Q9NZ52 (GGA3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ADP-ribosylation factor-binding protein GGA3

Alternative name(s):
Golgi-localized, gamma ear-containing, ARF-binding protein 3

Gene names

Name:	GGA3
Synonyms:	KIAA0154

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	723 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.8
Subunit structure	Monomer. Interacts with SORT1, SORL1, LRP3, GGA binding partner (GGABP) and P200 By similarity. Interacts with GGA1 and GGA2. Binds to clathrin and activated ARFs. Binds RABEP1 and RABGEF1. Interacts with the membrane proteins M6PR/CD-MPR, IGF2R/CI-MPR and BACE1 and the accessory proteins SYNRG, EPN4, NECAP1, NECAP2 and AFTPH/aftiphilin. Interacts with TSG101 and UBC. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19
Subcellular location	Golgi apparatus › trans-Golgi network membrane; Peripheral membrane protein. Endosome membrane; Peripheral membrane protein Ref.19.
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 and an autoinhibitory (AC-LL) motifs. The GAE domain binds accessory proteins regulating GGAs function.
Post-translational modification	Phosphorylated by CK2 and dephosphorylated by PP2A By similarity. Phosphorylation of GGA3 allows the internal AC-LL motif to bind the VHS domain and to inhibit the recognition of cargo signals. Ubiquitinated. Ref.16
Sequence similarities	Belongs to the GGA protein family. Contains 1 GAE domain. Contains 1 GAT domain. Contains 1 VHS domain.
Sequence caution	The sequence BAA09926.1 differs from that shown. Reason: Erroneous initiation.

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 Non-traceable author statement Ref.2. 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 trans-Golgi network Inferred from direct assay Ref.2. Source: UniProtKB
Molecular_function	ADP-ribosylation factor binding Inferred from direct assay Ref.2. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
RABEP1	Q15276	4	EBI-447404,EBI-447043
UBB	P0CG47	2	EBI-447404,EBI-413034

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform Long (identifier: Q9NZ52-1)

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 Short (identifier: Q9NZ52-2)

The sequence of this isoform differs from the canonical sequence as follows:
     68-100: Missing.

Isoform 3 (identifier: Q9NZ52-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-122: Missing.
     688-723: EKVRLRYKLTFALGEQLSTEVGEVDQFPPVEQWGNL → KQVLSFLGKACLQPWGQAILLTTSCLA

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 723

723

ADP-ribosylation factor-binding protein GGA3

PRO_0000212684

Regions

Domain

16 – 146

131

VHS

Domain

171 – 298

128

GAT

Domain

594 – 715

122

GAE

Region

1 – 313

313

Binds to ARF1 (in long isoform)

Region

299 – 593

295

Unstructured hinge

Motif

391 – 395

5

Autoinhibitory

Compositional bias

357 – 360

4

Poly-Pro

Compositional bias

453 – 457

5

Poly-Ser

Compositional bias

624 – 629

6

Poly-Val

Natural variations

Alternative sequence

1 – 122

122

Missing in isoform 3.

VSP_045133

Alternative sequence

68 – 100

33

Missing in isoform Short.

VSP_001745

Alternative sequence

688 – 723

36

EKVRL…QWGNL → KQVLSFLGKACLQPWGQAIL LTTSCLA in isoform 3.

VSP_045134

Natural variant

574

1

P → L in a breast cancer sample; somatic mutation. Ref.22

VAR_036524

Experimental info

Mutagenesis

194

1

N → A: Loss of interaction with ARF1 and Golgi localization. Ref.8

Mutagenesis

199

1

S → P: Loss of interaction with ARF1 and Golgi localization. Ref.8

Mutagenesis

217

1

T → P: Loss of interaction with ARF1 and Golgi localization. Ref.8

Mutagenesis

247

1

L → P: Loss of UBC-binding and ubiquitination. Ref.16

Mutagenesis

258

1

K → M: No effect. Confers an affinity to RABEP1 identical to GGA1; when associated with N-283. Ref.18

