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Protein

AP-1 complex subunit gamma-1

Gene

Ap1g1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Enzyme and pathway databases

ReactomeiR-MMU-2132295. MHC class II antigen presentation.
R-MMU-432720. Lysosome Vesicle Biogenesis.
R-MMU-432722. Golgi Associated Vesicle Biogenesis.

Names & Taxonomyi

Protein namesi
Recommended name:
AP-1 complex subunit gamma-1
Alternative name(s):
Adaptor protein complex AP-1 subunit gamma-1
Adaptor-related protein complex 1 subunit gamma-1
Clathrin assembly protein complex 1 gamma-1 large chain
Gamma-adaptin
Gamma1-adaptin
Golgi adaptor HA1/AP1 adaptin subunit gamma-1
Gene namesi
Name:Ap1g1
Synonyms:Adtg, Clapg1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:101919. Ap1g1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi753 – 7531A → D: Strongly reduces interaction with EPS15 and SYNRG. 1 Publication
Mutagenesisi762 – 7621L → E: Strongly reduces interaction with EPS15 and SYNRG. 1 Publication
Mutagenesisi765 – 7651P → N: Reduces interaction with EPS15 and SYNRG. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 822821AP-1 complex subunit gamma-1PRO_0000193759Add
BLAST

Proteomic databases

EPDiP22892.
MaxQBiP22892.
PaxDbiP22892.
PRIDEiP22892.

PTM databases

iPTMnetiP22892.
PhosphoSiteiP22892.
SwissPalmiP22892.

Expressioni

Tissue specificityi

Widely expressed.

Gene expression databases

BgeeiP22892.
CleanExiMM_AP1G1.
ExpressionAtlasiP22892. baseline and differential.
GenevisibleiP22892. MM.

Interactioni

Subunit structurei

Adaptor protein complex 1 (AP-1) is a heterotetramer composed of two large adaptins (gamma-type subunit AP1G1 and beta-type subunit AP1B1), a medium adaptin (mu-type subunit AP1M1 or AP1M2) and a small adaptin (sigma-type subunit AP1S1 or AP1S2 or AP1S3) (By similarity). Binds RABEP1 (By similarity). Binds EPS15 and SYNRG. Interacts (via GAE domain) with AP1AR (via coiled-coil domain) (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Ap1m1P355856EBI-1040262,EBI-1040251
CLINT1Q1467710EBI-1040262,EBI-1171113From a different organism.

GO - Molecular functioni

Protein-protein interaction databases

BioGridi198123. 2 interactions.
IntActiP22892. 18 interactions.
MINTiMINT-200421.
STRINGi10090.ENSMUSP00000090844.

