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Q9UJY5 (GGA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 156. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:GGA1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length639 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.10

Subunit structure

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. Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.29 Ref.31

Subcellular location

Golgi apparatustrans-Golgi network membrane; Peripheral membrane protein. Endosome membrane; Peripheral membrane protein Ref.20 Ref.25.

Tissue specificity

Ubiquitously expressed.

Domain

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.

Post-translational modification

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. Ref.15 Ref.18

Ubiquitinated By similarity.

Sequence similarities

Belongs to the GGA protein family.

Contains 1 GAE domain.

Contains 1 GAT domain.

Contains 1 VHS domain.

Caution

It is uncertain whether Met-1 or Met-5 is the initiator.

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9UJY5-1)

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.
Isoform 2 (identifier: Q9UJY5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     69-101: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q9UJY5-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-73: Missing.
Isoform 4 (identifier: Q9UJY5-4)

The sequence of this isoform differs from the canonical sequence as follows:
     277-363: Missing.
Isoform 5 (identifier: Q9UJY5-5)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 639639ADP-ribosylation factor-binding protein GGA1
PRO_0000212680

Regions

Domain17 – 147131VHS
Domain171 – 299129GAT
Domain510 – 631122GAE
Region114 – 274161Interaction with ARF3
Region300 – 509210Unstructured hinge
Motif358 – 3625Autoinhibitory

Amino acid modifications

Modified residue11N-acetylmethionine Ref.27 Ref.32
Modified residue3551Phosphoserine; by CK2 Probable

Natural variations

Alternative sequence1 – 7373Missing in isoform 3.
VSP_042806
Alternative sequence69 – 10133Missing in isoform 2.
VSP_001744
Alternative sequence70 – 8920LETCM…VGKFR → RRGEATIRPPPCDDTKGGQD in isoform 5.
VSP_042807
Alternative sequence90 – 639550Missing in isoform 5.
VSP_042808
Alternative sequence277 – 36387Missing in isoform 4.
VSP_042809
Natural variant2391G → S in a breast cancer sample; somatic mutation. Ref.36
VAR_036522
Natural variant4841P → A in a breast cancer sample; somatic mutation. Ref.36
VAR_036523

Experimental info

Mutagenesis921N → A: Abolishes interaction with IGF2R. Ref.15
Mutagenesis1821L → A: Abolishes interaction with ARF1, UBC and TSG101. Ref.24
Mutagenesis1941N → A: Abolishes interaction with ARF1 and RABEP1. Ref.24
Mutagenesis1971I → A: Abolishes interaction with ARF1, UBC and TSG101. Ref.24
Mutagenesis1981K → A: Abolishes interaction with ARF1. Ref.24
Mutagenesis2001M → A: Abolishes interaction with ARF1. Ref.24
Mutagenesis2041D → A: Abolishes interaction with ARF1. Ref.24
Mutagenesis2591M → K: Abolishes interaction with RABEP1.
Mutagenesis2601R → A: No effect on interaction with RABEP1. Ref.24
Mutagenesis2601R → E: Abolishes interaction with RABEP1 and UBC. Ref.24
Mutagenesis2641F → A: Abolishes interaction with RABEP1. Ref.24
Mutagenesis2671A → D: Abolishes interaction with RABEP1 and UBC. Ref.24
Mutagenesis2771L → A: Abolishes interaction with RABEP1, UBC and TSG101. Ref.24
Mutagenesis2811L → A: Abolishes interaction with RABEP1. Ref.24
Mutagenesis2841N → A: Abolishes interaction with RABEP1. Ref.24
Mutagenesis2841N → S: Abolishes interaction with RABEP1. Ref.24
Mutagenesis3551S → A: Increased interaction with IGF2R. Reduced phosphorylation. Ref.15
Mutagenesis3551S → D: Abolishes interaction with IGF2R. Ref.15
Mutagenesis356 – 3605LLDDE → AADAA: Partial loss of clathrin-binding. Ref.10
Mutagenesis3581D → A: Increased interaction with IGF2R. Ref.15
Mutagenesis361 – 3622LM → AA: Increased interaction with IGF2R.
Mutagenesis5631A → D: Abolishes interaction with CCDC91. Ref.21
Mutagenesis5641V → D: Abolishes interaction with CCDC91. Ref.21
Mutagenesis5701V → E: Abolishes interaction with CCDC91. Ref.21
Mutagenesis5721L → E: Abolishes interaction with CCDC91. Ref.21

Secondary structure

............................................................ 639
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: B0B6F089FA0F7DD5

FASTA63970,384
        10         20         30         40         50         60 
MEPAMEPETL EARINRATNP LNKELDWASI NGFCEQLNED FEGPPLATRL LAHKIQSPQE 

        70         80         90        100        110        120 
WEAIQALTVL ETCMKSCGKR FHDEVGKFRF LNELIKVVSP KYLGSRTSEK VKNKILELLY 

       130        140        150        160        170        180 
SWTVGLPEEV KIAEAYQMLK KQGIVKSDPK LPDDTTFPLP PPRPKNVIFE DEEKSKMLAR 

       190        200        210        220        230        240 
LLKSSHPEDL RAANKLIKEM VQEDQKRMEK ISKRVNAIEE VNNNVKLLTE MVMSHSQGGA 

       250        260        270        280        290        300 
AAGSSEDLMK ELYQRCERMR PTLFRLASDT EDNDEALAEI LQANDNLTQV INLYKQLVRG 

