Reviewed, UniProtKB/Swiss-Prot Q9UJY5 (GGA1_HUMAN)

Names and origin

Protein names

Recommended name:
    ADP-ribosylation factor-binding protein GGA1
Alternative name(s):
    Golgi-localized, gamma ear-containing, ARF-binding protein 1
    Gamma-adaptin-related protein 1

Gene names

Name:

GGA1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	639 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.9
Subunit structure	Monomeric. Interacts with NECAP1 By similarity. Interacts with GGA2 and GGA3. Binds to clathrin and activated ARFs. 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, AP1GBP1, EPN4, NECAP2 and AFTPH/aftiphilin. Interacts with TSG101 and UBC.
Subcellular location	Golgi apparatus › trans-Golgi network membrane; Peripheral membrane protein. Endosome membrane; Peripheral membrane protein. Ref.19 Ref.24
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. Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.14 Ref.17 Ref.25 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.

Ontologies

Keywords
Biological process	Protein transport Transport
Cellular component	Endosome Golgi apparatus Membrane
Coding sequence diversity	Alternative splicing Polymorphism
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure
Gene Ontology (GO)
Biological process	intracellular protein transport Traceable author statement. Source: UniProtKB vesicle-mediated transport Inferred from electronic annotation. Source: InterPro
Cellular component	Golgi apparatus part Inferred from electronic annotation. Source: InterPro clathrin adaptor complex Inferred from electronic annotation. Source: InterPro endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	protein binding Ref.16 Ref.23 Ref.28 Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Arf2	Q8BSL7	1	EBI-447141,EBI-931380	From a different organism.
RABEP1	Q15276	4	EBI-447141,EBI-447043
RABGEF1	O18973	1	EBI-447141,EBI-447376	From a different organism.
RPS27A	P62988	1	EBI-447141,EBI-413034

Alternative products

This entry describes 2 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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 639

639

ADP-ribosylation factor-binding protein GGA1

PRO_0000212680

Regions

Domain

17 – 147

131

VHS

Domain

171 – 299

129

GAT

Domain

510 – 631

122

GAE

Region

114 – 274

161

Interaction with ARF3

Region

300 – 509

210

Unstructured hinge

Motif

358 – 362

5

Autoinhibitory

Amino acid modifications

Modified residue

236

1

Phosphoserine Ref.25

Modified residue

355

1

Phosphoserine; by CK2 Probable

Natural variations

Alternative sequence

69 – 101

33

Missing in isoform 2.

VSP_001744

Natural variant

239

1

G → S in a breast cancer sample; somatic mutation. Ref.30

VAR_036522

Natural variant

484

1

P → A in a breast cancer sample; somatic mutation. Ref.30

VAR_036523

Experimental info

Mutagenesis

92

1

N → A: Abolishes interaction with IGF2R. Ref.14

Mutagenesis

182

1

L → A: Abolishes interaction with ARF1, UBC and TSG101. Ref.23

Mutagenesis

194

1

N → A: Abolishes interaction with ARF1 and RABEP1. Ref.23

Mutagenesis

197

1

I → A: Abolishes interaction with ARF1, UBC and TSG101. Ref.23

Mutagenesis

198

1

K → A: Abolishes interaction with ARF1. Ref.23

Mutagenesis

200

1

M → A: Abolishes interaction with ARF1. Ref.23

Mutagenesis

204

1

D → A: Abolishes interaction with ARF1. Ref.23

Mutagenesis

259

1

M → K: Abolishes interaction with RABEP1.

Mutagenesis

260

1

R → A: No effect on interaction with RABEP1. Ref.23

Mutagenesis

260

1

R → E: Abolishes interaction with RABEP1 and UBC. Ref.23

Mutagenesis

264

1

F → A: Abolishes interaction with RABEP1. Ref.23

Mutagenesis

267

1

A → D: Abolishes interaction with RABEP1 and UBC. Ref.23

Mutagenesis

277

1

L → A: Abolishes interaction with RABEP1, UBC and TSG101. Ref.23

Mutagenesis

281

1

L → A: Abolishes interaction with RABEP1. Ref.23

Mutagenesis

284

1

N → A: Abolishes interaction with RABEP1. Ref.23

Mutagenesis

284

1

N → S: Abolishes interaction with RABEP1. Ref.23

Mutagenesis

355

1

S → A: Increased interaction with IGF2R. Reduced phosphorylation. Ref.14

Mutagenesis

355

1

S → D: Abolishes interaction with IGF2R. Ref.14

Mutagenesis

356 – 360

5

LLDDE → AADAA: Partial loss of clathrin-binding. Ref.9

Mutagenesis

358

1

D → A: Increased interaction with IGF2R. Ref.14

Mutagenesis

361 – 362

2

LM → AA: Increased interaction with IGF2R.

Mutagenesis

563

1

A → D: Abolishes interaction with CCDC91. Ref.20

Mutagenesis

564

1

V → D: Abolishes interaction with CCDC91. Ref.20

Mutagenesis

570

1

V → E: Abolishes interaction with CCDC91. Ref.20

Mutagenesis

572

1

L → E: Abolishes interaction with CCDC91. Ref.20

Secondary structure

1

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639

Helix Strand Turn

Details...

Helix

3 – 5

3

Helix

10 – 17

8

Helix

27 – 38

12

Helix

43 – 55

13

Helix

60 – 76

17

Helix

78 – 85

8

Helix

88 – 98

11

Turn

100 – 106

7

Helix

109 – 125

17

Helix

130 – 141

12

Helix

172 – 182

11

Helix

187 – 205

19

Helix

209 – 234

26

Helix

246 – 257

12

Helix

259 – 267

9

Helix

274 – 297

24

Turn

298 – 300

3

Helix

494 – 497

4

Helix

504 – 506

3

Beta strand

515 – 520

6

Beta strand

523 – 531

9

Beta strand

540 – 549

10

Beta strand

555 – 563

9

Beta strand

568 – 572

5

Beta strand

592 – 599

8

Beta strand

608 – 616

9

Beta strand

619 – 627

9

Turn

633 – 635

3

Helix

636 – 638

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: B0B6F089FA0F7DD5	FASTA	639	70,384
	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
	Isoform 2. Checksum: 6231A20CC57997B1	FASTA	606	66,563
	10 20 30 40 50 60 MEPAMEPETL EARINRATNP LNKELDWASI NGFCEQLNED FEGPPLATRL LAHKIQSPQE 70 80 90 100 110 120 WEAIQALTYL GSRTSEKVKN KILELLYSWT VGLPEEVKIA EAYQMLKKQG IVKSDPKLPD 130 140 150 160 170 180 DTTFPLPPPR PKNVIFEDEE KSKMLARLLK SSHPEDLRAA NKLIKEMVQE DQKRMEKISK 190 200 210 220 230 240 RVNAIEEVNN NVKLLTEMVM SHSQGGAAAG SSEDLMKELY QRCERMRPTL FRLASDTEDN 250 260 270 280 290 300 DEALAEILQA NDNLTQVINL YKQLVRGEEV NGDATAGSIP GSTSALLDLS GLDLPPAGTT 310 320 330 340 350 360 YPAMPTRPGE QASPEQPSAS VSLLDDELMS LGLSDPTPPS GPSLDGTGWN SFQSSDATEP 370 380 390 400 410 420 PAPALAQAPS MESRPPAQTS LPASSGLDDL DLLGKTLLQQ SLPPESQQVR WEKQQPTPRL 430 440 450 460 470 480 TLRDLQNKSS SCSSPSSSAT SLLHTVSPEP PRPPQQPVPT ELSLASITVP LESIKPSNIL 490 500 510 520 530 540 PVTVYDQHGF RILFHFARDP LPGRSDVLVV VVSMLSTAPQ PIRNIVFQSA VPKVMKVKLQ 550 560 570 580 590 600 PPSGTELPAF NPIVHPSAIT QVLLLANPQK EKVRLRYKLT FTMGDQTYNE MGDVDQFPPP ETWGSL