Structurei

Secondary structure

1
822
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 159Combined sources
Helixi20 – 3920Combined sources
Beta strandi43 – 453Combined sources
Helixi46 – 5813Combined sources
Helixi64 – 663Combined sources
Helixi67 – 748Combined sources
Beta strandi76 – 783Combined sources
Helixi79 – 9214Combined sources
Helixi100 – 11112Combined sources
Helixi116 – 12914Combined sources
Helixi132 – 14615Combined sources
Helixi151 – 16717Combined sources
Helixi170 – 1756Combined sources
Helixi176 – 1794Combined sources
Helixi188 – 20417Combined sources
Helixi206 – 2127Combined sources
Helixi216 – 22813Combined sources
Turni233 – 2353Combined sources
Helixi243 – 25513Combined sources
Turni256 – 2594Combined sources
Helixi262 – 27716Combined sources
Helixi283 – 29816Combined sources
Helixi303 – 31715Combined sources
Helixi322 – 33413Combined sources
Beta strandi336 – 3394Combined sources
Helixi340 – 3434Combined sources
Helixi347 – 3526Combined sources
Helixi353 – 3553Combined sources
Helixi359 – 37012Combined sources
Turni375 – 3773Combined sources
Helixi378 – 39013Combined sources
Helixi394 – 41017Combined sources
Helixi415 – 42814Combined sources
Helixi430 – 4323Combined sources
Helixi435 – 4373Combined sources
Helixi438 – 4469Combined sources
Turni449 – 4524Combined sources
Helixi453 – 46513Combined sources
Helixi470 – 48213Combined sources
Helixi484 – 4885Combined sources
Helixi503 – 51412Combined sources
Helixi520 – 53617Combined sources
Helixi541 – 55010Combined sources
Helixi551 – 5533Combined sources
Helixi557 – 57216Combined sources
Helixi576 – 5805Combined sources
Beta strandi707 – 7126Combined sources
Beta strandi715 – 7228Combined sources
Beta strandi730 – 73910Combined sources
Beta strandi741 – 7433Combined sources
Beta strandi745 – 7539Combined sources
Beta strandi758 – 7625Combined sources
Helixi772 – 7743Combined sources
Beta strandi778 – 7858Combined sources
Beta strandi794 – 8029Combined sources
Beta strandi805 – 8139Combined sources
Helixi818 – 8203Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GYUX-ray1.81A704-822[»]
1GYVX-ray1.71A704-822[»]
1GYWX-ray2.40A/B695-822[»]
1W63X-ray4.00A/C/E/G/I/K1-613[»]
2A7BX-ray1.65A704-822[»]
3ZY7X-ray1.09A/B704-822[»]
4HMYX-ray7.00A1-595[»]
4P6ZX-ray3.00G1-613[»]
ProteinModelPortaliP22892.
SMRiP22892. Positions 1-589, 704-822.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22892.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini702 – 817116GAEPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 GAE domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1062. Eukaryota.
ENOG410XPKK. LUCA.
GeneTreeiENSGT00390000012618.
HOGENOMiHOG000210271.
HOVERGENiHBG067473.
InParanoidiP22892.
KOiK12391.
PhylomeDBiP22892.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
2.60.40.1230. 2 hits.
InterProiIPR017107. AP1_complex_gsu.
IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR002553. Clathrin/coatomer_adapt-like_N.
IPR008152. Clathrin_a/b/g-adaptin_app_Ig.
IPR008153. Clathrin_g-adaptin_app.
IPR013041. Coatomer/clathrin_app_Ig-like.
[Graphical view]
PfamiPF01602. Adaptin_N. 1 hit.
PF02883. Alpha_adaptinC2. 1 hit.
[Graphical view]
PIRSFiPIRSF037094. AP1_complex_gamma. 1 hit.
SMARTiSM00809. Alpha_adaptinC2. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
SSF49348. SSF49348. 1 hit.
PROSITEiPS50180. GAE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P22892-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPAPIRLREL IRTIRTARTQ AEEREMIQKE CAAIRSSFRE EDNTYRCRNV
60 70 80 90 100
AKLLYMHMLG YPAHFGQLEC LKLIASQKFT DKRIGYLGAM LLLDERQDVH
110 120 130 140 150
LLMTNCIKND LNHSTQFVQG LALCTLGCMG SSEMCRDLAG EVEKLLKTSN
160 170 180 190 200
SYLRKKAALC AVHVIRKVPE LMEMFLPATK NLLNEKNHGV LHTSVVLLTE
210 220 230 240 250
MCERSPDMLA HFRKLVPQLV RILKNLIMSG YSPEHDVSGI SDPFLQVRIL
260 270 280 290 300
RLLRILGRND DDSSEAMNDI LAQVATNTET SKNVGNAILY ETVLTIMDIK
310 320 330 340 350
SESGLRVLAI NILGRFLLNN DKNIRYVALT SLLKTVQTDH NAVQRHRSTI
360 370 380 390 400
VDCLKDLDVS IKRRAMELSF ALVNGNNIRG MMKELLYFLD SCEPEFKADC
410 420 430 440 450
ASGIFLAAEK YAPSKRWHID TIMRVLTTAG SYVRDDAVPN LIQLITNSVE
460 470 480 490 500
MHAYTVQRLY KAILGDYSQQ PLVQVAAWCI GEYGDLLVSG QCEEEEPIQV
510 520 530 540 550
TEDEVLDILE SVLISNMSTS VTRGYALTAI MKLSTRFTCT VNRIKKVVSI
560 570 580 590 600
YGSSIDVELQ QRAVEYNALF KKYDHMRSAL LERMPVMEKV TTNGPSEIVQ
610 620 630 640 650
TNGETEPAPL ETKPPPSGPQ PTSQANDLLD LLGGNDITPV IPTAPTSKPA
660 670 680 690 700
SAGGELLDLL GDITLTGAPA AAPTPASVPQ ISQPPFLLDG LSSQPLFNDI
710 720 730 740 750
APGIPSITAY SKNGLKIEFT FERSNTNPSV TVITIQASNS TELDMTDFVF
760 770 780 790 800
QAAVPKTFQL QLLSPSSSVV PAFNTGTITQ VIKVLNPQKQ QLRMRIKLTY
810 820
NHKGSAMQDL AEVNNFPPQS WQ
Length:822
Mass (Da):91,350
Last modified:January 23, 2007 - v3
Checksum:i15317E4BCD9503EB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X54424 mRNA. Translation: CAA38296.1.
CCDSiCCDS80929.1.
PIRiA36680.
RefSeqiNP_001288140.1. NM_001301211.1.
UniGeneiMm.37210.
Mm.486894.

