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Q9UJY5

- GGA1_HUMAN

UniProt

Q9UJY5 - GGA1_HUMAN

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
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    • History
      Entry version 157 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    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. 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 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 membrane Source: UniProtKB-SubCell
    3. Golgi apparatus Source: UniProtKB
    4. intracellular membrane-bounded organelle Source: HPA
    5. membrane Source: UniProtKB
    6. nucleus Source: HPA

    Keywords - Cellular componenti

    Endosome, Golgi apparatus, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi92 – 921N → A: Abolishes interaction with IGF2R. 2 Publications
    Mutagenesisi182 – 1821L → A: Abolishes interaction with ARF1, UBC and TSG101. 2 Publications
    Mutagenesisi194 – 1941N → A: Abolishes interaction with ARF1 and RABEP1. 2 Publications
    Mutagenesisi197 – 1971I → A: Abolishes interaction with ARF1, UBC and TSG101. 2 Publications
    Mutagenesisi198 – 1981K → A: Abolishes interaction with ARF1. 2 Publications
    Mutagenesisi200 – 2001M → A: Abolishes interaction with ARF1. 2 Publications
    Mutagenesisi204 – 2041D → A: Abolishes interaction with ARF1. 2 Publications
    Mutagenesisi259 – 2591M → K: Abolishes interaction with RABEP1. 1 Publication
    Mutagenesisi260 – 2601R → A: No effect on interaction with RABEP1. 2 Publications
    Mutagenesisi260 – 2601R → E: Abolishes interaction with RABEP1 and UBC. 2 Publications
    Mutagenesisi264 – 2641F → A: Abolishes interaction with RABEP1. 2 Publications
    Mutagenesisi267 – 2671A → D: Abolishes interaction with RABEP1 and UBC. 2 Publications
    Mutagenesisi277 – 2771L → A: Abolishes interaction with RABEP1, UBC and TSG101. 2 Publications
    Mutagenesisi281 – 2811L → A: Abolishes interaction with RABEP1. 2 Publications
    Mutagenesisi284 – 2841N → A: Abolishes interaction with RABEP1. 2 Publications
    Mutagenesisi284 – 2841N → S: Abolishes interaction with RABEP1. 2 Publications
    Mutagenesisi355 – 3551S → A: Increased interaction with IGF2R. Reduced phosphorylation. 2 Publications
    Mutagenesisi355 – 3551S → D: Abolishes interaction with IGF2R. 2 Publications
    Mutagenesisi356 – 3605LLDDE → AADAA: Partial loss of clathrin-binding. 1 Publication
    Mutagenesisi358 – 3581D → A: Increased interaction with IGF2R. 2 Publications
    Mutagenesisi361 – 3622LM → AA: Increased interaction with IGF2R. 1 Publication
    Mutagenesisi563 – 5631A → D: Abolishes interaction with CCDC91. 2 Publications
    Mutagenesisi564 – 5641V → D: Abolishes interaction with CCDC91. 2 Publications
    Mutagenesisi570 – 5701V → E: Abolishes interaction with CCDC91. 2 Publications
    Mutagenesisi572 – 5721L → E: Abolishes interaction with CCDC91. 2 Publications

    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

    ArrayExpressiQ9UJY5.
    BgeeiQ9UJY5.
    CleanExiHS_GGA1.
    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 – 53
    Helixi10 – 178
    Helixi27 – 3610
    Helixi37 – 393
    Beta strandi40 – 423
    Helixi43 – 5513
    Helixi60 – 7617
    Helixi79 – 857
    Helixi88 – 9811
    Turni100 – 1034
    Helixi104 – 1063
    Helixi109 – 12517
    Helixi130 – 14112
    Helixi172 – 18211
    Helixi187 – 20519
    Helixi212 – 23322
    Turni235 – 2384
    Helixi243 – 26725
    Helixi274 – 29825
    Helixi494 – 4974
    Helixi504 – 5063
    Beta strandi515 – 5206
    Beta strandi523 – 5319
    Beta strandi533 – 5353
    Beta strandi540 – 54910
    Beta strandi555 – 5639
    Beta strandi568 – 5725
    Beta strandi592 – 5998
    Beta strandi608 – 6169
    Beta strandi619 – 6279
    Turni633 – 6353
    Helixi636 – 6383

    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.
    HOGENOMiHOG000231169.
    HOVERGENiHBG015945.
    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

    MEPAMEPETL EARINRATNP LNKELDWASI NGFCEQLNED FEGPPLATRL    50
    LAHKIQSPQE WEAIQALTVL ETCMKSCGKR FHDEVGKFRF LNELIKVVSP 100
    KYLGSRTSEK VKNKILELLY SWTVGLPEEV KIAEAYQMLK KQGIVKSDPK 150
    LPDDTTFPLP PPRPKNVIFE DEEKSKMLAR LLKSSHPEDL RAANKLIKEM 200
    VQEDQKRMEK ISKRVNAIEE VNNNVKLLTE MVMSHSQGGA AAGSSEDLMK 250
    ELYQRCERMR PTLFRLASDT EDNDEALAEI LQANDNLTQV INLYKQLVRG 300
    EEVNGDATAG SIPGSTSALL DLSGLDLPPA GTTYPAMPTR PGEQASPEQP 350
    SASVSLLDDE LMSLGLSDPT PPSGPSLDGT GWNSFQSSDA TEPPAPALAQ 400
    APSMESRPPA QTSLPASSGL DDLDLLGKTL LQQSLPPESQ QVRWEKQQPT 450
    PRLTLRDLQN KSSSCSSPSS SATSLLHTVS PEPPRPPQQP VPTELSLASI 500
    TVPLESIKPS NILPVTVYDQ HGFRILFHFA RDPLPGRSDV LVVVVSMLST 550
    APQPIRNIVF QSAVPKVMKV KLQPPSGTEL PAFNPIVHPS AITQVLLLAN 600
    PQKEKVRLRY KLTFTMGDQT YNEMGDVDQF PPPETWGSL 639
    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]
    CCDS46704.1. [Q9UJY5-5]
    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 ]
    CCDS46704.1. [Q9UJY5-5 ]
    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.
    HOGENOMi HOG000231169.
    HOVERGENi HBG015945.
    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

    ArrayExpressi Q9UJY5.
    Bgeei Q9UJY5.
    CleanExi HS_GGA1.
    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 ]
    ProtoNeti Search...

    Publicationsi

    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 1, 2014
    This is version 157 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

    Dasty 3