Q9UJY5 (GGA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

GGA1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	639 AA.
Sequence status	Complete.
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.10
Subunit structure	Monomer. Interacts with NECAP1. Interacts with CNST 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, 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.28
Subcellular location	Golgi apparatus › trans-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.

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 Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	intracellular protein transport Traceable author statement PubMed 20211637. Source: UniProtKB vesicle-mediated transport Inferred from electronic annotation. Source: InterPro
Cellular_component	Golgi apparatus Traceable author statement PubMed 20214818. Source: UniProtKB 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
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
RABEP1	Q15276	8	EBI-447141,EBI-447043
RABGEF1	O18973	2	EBI-447141,EBI-447376	From a different organism.
RNF11	Q9Y3C5	2	EBI-447141,EBI-396669
UBB	P0CG47	3	EBI-447141,EBI-413034

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 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

355

1

Phosphoserine; by CK2 Probable

Natural variations

Alternative sequence

1 – 73

73

Missing in isoform 3.

VSP_042806

Alternative sequence

69 – 101

33

Missing in isoform 2.

VSP_001744

Alternative sequence

70 – 89

20

LETCM…VGKFR → RRGEATIRPPPCDDTKGGQD in isoform 5.

VSP_042807

Alternative sequence

90 – 639

550

Missing in isoform 5.

VSP_042808

Alternative sequence

277 – 363

87

Missing in isoform 4.

VSP_042809

Natural variant

239

1

G → S in a breast cancer sample; somatic mutation. Ref.33

VAR_036522

Natural variant

484

1

P → A in a breast cancer sample; somatic mutation. Ref.33

VAR_036523

Experimental info

Mutagenesis

92

1

N → A: Abolishes interaction with IGF2R. Ref.15

Mutagenesis

182

1

L → A: Abolishes interaction with ARF1, UBC and TSG101. Ref.24

Mutagenesis

194

1

N → A: Abolishes interaction with ARF1 and RABEP1. Ref.24

Mutagenesis

197

1

I → A: Abolishes interaction with ARF1, UBC and TSG101. Ref.24

Mutagenesis

198

1

K → A: Abolishes interaction with ARF1. Ref.24

Mutagenesis

200

1

M → A: Abolishes interaction with ARF1. Ref.24

Mutagenesis

204

1

D → A: Abolishes interaction with ARF1. Ref.24

Mutagenesis

259

1

M → K: Abolishes interaction with RABEP1.

Mutagenesis

260

1

R → A: No effect on interaction with RABEP1. Ref.24

Mutagenesis

260

1

R → E: Abolishes interaction with RABEP1 and UBC. Ref.24

Mutagenesis

264

1

F → A: Abolishes interaction with RABEP1. Ref.24

Mutagenesis

267

1

A → D: Abolishes interaction with RABEP1 and UBC. Ref.24

Mutagenesis

277

1

L → A: Abolishes interaction with RABEP1, UBC and TSG101. Ref.24

Mutagenesis

281

1

L → A: Abolishes interaction with RABEP1. Ref.24

Mutagenesis

284

1

N → A: Abolishes interaction with RABEP1. Ref.24

Mutagenesis

284

1

N → S: Abolishes interaction with RABEP1. Ref.24

Mutagenesis

355

1

S → A: Increased interaction with IGF2R. Reduced phosphorylation. Ref.15

Mutagenesis

355

1

S → D: Abolishes interaction with IGF2R. Ref.15

Mutagenesis

356 – 360

5

LLDDE → AADAA: Partial loss of clathrin-binding. Ref.10

Mutagenesis

358

1

D → A: Increased interaction with IGF2R. Ref.15

Mutagenesis

361 – 362

2

LM → AA: Increased interaction with IGF2R.

Mutagenesis

563

1

A → D: Abolishes interaction with CCDC91. Ref.21

Mutagenesis

564

1

V → D: Abolishes interaction with CCDC91. Ref.21

Mutagenesis

570

1

V → E: Abolishes interaction with CCDC91. Ref.21

Mutagenesis

572

1

L → E: Abolishes interaction with CCDC91. Ref.21

Secondary structure

1

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639

Helix Strand Turn

Details...

Helix

3 – 5

3

Helix

10 – 17

8

Helix

27 – 36

10

Helix

37 – 39

3

Beta strand

40 – 42

3

Helix

43 – 55

13

Helix

60 – 76

17

Helix

79 – 85

7

Helix

88 – 98

11

Turn

100 – 103

4

Helix

104 – 106

3

Helix

109 – 125

17

Helix

130 – 141

12

Helix

172 – 182

11

Helix

187 – 205

19

Helix

212 – 233

22

Turn

235 – 238

4

Helix

243 – 267

25

Helix

274 – 298

25

Helix

494 – 497

4

Helix

504 – 506

3

Beta strand

515 – 520

6

Beta strand

523 – 531

9

Beta strand

533 – 535

3

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 [UniParc]. 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
	Isoform 3 [UniParc]. Checksum: F96825C24B633E03	FASTA	566	62,138
	10 20 30 40 50 60 MKSCGKRFHD EVGKFRFLNE LIKVVSPKYL GSRTSEKVKN KILELLYSWT VGLPEEVKIA 70 80 90 100 110 120 EAYQMLKKQG IVKSDPKLPD DTTFPLPPPR PKNVIFEDEE KSKMLARLLK SSHPEDLRAA 130 140 150 160 170 180 NKLIKEMVQE DQKRMEKISK RVNAIEEVNN NVKLLTEMVM SHSQGGAAAG SSEDLMKELY 190 200 210 220 230 240 QRCERMRPTL FRLASDTEDN DEALAEILQA NDNLTQVINL YKQLVRGEEV NGDATAGSIP 250 260 270 280 290 300 GSTSALLDLS GLDLPPAGTT YPAMPTRPGE QASPEQPSAS VSLLDDELMS LGLSDPTPPS 310 320 330 340 350 360 GPSLDGTGWN SFQSSDATEP PAPALAQAPS MESRPPAQTS LPASSGLDDL DLLGKTLLQQ 370 380 390 400 410 420 SLPPESQQVR WEKQQPTPRL TLRDLQNKSS SCSSPSSSAT SLLHTVSPEP PRPPQQPVPT 430 440 450 460 470 480 ELSLASITVP LESIKPSNIL PVTVYDQHGF RILFHFARDP LPGRSDVLVV VVSMLSTAPQ 490 500 510 520 530 540 PIRNIVFQSA VPKVMKVKLQ PPSGTELPAF NPIVHPSAIT QVLLLANPQK EKVRLRYKLT 550 560 FTMGDQTYNE MGDVDQFPPP ETWGSL
	Isoform 4 [UniParc]. Checksum: AC507C9F975A32C3	FASTA	552	61,379
	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 EDNDEALGLS DPTPPSGPSL DGTGWNSFQS 310 320 330 340 350 360 SDATEPPAPA LAQAPSMESR PPAQTSLPAS SGLDDLDLLG KTLLQQSLPP ESQQVRWEKQ 370 380 390 400 410 420 QPTPRLTLRD LQNKSSSCSS PSSSATSLLH TVSPEPPRPP QQPVPTELSL ASITVPLESI 430 440 450 460 470 480 KPSNILPVTV YDQHGFRILF HFARDPLPGR SDVLVVVVSM LSTAPQPIRN IVFQSAVPKV 490 500 510 520 530 540 MKVKLQPPSG TELPAFNPIV HPSAITQVLL LANPQKEKVR LRYKLTFTMG DQTYNEMGDV 550 DQFPPPETWG SL
	Isoform 5 [UniParc]. Checksum: F209D7D764D4CA7E	FASTA	89	9,969
	10 20 30 40 50 60 MEPAMEPETL EARINRATNP LNKELDWASI NGFCEQLNED FEGPPLATRL LAHKIQSPQE 70 80 WEAIQALTVR RGEATIRPPP CDDTKGGQD

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] [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]	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. , 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]	"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.
[28]	"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.
[29]	"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].
[30]	"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.
[31]	"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.
[32]	"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.
[33]	"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] [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.

IPI

IPI00216337.
IPI00744361.

PIR

T14759.

RefSeq

NP_001001560.1. NM_001001560.2.
NP_001001561.1. NM_001001561.2.
NP_001166158.1. NM_001172687.1.
NP_001166159.1. NM_001172688.1.
NP_037497.1. NM_013365.4.

UniGene

Hs.499158.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

DisProt

DP00314.

ProteinModelPortal

Q9UJY5.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9UJY5. 12 interactions.

MINT

MINT-126174.

STRING

9606.ENSP00000341344.

PTM databases

PhosphoSite

Q9UJY5.

Polymorphism databases

DMDM

14548066.

Proteomic databases

PaxDb

Q9UJY5.

PRIDE

Q9UJY5.

Protocols and materials databases

DNASU

26088.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000325180; ENSP00000321288; ENSG00000100083.
ENST00000337437; ENSP00000338647; ENSG00000100083.
ENST00000343632; ENSP00000341344; ENSG00000100083.
ENST00000406772; ENSP00000385287; ENSG00000100083.
ENST00000414350; ENSP00000414387; ENSG00000100083.

GeneID

26088.

KEGG

hsa:26088.

UCSC

uc003atc.3. human.

Organism-specific databases

CTD

26088.

GeneCards

GC22P038004.

HGNC

HGNC:17842. GGA1.

HPA

HPA048280.
HPA051016.

MIM

606004. gene.

neXtProt

NX_Q9UJY5.

PharmGKB

PA28657.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG321636.

HOGENOM

HOG000231169.

HOVERGEN

HBG015945.

KO

K12404.

OrthoDB

EOG4J117V.

PhylomeDB

Q9UJY5.

Gene expression databases

ArrayExpress

Q9UJY5.

Bgee

Q9UJY5.

CleanEx

HS_GGA1.

Genevestigator

Q9UJY5.

GermOnline

ENSG00000100083. Homo sapiens.

Family and domain databases

Gene3D

1.25.40.90. 1 hit.
2.60.40.1230. 1 hit.

InterPro

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]

Pfam

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

SMART

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

SUPFAM

SSF49348. Clath_adapt. 1 hit.
SSF48464. ENTH_VHS. 1 hit.

PROSITE

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

ProtoNet

Search...

Other

ChiTaRS

GGA1. human.

EvolutionaryTrace

Q9UJY5.

GenomeRNAi

26088.

NextBio

48013.

SOURCE

Search...

Entry information

Entry name

GGA1_HUMAN

Accession

Primary (citable) accession number: Q9UJY5
Secondary accession number(s): A8K3D3 , 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:	May 1, 2013
This is version 144 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.