN
AccessioniPrimary (citable) accession number: Q9NZ52
Secondary accession number(s): B7Z7E2
, B7Z7M9, J3KRN0, Q15017, Q6IS16, Q9UJY3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: October 1, 2000
Last modified: October 29, 2014
This is version 155 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 17
    Human chromosome 17: 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

Dasty 3