Mutagenesis

262

1

L → S: Loss of UBC-binding and ubiquitination. Ref.16

Mutagenesis

276

1

L → A: Loss of UBC-binding and ubiquitination. Ref.16 Ref.19

Mutagenesis

276

1

L → S: Loss of UBC-binding and ubiquitination. Ref.16 Ref.19

Mutagenesis

280

1

L → R: Loss of UBC-binding and ubiquitination. Ref.16

Mutagenesis

283

1

S → N: Can bind RABEP1. Confers an affinity to RABEP1 identical to GGA1; when associated with M-258. Ref.18

Mutagenesis

284

1

D → G: Loss of UBC-binding and ubiquitination. Ref.16

Mutagenesis

293

1

Y → H: Loss of UBC-binding and ubiquitination. Ref.16

Mutagenesis

391 – 395

5

DEELL → AAAAA: Increased binding to IGF2R. Ref.12

Sequence conflict

448

1

Q → K in AAH70044. Ref.6

Secondary structure

1

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723

Helix Strand Turn

Details...

Helix

9 – 16

8

Helix

26 – 38

13

Helix

42 – 54

13

Helix

59 – 75

17

Helix

77 – 84

8

Helix

87 – 97

11

Helix

99 – 103

5

Helix

108 – 124

17

Helix

129 – 140

12

Helix

218 – 231

14

Turn

232 – 234

3

Turn

237 – 239

3

Helix

242 – 267

26

Helix

276 – 290

15

Helix

292 – 295

4

Turn

296 – 298

3

Helix

588 – 590

3

Beta strand

599 – 604

6

Beta strand

607 – 616

10

Beta strand

624 – 633

10

Beta strand

635 – 637

3

Beta strand

639 – 647

9

Beta strand

652 – 656

5

Beta strand

675 – 683

9

Beta strand

692 – 700

9

Beta strand

703 – 711

9

Helix

717 – 719

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform Long [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 4F80D6032239168C	FASTA	723	78,315
	10 20 30 40 50 60 MAEAEGESLE SWLNKATNPS NRQEDWEYII GFCDQINKEL EGPQIAVRLL AHKIQSPQEW 70 80 90 100 110 120 EALQALTVLE ACMKNCGRRF HNEVGKFRFL NELIKVVSPK YLGDRVSEKV KTKVIELLYS 130 140 150 160 170 180 WTMALPEEAK IKDAYHMLKR QGIVQSDPPI PVDRTLIPSP PPRPKNPVFD DEEKSKLLAK 190 200 210 220 230 240 LLKSKNPDDL QEANKLIKSM VKEDEARIQK VTKRLHTLEE VNNNVRLLSE MLLHYSQEDS 250 260 270 280 290 300 SDGDRELMKE LFDQCENKRR TLFKLASETE DNDNSLGDIL QASDNLSRVI NSYKTIIEGQ 310 320 330 340 350 360 VINGEVATLT LPDSEGNSQC SNQGTLIDLA ELDTTNSLSS VLAPAPTPPS SGIPILPPPP 370 380 390 400 410 420 QASGPPRSRS SSQAEATLGP SSTSNALSWL DEELLCLGLA DPAPNVPPKE SAGNSQWHLL 430 440 450 460 470 480 QREQSDLDFF SPRPGTAACG ASDAPLLQPS APSSSSSQAP LPPPFPAPVV PASVPAPSAG 490 500 510 520 530 540 SSLFSTGVAP ALAPKVEPAV PGHHGLALGN SALHHLDALD QLLEEAKVTS GLVKPTTSPL 550 560 570 580 590 600 IPTTTPARPL LPFSTGPGSP LFQPLSFQSQ GSPPKGPELS LASIHVPLES IKPSSALPVT 610 620 630 640 650 660 AYDKNGFRIL FHFAKECPPG RPDVLVVVVS MLNTAPLPVK SIVLQAAVPK SMKVKLQPPS 670 680 690 700 710 720 GTELSPFSPI QPPAAITQVM LLANPLKEKV RLRYKLTFAL GEQLSTEVGE VDQFPPVEQW GNL
	Isoform Short [UniParc]. Checksum: E3A1C841AB3966C8	FASTA	690	74,470
	10 20 30 40 50 60 MAEAEGESLE SWLNKATNPS NRQEDWEYII GFCDQINKEL EGPQIAVRLL AHKIQSPQEW 70 80 90 100 110 120 EALQALTYLG DRVSEKVKTK VIELLYSWTM ALPEEAKIKD AYHMLKRQGI VQSDPPIPVD 130 140 150 160 170 180 RTLIPSPPPR PKNPVFDDEE KSKLLAKLLK SKNPDDLQEA NKLIKSMVKE DEARIQKVTK 190 200 210 220 230 240 RLHTLEEVNN NVRLLSEMLL HYSQEDSSDG DRELMKELFD QCENKRRTLF KLASETEDND 250 260 270 280 290 300 NSLGDILQAS DNLSRVINSY KTIIEGQVIN GEVATLTLPD SEGNSQCSNQ GTLIDLAELD 310 320 330 340 350 360 TTNSLSSVLA PAPTPPSSGI PILPPPPQAS GPPRSRSSSQ AEATLGPSST SNALSWLDEE 370 380 390 400 410 420 LLCLGLADPA PNVPPKESAG NSQWHLLQRE QSDLDFFSPR PGTAACGASD APLLQPSAPS 430 440 450 460 470 480 SSSSQAPLPP PFPAPVVPAS VPAPSAGSSL FSTGVAPALA PKVEPAVPGH HGLALGNSAL 490 500 510 520 530 540 HHLDALDQLL EEAKVTSGLV KPTTSPLIPT TTPARPLLPF STGPGSPLFQ PLSFQSQGSP 550 560 570 580 590 600 PKGPELSLAS IHVPLESIKP SSALPVTAYD KNGFRILFHF AKECPPGRPD VLVVVVSMLN 610 620 630 640 650 660 TAPLPVKSIV LQAAVPKSMK VKLQPPSGTE LSPFSPIQPP AAITQVMLLA NPLKEKVRLR 670 680 690 YKLTFALGEQ LSTEVGEVDQ FPPVEQWGNL
	Isoform 3 [UniParc]. Checksum: CACD3268CEE80BBE	FASTA	592	62,921
	10 20 30 40 50 60 MALPEEAKIK DAYHMLKRQG IVQSDPPIPV DRTLIPSPPP RPKNPVFDDE EKSKLLAKLL 70 80 90 100 110 120 KSKNPDDLQE ANKLIKSMVK EDEARIQKVT KRLHTLEEVN NNVRLLSEML LHYSQEDSSD 130 140 150 160 170 180 GDRELMKELF DQCENKRRTL FKLASETEDN DNSLGDILQA SDNLSRVINS YKTIIEGQVI 190 200 210 220 230 240 NGEVATLTLP DSEGNSQCSN QGTLIDLAEL DTTNSLSSVL APAPTPPSSG IPILPPPPQA 250 260 270 280 290 300 SGPPRSRSSS QAEATLGPSS TSNALSWLDE ELLCLGLADP APNVPPKESA GNSQWHLLQR 310 320 330 340 350 360 EQSDLDFFSP RPGTAACGAS DAPLLQPSAP SSSSSQAPLP PPFPAPVVPA SVPAPSAGSS 370 380 390 400 410 420 LFSTGVAPAL APKVEPAVPG HHGLALGNSA LHHLDALDQL LEEAKVTSGL VKPTTSPLIP 430 440 450 460 470 480 TTTPARPLLP FSTGPGSPLF QPLSFQSQGS PPKGPELSLA SIHVPLESIK PSSALPVTAY 490 500 510 520 530 540 DKNGFRILFH FAKECPPGRP DVLVVVVSML NTAPLPVKSI VLQAAVPKSM KVKLQPPSGT 550 560 570 580 590 ELSPFSPIQP PAAITQVMLL ANPLKKQVLS FLGKACLQPW GQAILLTTSC LA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"GGAs: a family of ADP ribosylation factor-binding proteins related to adaptors and associated with the Golgi complex." Dell'Angelica E.C., Puertollano R., Mullins C., Aguilar R.C., Vargas J.D., Hartnell L.M., Bonifacino J.S. J. Cell Biol. 149:81-94(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT). Tissue: Heart.
[2]	"A family of ADP-ribosylation factor effectors that can alter transport through the trans-Golgi." Boman A.L., Zhang C.-J., Zhu X., Kahn R.A. Mol. Biol. Cell 11:1241-1255(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
[3]	"Prediction of the coding sequences of unidentified human genes. IV. The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of cDNA clones from human cell line KG-1." Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N. DNA Res. 2:167-174(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT). Tissue: Bone marrow.
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). Tissue: Testis.
[5]	"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage." Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C. Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT). Tissue: Brain.
[7]	"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.
[8]	"The GGAs promote ARF-dependent recruitment of clathrin to the TGN." Puertollano R., Randazzo P.A., Presley J.F., Hartnell L.M., Bonifacino J.S. Cell 105:93-102(2001) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF ASN-194; SER-199 AND THR-217, INTERACTION WITH ARF1 AND CLATHRIN, FUNCTION.
[9]	"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.
[10]	"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.
[11]	"Enthoprotin: a novel clathrin-associated protein identified through subcellular proteomics." Wasiak S., Legendre-Guillemin V., Puertollano R., Blondeau F., Girard M., de Heuvel E., Boismenu D., Bell A.W., Bonifacino J.S., McPherson P.S. J. Cell Biol. 158:855-862(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH EPN4.
[12]	"Autoinhibition of the ligand-binding site of GGA1/3 VHS domains by an internal acidic cluster-dileucine motif." Doray B., Bruns K., Ghosh P., Kornfeld S.A. Proc. Natl. Acad. Sci. U.S.A. 99:8072-8077(2002) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF 391-ASP--LEU-395, INTERACTION WITH IGF2R, AUTOINHIBITION.
[13]	"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.
[14]	"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.
[15]	"Mammalian GGAs act together to sort mannose 6-phosphate receptors." Ghosh P., Griffith J., Geuze H.J., Kornfeld S. J. Cell Biol. 163:755-766(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH GGA1 AND GGA2.
[16]	"GAT (GGA and Tom1) domain responsible for ubiquitin binding and ubiquitination." Shiba Y., Katoh Y., Shiba T., Yoshino K., Takatsu H., Kobayashi H., Shin H.-W., Wakatsuki S., Nakayama K. J. Biol. Chem. 279:7105-7111(2004) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF LEU-247; LEU-262; LEU-276; LEU-280; ASP-284 AND TYR-293, INTERACTION WITH UBC, UBIQUITINATION.
[17]	"Definition of the consensus motif recognized by gamma-adaptin ear domains." Mattera R., Ritter B., Sidhu S.S., McPherson P.S., Bonifacino J.S. J. Biol. Chem. 279:8018-8028(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NECAP1; NECAP2 AND AFTPH.
[18]	"The trihelical bundle subdomain of the GGA proteins interacts with multiple partners through overlapping but distinct sites." Mattera R., Puertollano R., Smith W.J., Bonifacino J.S. J. Biol. Chem. 279:31409-31418(2004) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF LYS-258 AND SER-283, INTERACTION WITH RABEP1.
[19]	"Interactions of GGA3 with the ubiquitin sorting machinery." Puertollano R., Bonifacino J.S. Nat. Cell Biol. 6:244-251(2004) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF LEU-276, INTERACTION WITH UBC AND TSG101.
[20]	"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].
[21]	"Phosphoregulation of sorting signal-VHS domain interactions by a direct electrostatic mechanism." Kato Y., Misra S., Puertollano R., Hurley J.H., Bonifacino J.S. Nat. Struct. Biol. 9:532-536(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-166.
[22]	"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: VARIANT [LARGE SCALE ANALYSIS] LEU-574.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF219138 mRNA. Translation: AAF42848.1.
AF190864 mRNA. Translation: AAF05709.1.
AF219139 mRNA. Translation: AAF42849.1.
D63876 mRNA. Translation: BAA09926.1. Different initiation.
AK301895 mRNA. Translation: BAH13578.1.
AC022211 Genomic DNA. No translation available.
BC070044 mRNA. Translation: AAH70044.1.

IPI

IPI00021174.
IPI00219305.

RefSeq

NP_001166174.1. NM_001172703.1.
NP_001166175.1. NM_001172704.1.
NP_054720.1. NM_014001.3.
NP_619525.1. NM_138619.2.

UniGene

Hs.87726.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1JPL	X-ray	2.40	A/B/C/D	1-166	[»]
1JUQ	X-ray	2.20	A/B/C/D	1-166	[»]
1LF8	X-ray	2.30	A/B/C/D	1-166	[»]
1P4U	X-ray	2.20	A	571-723	[»]
1WR6	X-ray	2.60	A/B/C/D	209-319	[»]
1YD8	X-ray	2.80	G/H	208-301	[»]

ProteinModelPortal

Q9NZ52.

ModBase

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Protein-protein interaction databases

IntAct

Q9NZ52. 4 interactions.

MINT

MINT-126320.

STRING

9606.ENSP00000245541.

PTM databases

PhosphoSite

Q9NZ52.

Polymorphism databases

DMDM

14548064.

Proteomic databases

PaxDb

Q9NZ52.

PRIDE

Q9NZ52.

Protocols and materials databases

StructuralBiologyKnowledgebase

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Genome annotation databases

Ensembl

ENST00000245541; ENSP00000245541; ENSG00000125447.
ENST00000351904; ENSP00000326575; ENSG00000125447.
ENST00000578348; ENSP00000463288; ENSG00000125447.

GeneID

23163.

KEGG

hsa:23163.

UCSC

uc002jni.2. human.
uc002jnj.2. human.

Organism-specific databases

CTD

23163.

GeneCards

GC17M073229.

HGNC

HGNC:17079. GGA3.

HPA

HPA022945.

MIM

606006. gene.

neXtProt

NX_Q9NZ52.

PharmGKB

PA28659.

HUGE

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GenAtlas

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Phylogenomic databases

eggNOG

NOG321636.

HOGENOM

HOG000231169.

HOVERGEN

HBG015945.

InParanoid

Q9NZ52.

KO

K12404.

OMA

IPMDRTL.

OrthoDB

EOG4W0XCS.

PhylomeDB

Q9NZ52.

Enzyme and pathway databases

Pathway_Interaction_DB

arf_3pathway. Arf1 pathway.

Gene expression databases

ArrayExpress

Q9NZ52.

Bgee

Q9NZ52.

CleanEx

HS_GGA3.

Genevestigator

Q9NZ52.

GermOnline

ENSG00000125447. 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

EvolutionaryTrace

Q9NZ52.

GenomeRNAi

23163.

NextBio

44545.

SOURCE

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Entry information

Entry name

GGA3_HUMAN

Accession

Primary (citable) accession number: Q9NZ52
Secondary accession number(s): B7Z7E2 , Q15017, Q6IS16, Q9UJY3

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2001
Last sequence update:	October 1, 2000
Last modified:	May 1, 2013
This is version 139 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.