References

	« Hide 'large scale' referencesShow '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: 10749927] [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: 10747089] [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: 10747088] [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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[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: 10591208] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2).
[6]	"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., Blocker H., Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., Ottenwalder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 31-639 (ISOFORM 1). Tissue: Testis.
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 275-639. 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: 10814529] [Abstract] Cited for: INTERACTION WITH AP1GBP1.
[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: 11301005] [Abstract] Cited for: INTERACTION WITH CLATHRIN, FUNCTION, MUTAGENESIS OF 356-LEU--GLU-360.
[10]	"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: 11390366] [Abstract] Cited for: INTERACTION WITH SORT1; LRP3 AND IGF2R.
[11]	"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: 11387475] [Abstract] Cited for: INTERACTION WITH M6PR AND IGF2R.
[12]	"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: 11950392] [Abstract] Cited for: INTERACTION WITH ARF1; ARF5 AND ARF6.
[13]	"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: 11821067] [Abstract] Cited for: INTERACTION WITH SORT1 AND SORL1.
[14]	"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: 12060753] [Abstract] Cited for: MUTAGENESIS OF ASN-92; SER-355; ASP-358 AND 361-LEU-MET-362, PHOSPHORYLATION AT SER-355, INTERACTION WITH IGF2R.
[15]	"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: 14567678] [Abstract] Cited for: INTERACTION WITH BACE1.
[16]	"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: 12505986] [Abstract] Cited for: INTERACTION WITH RABEP1 AND RABGEF1.
[17]	"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: 12578827] [Abstract] Cited for: REGULATION BY PHOSPHORYLATION, DEPHOSPHORYLATION BY PP2A.
[18]	"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: 12538641] [Abstract] Cited for: INTERACTION WITH EPN4.
[19]	"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: 14638859] [Abstract] Cited for: INTERACTION WITH GGA2 AND GGA3, SUBCELLULAR LOCATION.
[20]	"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: 12808037] [Abstract] Cited for: INTERACTION WITH CCDC91; P200 AND AP1GBP1, MUTAGENESIS OF ALA-563; VAL-564; VAL-570 AND LEU-572.
[21]	"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: 14660606] [Abstract] Cited for: INTERACTION WITH UBC.
[22]	"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: 14665628] [Abstract] Cited for: INTERACTION WITH NECAP2 AND AFTPH.
[23]	"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: 15143060] [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.
[24]	"Interactions of GGA3 with the ubiquitin sorting machinery." Puertollano R., Bonifacino J.S. Nat. Cell Biol. 6:244-251(2004) [PubMed: 15039775] [Abstract] Cited for: SUBCELLULAR LOCATION.
[25]	"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: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-236, MASS SPECTROMETRY.
[26]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[27]	"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: 11859376] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-147.
[28]	"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: 12679809] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 168-208 IN COMPLEX WITH MOUSE ARF1.
[29]	"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: 12858163] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2-16 IN COMPLEX WITH CCDC91.
[30]	"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. , 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: 16959974] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] SER-239 AND ALA-484.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AF190862 mRNA. Translation: AAF05707.1.
AF218584 mRNA. Translation: AAF42847.1.
AF233521 mRNA. Translation: AAF35393.1.
AK075256 mRNA. Translation: BAC11501.1.
AL035496, Z83844 Genomic DNA. Translation: CAI20951.1.
Z83844, AL035496 Genomic DNA. Translation: CAI20369.1.
AL110219 mRNA. Translation: CAB53679.1.
BC000538 mRNA. Translation: AAH00538.2.

IPI

IPI00216337.
IPI00744361.

PIR

T14759.

RefSeq

NP_001001560.1.
NP_001001561.1.
NP_037497.1.

UniGene

Hs.499158

3D structure databases

PDBPDBe

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	[»]

DisProt

DP00314.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9UJY5. 6 interactions.

PTM databases

PhosphoSite

Q9UJY5.

Proteomic databases

PRIDE

Q9UJY5.

Genome annotation databases

Ensembl

ENSG00000100083. Homo sapiens. [Contig view]

GeneID

26088.

KEGG

hsa:26088.

Organism-specific databases

GeneCards

GC22P036329.

H-InvDB

HIX0016447.

HGNC

HGNC:17842. GGA1.

MIM

606004. gene.

PharmGKB

PA28657.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

Q9UJY5.

Gene expression databases

ArrayExpress

Q9UJY5.

Bgee

Q9UJY5.

CleanEx

HS_GGA1.

GermOnline

ENSG00000100083. Homo sapiens.

Family and domain databases

InterPro

IPR008152. Clathrin_a/b/g-adaptin_app_Ig.
IPR008153. Clathrin_g-adaptin_app.
IPR008942. ENTH_VHS.
IPR004152. GAT.
IPR002014. VHS.
IPR018205. VHS_subgroup.
[Graphical view]

Gene3D

G3DSA:2.60.40.1230. Clathrin_g-adaptin_app. 1 hit.
G3DSA:1.25.40.90. ENTH_VHS. 1 hit.

Pfam

PF02883. Alpha_adaptinC2. 1 hit.
PF03127. GAT. 1 hit.
PF00790. VHS. 1 hit.
[Graphical view]

ProDom

PD021457. Gamma_adaptin_C. 1 hit.
PD003686. VHS. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00809. Alpha_adaptinC2. 1 hit.
SM00288. VHS. 1 hit.
[Graphical view]

PROSITE

PS50180. GAE. 1 hit.
PS50909. GAT. 1 hit.
PS50179. VHS. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

48013.

SOURCE

Search...

Entry information

Entry name

GGA1_HUMAN

Accession

Primary (citable) accession number: Q9UJY5
Secondary accession number(s): Q5TG07 , Q9BW94, Q9UG00, Q9UGW0, Q9UGW1

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2001
Last sequence update:	May 1, 2000
Last modified:	June 16, 2009
This is version 102 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)