Genome annotation databases

EnsembliENSMUST00000034171; ENSMUSP00000034171; ENSMUSG00000031731.
GeneIDi11765.
KEGGimmu:11765.
UCSCiuc012gkl.3. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X54424 mRNA. Translation: CAA38296.1.
CCDSiCCDS80929.1.
PIRiA36680.
RefSeqiNP_001288140.1. NM_001301211.1.
UniGeneiMm.37210.
Mm.486894.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GYUX-ray1.81A704-822[»]
1GYVX-ray1.71A704-822[»]
1GYWX-ray2.40A/B695-822[»]
1W63X-ray4.00A/C/E/G/I/K1-613[»]
2A7BX-ray1.65A704-822[»]
3ZY7X-ray1.09A/B704-822[»]
4HMYX-ray7.00A1-595[»]
4P6ZX-ray3.00G1-613[»]
ProteinModelPortaliP22892.
SMRiP22892. Positions 1-589, 704-822.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198123. 2 interactions.
IntActiP22892. 18 interactions.
MINTiMINT-200421.
STRINGi10090.ENSMUSP00000090844.

PTM databases

iPTMnetiP22892.
PhosphoSiteiP22892.
SwissPalmiP22892.

Proteomic databases

EPDiP22892.
MaxQBiP22892.
PaxDbiP22892.
PRIDEiP22892.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000034171; ENSMUSP00000034171; ENSMUSG00000031731.
GeneIDi11765.
KEGGimmu:11765.
UCSCiuc012gkl.3. mouse.

Organism-specific databases

CTDi164.
MGIiMGI:101919. Ap1g1.

Phylogenomic databases

eggNOGiKOG1062. Eukaryota.
ENOG410XPKK. LUCA.
GeneTreeiENSGT00390000012618.
HOGENOMiHOG000210271.
HOVERGENiHBG067473.
InParanoidiP22892.
KOiK12391.
PhylomeDBiP22892.

Enzyme and pathway databases

ReactomeiR-MMU-2132295. MHC class II antigen presentation.
R-MMU-432720. Lysosome Vesicle Biogenesis.
R-MMU-432722. Golgi Associated Vesicle Biogenesis.

Miscellaneous databases

EvolutionaryTraceiP22892.
PROiP22892.
SOURCEiSearch...

Gene expression databases

BgeeiP22892.
CleanExiMM_AP1G1.
ExpressionAtlasiP22892. baseline and differential.
GenevisibleiP22892. MM.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
2.60.40.1230. 2 hits.
InterProiIPR017107. AP1_complex_gsu.
IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR002553. Clathrin/coatomer_adapt-like_N.
IPR008152. Clathrin_a/b/g-adaptin_app_Ig.
IPR008153. Clathrin_g-adaptin_app.
IPR013041. Coatomer/clathrin_app_Ig-like.
[Graphical view]
PfamiPF01602. Adaptin_N. 1 hit.
PF02883. Alpha_adaptinC2. 1 hit.
[Graphical view]
PIRSFiPIRSF037094. AP1_complex_gamma. 1 hit.
SMARTiSM00809. Alpha_adaptinC2. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
SSF49348. SSF49348. 1 hit.
PROSITEiPS50180. GAE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and expression of gamma-adaptin, a component of clathrin-coated vesicles associated with the Golgi apparatus."
    Robinson M.S.
    J. Cell Biol. 111:2319-2326(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-25.
    Tissue: Brain.
  2. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  3. "Gamma-adaptin appendage domain: structure and binding site for Eps15 and gamma-synergin."
    Kent H.M., McMahon H.T., Evans P.R., Benmerah A., Owen D.J.
    Structure 10:1139-1148(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF 704-822, MUTAGENESIS OF ALA-753; LEU-762 AND PRO-765, INTERACTION WITH EPS15 AND SYNRG.
  4. Cited for: X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) OF 1-613, SUBUNIT.

Entry informationi

Entry nameiAP1G1_MOUSE
AccessioniPrimary (citable) accession number: P22892
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 147 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.