       310        320        330        340        350        360 
EEVNGDATAG SIPGSTSALL DLSGLDLPPA GTTYPAMPTR PGEQASPEQP SASVSLLDDE 

       370        380        390        400        410        420 
LMSLGLSDPT PPSGPSLDGT GWNSFQSSDA TEPPAPALAQ APSMESRPPA QTSLPASSGL 

       430        440        450        460        470        480 
DDLDLLGKTL LQQSLPPESQ QVRWEKQQPT PRLTLRDLQN KSSSCSSPSS SATSLLHTVS 

       490        500        510        520        530        540 
PEPPRPPQQP VPTELSLASI TVPLESIKPS NILPVTVYDQ HGFRILFHFA RDPLPGRSDV 

       550        560        570        580        590        600 
LVVVVSMLST APQPIRNIVF QSAVPKVMKV KLQPPSGTEL PAFNPIVHPS AITQVLLLAN 

       610        620        630 
PQKEKVRLRY KLTFTMGDQT YNEMGDVDQF PPPETWGSL 

« Hide

Isoform 2 [UniParc].

Checksum: 6231A20CC57997B1
Show »

FASTA60666,563
Isoform 3 [UniParc].

Checksum: F96825C24B633E03
Show »

FASTA56662,138
Isoform 4 [UniParc].

Checksum: AC507C9F975A32C3
Show »

FASTA55261,379
Isoform 5 [UniParc].

Checksum: F209D7D764D4CA7E
Show »

FASTA899,969

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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]"EpsinR: an AP1/clathrin interacting protein involved in vesicle trafficking."
Mills I.G., Praefcke G.J.K., Vallis Y., Peter B.J., Olesen L.E., Gallop J.L., Butler P.J.G., Evans P.R., McMahon H.T.
J. Cell Biol. 160:213-222(2003) [PubMed] [Europe PMC] [Abstract]
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]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] SER-239 AND ALA-484.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS13951.1. [Q9UJY5-1]
CCDS33643.1. [Q9UJY5-4]
CCDS46704.1. [Q9UJY5-5]
CCDS54526.1. [Q9UJY5-3]
PIRT14759.
RefSeqNP_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]
UniGeneHs.499158.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
DisProtDP00314.
ProteinModelPortalQ9UJY5.
SMRQ9UJY5. Positions 2-147, 171-302, 498-639.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117540. 43 interactions.
IntActQ9UJY5. 21 interactions.
MINTMINT-126174.
STRING9606.ENSP00000341344.

PTM databases

PhosphoSiteQ9UJY5.

Polymorphism databases

DMDM14548066.

Proteomic databases

MaxQBQ9UJY5.
PaxDbQ9UJY5.
PRIDEQ9UJY5.

Protocols and materials databases

DNASU26088.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000325180; ENSP00000321288; ENSG00000100083. [Q9UJY5-4]
ENST00000337437; ENSP00000338647; ENSG00000100083. [Q9UJY5-2]
ENST00000343632; ENSP00000341344; ENSG00000100083. [Q9UJY5-1]
ENST00000406772; ENSP00000385287; ENSG00000100083. [Q9UJY5-3]
ENST00000414350; ENSP00000414387; ENSG00000100083. [Q9UJY5-5]
GeneID26088.
KEGGhsa:26088.
UCSCuc003atb.3. human. [Q9UJY5-5]
uc003atc.3. human. [Q9UJY5-1]
uc003atd.3. human. [Q9UJY5-4]

Organism-specific databases

CTD26088.
GeneCardsGC22P038004.
HGNCHGNC:17842. GGA1.
HPAHPA048280.
HPA051016.
MIM606004. gene.
neXtProtNX_Q9UJY5.
PharmGKBPA28657.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG321636.
HOGENOMHOG000231169.
HOVERGENHBG015945.
KOK12404.
OrthoDBEOG7V49Z0.
PhylomeDBQ9UJY5.
TreeFamTF318574.

Gene expression databases

ArrayExpressQ9UJY5.
BgeeQ9UJY5.
CleanExHS_GGA1.
GenevestigatorQ9UJY5.

Family and domain databases

Gene3D1.25.40.90. 1 hit.
2.60.40.1230. 1 hit.
InterProIPR008152. 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]
PfamPF02883. Alpha_adaptinC2. 1 hit.
PF03127. GAT. 1 hit.
PF00790. VHS. 1 hit.
[Graphical view]
SMARTSM00809. Alpha_adaptinC2. 1 hit.
SM00288. VHS. 1 hit.
[Graphical view]
SUPFAMSSF48464. SSF48464. 1 hit.
SSF49348. SSF49348. 1 hit.
PROSITEPS50180. GAE. 1 hit.
PS50909. GAT. 1 hit.
PS50179. VHS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGGA1. human.
EvolutionaryTraceQ9UJY5.
GeneWikiGGA1.
GenomeRNAi26088.
NextBio48013.
PROQ9UJY5.
SOURCESearch...

Entry information

Entry nameGGA1_HUMAN
AccessionPrimary (citable) accession number: Q9UJY5
Secondary accession number(s): A8K3D3 expand/collapse secondary AC list , B0QYR7, Q5TG07, Q86YA9, Q8NCS6, Q9BW94, Q9UG00, Q9UGW0, Q9UGW1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 156 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM