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Q9NZ52 (GGA3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 152. 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 GGA3
Alternative name(s):
Golgi-localized, gamma ear-containing, ARF-binding protein 3
Gene names
Name:GGA3
Synonyms:KIAA0154
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length723 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.9

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.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20

Subcellular location

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

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.17

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.

Binary interactions

Alternative products

This entry describes 4 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
Isoform 4 (identifier: Q9NZ52-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-72: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 723723ADP-ribosylation factor-binding protein GGA3
PRO_0000212684

Regions

Domain16 – 146131VHS
Domain171 – 298128GAT
Domain594 – 715122GAE
Region1 – 313313Binds to ARF1 (in long isoform)
Region299 – 593295Unstructured hinge
Motif391 – 3955Autoinhibitory
Compositional bias357 – 3604Poly-Pro
Compositional bias453 – 4575Poly-Ser
Compositional bias624 – 6296Poly-Val

Natural variations

Alternative sequence1 – 122122Missing in isoform 3.
VSP_045133
Alternative sequence1 – 7272Missing in isoform 4.
VSP_046868
Alternative sequence68 – 10033Missing in isoform Short.
VSP_001745
Alternative sequence688 – 72336EKVRL…QWGNL → KQVLSFLGKACLQPWGQAIL LTTSCLA in isoform 3.
VSP_045134
Natural variant5741P → L in a breast cancer sample; somatic mutation. Ref.23
VAR_036524

Experimental info

Mutagenesis1941N → A: Loss of interaction with ARF1 and Golgi localization. Ref.9
Mutagenesis1991S → P: Loss of interaction with ARF1 and Golgi localization. Ref.9
Mutagenesis2171T → P: Loss of interaction with ARF1 and Golgi localization. Ref.9
Mutagenesis2471L → P: Loss of UBC-binding and ubiquitination. Ref.17
Mutagenesis2581K → M: No effect. Confers an affinity to RABEP1 identical to GGA1; when associated with N-283. Ref.19
Mutagenesis2621L → S: Loss of UBC-binding and ubiquitination. Ref.17
Mutagenesis2761L → A: Loss of UBC-binding and ubiquitination. Ref.17 Ref.20
Mutagenesis2761L → S: Loss of UBC-binding and ubiquitination. Ref.17 Ref.20
Mutagenesis2801L → R: Loss of UBC-binding and ubiquitination. Ref.17
Mutagenesis2831S → N: Can bind RABEP1. Confers an affinity to RABEP1 identical to GGA1; when associated with M-258. Ref.19
Mutagenesis2841D → G: Loss of UBC-binding and ubiquitination. Ref.17
Mutagenesis2931Y → H: Loss of UBC-binding and ubiquitination. Ref.17
Mutagenesis391 – 3955DEELL → AAAAA: Increased binding to IGF2R. Ref.13
Sequence conflict4481Q → K in AAH70044. Ref.7
Sequence conflict5621F → S in BAH13665. Ref.4

Secondary structure

..................................................... 723
Helix Strand Turn

Details...

Sequences

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

Last modified October 1, 2000. Version 1.
Checksum: 4F80D6032239168C

FASTA72378,315
        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 

« Hide

Isoform Short [UniParc].

Checksum: E3A1C841AB3966C8
Show »

FASTA69074,470
Isoform 3 [UniParc].

Checksum: CACD3268CEE80BBE
Show »

FASTA59262,921
Isoform 4 [UniParc].

Checksum: 416484203E34542A
Show »

FASTA65170,148

References

« Hide '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. 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 3 AND 4).
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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton 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] (ISOFORM SHORT).
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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SYNRG.
[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] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF ASN-194; SER-199 AND THR-217, INTERACTION WITH ARF1 AND CLATHRIN, FUNCTION.
[10]"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.
[11]"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.
[12]"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.
[13]"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.
[14]"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.
[15]"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.
[16]"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.
[17]"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.
[18]"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.
[19]"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.
[20]"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.
[21]"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].
[22]"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.
[23]"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: 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.
AK302278 mRNA. Translation: BAH13665.1.
AC022211 Genomic DNA. No translation available.
CH471099 Genomic DNA. Translation: EAW89258.1.
BC070044 mRNA. Translation: AAH70044.1.
CCDSCCDS11716.1. [Q9NZ52-2]
CCDS11717.1. [Q9NZ52-1]
CCDS54164.1. [Q9NZ52-4]
CCDS58597.1. [Q9NZ52-3]
RefSeqNP_001166174.1. NM_001172703.2. [Q9NZ52-4]
NP_001166175.1. NM_001172704.2. [Q9NZ52-3]
NP_001278570.1. NM_001291641.1.
NP_001278571.1. NM_001291642.1.
NP_054720.1. NM_014001.4. [Q9NZ52-2]
NP_619525.1. NM_138619.3. [Q9NZ52-1]
UniGeneHs.87726.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JPLX-ray2.40A/B/C/D1-166[»]
1JUQX-ray2.20A/B/C/D1-166[»]
1LF8X-ray2.30A/B/C/D1-166[»]
1P4UX-ray2.20A571-723[»]
1WR6X-ray2.60A/B/C/D209-319[»]
1YD8X-ray2.80G/H208-301[»]
ProteinModelPortalQ9NZ52.
SMRQ9NZ52. Positions 1-157, 168-304, 579-723.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116775. 32 interactions.
DIPDIP-31600N.
IntActQ9NZ52. 13 interactions.
MINTMINT-126320.
STRING9606.ENSP00000245541.

PTM databases

PhosphoSiteQ9NZ52.

Polymorphism databases

DMDM14548064.

Proteomic databases

MaxQBQ9NZ52.
PaxDbQ9NZ52.
PRIDEQ9NZ52.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000245541; ENSP00000245541; ENSG00000125447. [Q9NZ52-1]
ENST00000351904; ENSP00000326575; ENSG00000125447. [Q9NZ52-2]
ENST00000578348; ENSP00000463288; ENSG00000125447. [Q9NZ52-3]
ENST00000582717; ENSP00000462081; ENSG00000125447. [Q9NZ52-4]
GeneID23163.
KEGGhsa:23163.
UCSCuc002jni.2. human. [Q9NZ52-1]
uc002jnj.2. human. [Q9NZ52-2]

Organism-specific databases

CTD23163.
GeneCardsGC17M073229.
HGNCHGNC:17079. GGA3.
HPAHPA022945.
MIM606006. gene.
neXtProtNX_Q9NZ52.
PharmGKBPA28659.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG321636.
HOGENOMHOG000231169.
HOVERGENHBG015945.
InParanoidQ9NZ52.
KOK12404.
OMAQGSPMKG.
PhylomeDBQ9NZ52.
TreeFamTF318574.

Gene expression databases

ArrayExpressQ9NZ52.
BgeeQ9NZ52.
CleanExHS_GGA3.
GenevestigatorQ9NZ52.

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.
IPR027422. GGA3.
IPR002014. VHS.
IPR018205. VHS_subgr.
[Graphical view]
PANTHERPTHR13856:SF34. PTHR13856:SF34. 1 hit.
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]
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Other

EvolutionaryTraceQ9NZ52.
GeneWikiGGA3.
GenomeRNAi23163.
NextBio35535625.
PROQ9NZ52.
SOURCESearch...

Entry information

Entry nameGGA3_HUMAN
AccessionPrimary (citable) accession number: Q9NZ52
Secondary accession number(s): B7Z7E2 expand/collapse secondary AC list , B7Z7M9, J3KRN0, Q15017, Q6IS16, Q9UJY3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: October 1, 2000
Last modified: July 9, 2014
This is version 152 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 17

Human chromosome 17: entries, gene names and cross-references to MIM