Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9NZ52

- GGA3_HUMAN

UniProt

Q9NZ52 - GGA3_HUMAN

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 154 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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
    2. protein binding Source: IntAct

    GO - Biological processi

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

    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 membrane Source: UniProtKB-SubCell
    3. trans-Golgi network Source: UniProtKB

    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. 2 Publications
    Mutagenesisi199 – 1991S → P: Loss of interaction with ARF1 and Golgi localization. 2 Publications
    Mutagenesisi217 – 2171T → P: Loss of interaction with ARF1 and Golgi localization. 2 Publications
    Mutagenesisi247 – 2471L → P: Loss of UBC-binding and ubiquitination. 2 Publications
    Mutagenesisi258 – 2581K → M: No effect. Confers an affinity to RABEP1 identical to GGA1; when associated with N-283. 2 Publications
    Mutagenesisi262 – 2621L → S: Loss of UBC-binding and ubiquitination. 2 Publications
    Mutagenesisi276 – 2761L → A: Loss of UBC-binding and ubiquitination. 3 Publications
    Mutagenesisi276 – 2761L → S: Loss of UBC-binding and ubiquitination. 3 Publications
    Mutagenesisi280 – 2801L → R: Loss of UBC-binding and ubiquitination. 2 Publications
    Mutagenesisi283 – 2831S → N: Can bind RABEP1. Confers an affinity to RABEP1 identical to GGA1; when associated with M-258. 2 Publications
    Mutagenesisi284 – 2841D → G: Loss of UBC-binding and ubiquitination. 2 Publications
    Mutagenesisi293 – 2931Y → H: Loss of UBC-binding and ubiquitination. 2 Publications
    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

    ArrayExpressiQ9NZ52.
    BgeeiQ9NZ52.
    CleanExiHS_GGA3.
    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.
    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

    MAEAEGESLE SWLNKATNPS NRQEDWEYII GFCDQINKEL EGPQIAVRLL    50
    AHKIQSPQEW EALQALTVLE ACMKNCGRRF HNEVGKFRFL NELIKVVSPK 100
    YLGDRVSEKV KTKVIELLYS WTMALPEEAK IKDAYHMLKR QGIVQSDPPI 150
    PVDRTLIPSP PPRPKNPVFD DEEKSKLLAK LLKSKNPDDL QEANKLIKSM 200
    VKEDEARIQK VTKRLHTLEE VNNNVRLLSE MLLHYSQEDS SDGDRELMKE 250
    LFDQCENKRR TLFKLASETE DNDNSLGDIL QASDNLSRVI NSYKTIIEGQ 300
    VINGEVATLT LPDSEGNSQC SNQGTLIDLA ELDTTNSLSS VLAPAPTPPS 350
    SGIPILPPPP QASGPPRSRS SSQAEATLGP SSTSNALSWL DEELLCLGLA 400
    DPAPNVPPKE SAGNSQWHLL QREQSDLDFF SPRPGTAACG ASDAPLLQPS 450
    APSSSSSQAP LPPPFPAPVV PASVPAPSAG SSLFSTGVAP ALAPKVEPAV 500
    PGHHGLALGN SALHHLDALD QLLEEAKVTS GLVKPTTSPL IPTTTPARPL 550
    LPFSTGPGSP LFQPLSFQSQ GSPPKGPELS LASIHVPLES IKPSSALPVT 600
    AYDKNGFRIL FHFAKECPPG RPDVLVVVVS MLNTAPLPVK SIVLQAAVPK 650
    SMKVKLQPPS GTELSPFSPI QPPAAITQVM LLANPLKEKV RLRYKLTFAL 700
    GEQLSTEVGE VDQFPPVEQW GNL 723
    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

    EnsembliENST00000578348; ENSP00000463288; ENSG00000125447. [Q9NZ52-3]
    ENST00000582717; ENSP00000462081; ENSG00000125447. [Q9NZ52-4]
    GeneIDi23163.
    KEGGihsa:23163.
    UCSCiuc002jni.2. human. [Q9NZ52-1]
    uc002jnj.2. human. [Q9NZ52-2]

    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 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 ]

    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.
    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

    ArrayExpressi Q9NZ52.
    Bgeei Q9NZ52.
    CleanExi HS_GGA3.
    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

    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 1, 2014
    This is version 154 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