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O75843 (AP1G2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 125. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
AP-1 complex subunit gamma-like 2
Alternative name(s):
Gamma2-adaptin
Short name=G2ad
Gene names
Name:AP1G2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length785 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May function in protein sorting in late endosomes or multivesucular bodies (MVBs). Involved in MVB-assisted maturation of hepatitis B virus (HBV). Ref.1 Ref.5 Ref.6

Subunit structure

Probably interacts with AP1S1/Sigma1A-adaptin AP1S2/Sigma1B-adaptin. Probably does not interact with APB1. Interacts with HBV major surface antigen L. Interacts with HBV core protein C in a ubiquitin-dependent manner. Binds ubiquitin. Ref.1 Ref.4 Ref.5

Subcellular location

Golgi apparatus membrane; Peripheral membrane protein. Cytoplasmic vesicle membrane; Peripheral membrane protein. Endosome membrane; Peripheral membrane protein. Note: Mainly localized to perinuclear vesicular structures. Colocalizes with HBV major surface antigen L and HBV core protein C in CD63-containing compartments. Colocalizes with HBV major surface antigen L to cis-Golgi-like structures. Ref.1 Ref.2 Ref.4 Ref.5

Tissue specificity

Expressed in all but one (skeletal muscle) tissues examined.

Sequence similarities

Belongs to the adaptor complexes large subunit family.

Contains 1 GAE domain.

Caution

Does not appear to be a subunit of the clathrin-associated adaptor protein complex 1 (AP-1).

Sequence caution

The sequence AAC67390.1 differs from that shown. Reason: Frameshift at position 713.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RABEP1Q152762EBI-373637,EBI-447043

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 785785AP-1 complex subunit gamma-like 2
PRO_0000193760

Regions

Domain665 – 780116GAE
Region369 – 37911Essential for ubiquitin-binding

Natural variations

Natural variant3771S → F.
Corresponds to variant rs12897422 [ dbSNP | Ensembl ].
VAR_024363

Experimental info

Mutagenesis3691L → G: Greatly diminishes interaction with ubiquitin; when associated with G-372. Ref.5
Mutagenesis3721A → G: Greatly diminishes interaction with ubiquitin; when associated with G-369. Ref.5
Mutagenesis3721A → G: Greatly diminishes interaction with ubiquitin; when associated with G-376.
Mutagenesis3761S → G: Greatly diminishes interaction with ubiquitin; when associated with G-372. Ref.5
Sequence conflict204 – 2063ERS → GRN in AAC67390. Ref.2
Sequence conflict3991A → C in AAC67390. Ref.2
Sequence conflict4021A → D in AAC67390. Ref.2
Sequence conflict4161K → T in AAC67390. Ref.2
Sequence conflict4291T → S in AAC67390. Ref.2
Sequence conflict439 – 4413VAN → AGHT in AAC67390. Ref.2

Secondary structure

......................... 785
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O75843 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: C189192C9811111C

FASTA78587,117
        10         20         30         40         50         60 
MVVPSLKLQD LIEEIRGAKT QAQEREVIQK ECAHIRASFR DGDPVHRHRQ LAKLLYVHML 

        70         80         90        100        110        120 
GYPAHFGQME CLKLIASSRF TDKRVGYLGA MLLLDERHDA HLLITNSIKN DLSQGIQPVQ 

       130        140        150        160        170        180 
GLALCTLSTM GSAEMCRDLA PEVEKLLLQP SPYVRKKAIL TAVHMIRKVP ELSSVFLPPC 

       190        200        210        220        230        240 
AQLLHERHHG ILLGTITLIT ELCERSPAAL RHFRKVVPQL VHILRTLVTM GYSTEHSISG 

       250        260        270        280        290        300 
VSDPFLQVQI LRLLRILGRN HEESSETMND LLAQVATNTD TSRNAGNAVL FETVLTIMDI 

       310        320        330        340        350        360 
RSAAGLRVLA VNILGRFLLN SDRNIRYVAL TSLLRLVQSD HSAVQRHRPT VVECLRETDA 

       370        380        390        400        410        420 
SLSRRALELS LALVNSSNVR AMMQELQAFL ESCPPDLRAD CASGILLAAE RFAPTKRWHI 

       430        440        450        460        470        480 
DTILHVLTTA GTHVRDDAVA NLTQLIGGAQ ELHAYSVRRL YNALAEDISQ QPLVQVAAWC 

       490        500        510        520        530        540 
IGEYGDLLLA GNCEEIEPLQ VDEEEVLALL EKVLQSHMSL PATRGYALTA LMKLSTRLCG 

       550        560        570        580        590        600 
DNNRIRQVVS IYGSCLDVEL QQRAVEYDTL FRKYDHMRAA ILEKMPLVER DGPQADEEAK 

       610        620        630        640        650        660 
ESKEAAQLSE AAPVPTEPQA SQLLDLLDLL DGASGDVQHP PHLDPSPGGA LVHLLDLPCV 

       670        680        690        700        710        720 
PPPPAPIPDL KVFEREGVQL NLSFIRPPEN PALLLITITA TNFSEGDVTH FICQAAVPKS 

       730        740        750        760        770        780 
LQLQLQAPSG NTVPARGGLP ITQLFRILNP NKAPLRLKLR LTYDHFHQSV QEIFEVNNLP 


VESWQ 

« Hide

References

« Hide 'large scale' references
[1]"Identification and characterization of novel clathrin adaptor-related proteins."
Takatsu H., Sakurai M., Shin H.-W., Murakami K., Nakayama K.
J. Biol. Chem. 273:24693-24700(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, NEGATIVE INTERACTION WITH APB1, INTERACTION WITH AP1S1 AND AP1S2.
Tissue: Liver.
[2]"Cloning, expression, and localization of a novel gamma-adaptin-like molecule."
Lewin D.A., Sheff D., Ooi C.E., Whitney J.A., Yamamoto E., Chicione L.M., Webster P., Bonifacino J.S., Mellman I.
FEBS Lett. 435:263-268(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
[3]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. 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"Hepatitis B virus large envelope protein interacts with gamma2-adaptin, a clathrin adaptor-related protein."
Hartmann-Stuehler C., Prange R.
J. Virol. 75:5343-5351(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HBV MAJOR SURFACE ANTIGEN L, SUBCELLULAR LOCATION.
[5]"Gamma-adaptin, a novel ubiquitin-interacting adaptor, and Nedd4 ubiquitin ligase control hepatitis B virus maturation."
Rost M., Mann S., Lambert C., Doring T., Thome N., Prange R.
J. Biol. Chem. 281:29297-29308(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN HEPATITIS VIRUS B MATURATION, SUBCELLULAR LOCATION, INTERACTION WITH HBV CORE PROTEIN AND UBIQUITIN, MUTAGENESIS OF LEU-369; ALA-372 AND SER-376.
[6]"Hepatitis B virus maturation is sensitive to functional inhibition of ESCRT-III, Vps4, and gamma 2-adaptin."
Lambert C., Doering T., Prange R.
J. Virol. 81:9050-9060(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN HEPATITIS VIRUS B MATURATION.
[7]"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].
[8]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"Solution structure of the alpha adaptin C2 domain from human adapter-related protein complex 1 gamma 2 subunit."
RIKEN structural genomics initiative (RSGI)
Submitted (JUL-2007) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 662-785.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB015318 mRNA. Translation: BAA33390.1.
AF068706 mRNA. Translation: AAC67390.1. Frameshift.
CH471078 Genomic DNA. Translation: EAW66132.1.
CH471078 Genomic DNA. Translation: EAW66134.1.
CH471078 Genomic DNA. Translation: EAW66138.1.
CCDSCCDS9602.1.
RefSeqNP_003908.1. NM_003917.4.
XP_005268229.1. XM_005268172.1.
XP_005268230.1. XM_005268173.1.
UniGeneHs.343244.
Hs.569375.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2E9GNMR-A662-785[»]
2YMTX-ray1.80A665-785[»]
3ZHFX-ray1.70A665-785[»]
4BCXX-ray2.00A665-785[»]
ProteinModelPortalO75843.
SMRO75843. Positions 8-586, 665-785.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114420. 12 interactions.
IntActO75843. 11 interactions.
MINTMINT-5005892.
STRING9606.ENSP00000312442.

PTM databases

PhosphoSiteO75843.

Proteomic databases

MaxQBO75843.
PaxDbO75843.
PeptideAtlasO75843.
PRIDEO75843.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000308724; ENSP00000312442; ENSG00000213983.
ENST00000397120; ENSP00000380309; ENSG00000213983.
GeneID8906.
KEGGhsa:8906.
UCSCuc001wkl.2. human.

Organism-specific databases

CTD8906.
GeneCardsGC14M024028.
HGNCHGNC:556. AP1G2.
HPAHPA004106.
MIM603534. gene.
neXtProtNX_O75843.
PharmGKBPA24846.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG303101.
HOGENOMHOG000210271.
HOVERGENHBG067473.
InParanoidO75843.
KOK12391.
OMAPCAQLLH.
OrthoDBEOG7S7SD7.
PhylomeDBO75843.
TreeFamTF300367.

Gene expression databases

ArrayExpressO75843.
BgeeO75843.
CleanExHS_AP1G2.
GenevestigatorO75843.

Family and domain databases

Gene3D1.25.10.10. 1 hit.
2.60.40.1230. 1 hit.
InterProIPR017107. 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]
PfamPF01602. Adaptin_N. 1 hit.
PF02883. Alpha_adaptinC2. 1 hit.
[Graphical view]
PIRSFPIRSF037094. AP1_complex_gamma. 1 hit.
SMARTSM00809. Alpha_adaptinC2. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 1 hit.
SSF49348. SSF49348. 1 hit.
PROSITEPS50180. GAE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSAP1G2. human.
EvolutionaryTraceO75843.
GeneWikiAP1G2.
GenomeRNAi8906.
NextBio33461.
PROO75843.
SOURCESearch...

Entry information

Entry nameAP1G2_HUMAN
AccessionPrimary (citable) accession number: O75843
Secondary accession number(s): D3DS51, O75504
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: November 1, 1998
Last modified: July 9, 2014
This is version 125 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 14

Human chromosome 14: entries, gene names and cross-references to MIM