ID AP1G2_HUMAN Reviewed; 785 AA. AC O75843; D3DS51; O75504; DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 24-JAN-2024, entry version 190. DE RecName: Full=AP-1 complex subunit gamma-like 2; DE AltName: Full=Gamma2-adaptin; DE Short=G2ad; GN Name=AP1G2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, NEGATIVE RP INTERACTION WITH APB1, AND INTERACTION WITH AP1S1 AND AP1S2. RC TISSUE=Liver; RX PubMed=9733768; DOI=10.1074/jbc.273.38.24693; RA Takatsu H., Sakurai M., Shin H.-W., Murakami K., Nakayama K.; RT "Identification and characterization of novel clathrin adaptor-related RT proteins."; RL J. Biol. Chem. 273:24693-24700(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION. RX PubMed=9762922; DOI=10.1016/s0014-5793(98)01083-7; RA Lewin D.A., Sheff D., Ooi C.E., Whitney J.A., Yamamoto E., Chicione L.M., RA Webster P., Bonifacino J.S., Mellman I.; RT "Cloning, expression, and localization of a novel gamma-adaptin-like RT molecule."; RL FEBS Lett. 435:263-268(1998). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP INTERACTION WITH HBV MAJOR SURFACE ANTIGEN L (MICROBIAL INFECTION), AND RP SUBCELLULAR LOCATION. RX PubMed=11333915; DOI=10.1128/jvi.75.11.5343-5351.2001; RA Hartmann-Stuehler C., Prange R.; RT "Hepatitis B virus large envelope protein interacts with gamma2-adaptin, a RT clathrin adaptor-related protein."; RL J. Virol. 75:5343-5351(2001). RN [5] RP INTERACTION WITH RABEP1; CLINT1; NECAP1 AND AFTPH. RX PubMed=14665628; DOI=10.1074/jbc.m311873200; RA Mattera R., Ritter B., Sidhu S.S., McPherson P.S., Bonifacino J.S.; RT "Definition of the consensus motif recognized by gamma-adaptin ear RT domains."; RL J. Biol. Chem. 279:8018-8028(2004). RN [6] RP FUNCTION (MICROBIAL INFECTION), SUBCELLULAR LOCATION, INTERACTION WITH HBV RP CORE PROTEIN (MICROBIAL INFECTION) AND UBIQUITIN, AND MUTAGENESIS OF RP LEU-369; ALA-372 AND SER-376. RX PubMed=16867982; DOI=10.1074/jbc.m603517200; RA Rost M., Mann S., Lambert C., Doring T., Thome N., Prange R.; RT "Gamma-adaptin, a novel ubiquitin-interacting adaptor, and Nedd4 ubiquitin RT ligase control hepatitis B virus maturation."; RL J. Biol. Chem. 281:29297-29308(2006). RN [7] RP FUNCTION (MICROBIAL INFECTION). RX PubMed=17553870; DOI=10.1128/jvi.00479-07; RA Lambert C., Doering T., Prange R.; RT "Hepatitis B virus maturation is sensitive to functional inhibition of RT ESCRT-III, Vps4, and gamma 2-adaptin."; RL J. Virol. 81:9050-9060(2007). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [10] RP STRUCTURE BY NMR OF 662-785. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the alpha adaptin C2 domain from human adapter- RT related protein complex 1 gamma 2 subunit."; RL Submitted (JUL-2007) to the PDB data bank. CC -!- FUNCTION: May function in protein sorting in late endosomes or CC multivesucular bodies (MVBs). {ECO:0000269|PubMed:9733768}. CC -!- FUNCTION: (Microbial infection) Involved in MVB-assisted maturation of CC hepatitis B virus (HBV). {ECO:0000269|PubMed:16867982, CC ECO:0000269|PubMed:17553870}. CC -!- SUBUNIT: May interact with AP1S1/Sigma1A-adaptin and AP1S2/Sigma1B- CC adaptin (PubMed:9733768). Probably does not interact with APB1 CC (PubMed:9733768). Interacts (via GAE domain) with RABEP1, NECAP1, CC CLINT1 and AFTPH/aftiphilin (PubMed:14665628). CC {ECO:0000269|PubMed:14665628, ECO:0000269|PubMed:9733768}. CC -!- SUBUNIT: (Microbial infection) Interacts with HBV major surface antigen CC L. Interacts with HBV core protein C in a ubiquitin-dependent manner. CC {ECO:0000269|PubMed:11333915, ECO:0000269|PubMed:16867982}. CC -!- INTERACTION: CC O75843; Q15276: RABEP1; NbExp=2; IntAct=EBI-373637, EBI-447043; CC O75843; P03139-1: S; Xeno; NbExp=6; IntAct=EBI-373637, EBI-16065097; CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane CC {ECO:0000269|PubMed:11333915, ECO:0000269|PubMed:9762922}; Peripheral CC membrane protein; Cytoplasmic side {ECO:0000269|PubMed:11333915}. CC Cytoplasmic vesicle membrane {ECO:0000269|PubMed:9733768}; Peripheral CC membrane protein. Endosome membrane {ECO:0000269|PubMed:16867982}; CC Peripheral membrane protein. Note=Mainly localized to perinuclear CC vesicular structures (PubMed:9733768). Colocalizes with HBV major CC surface antigen L and HBV core protein C in CD63-containing CC compartments (PubMed:16867982). Colocalizes with HBV major surface CC antigen L to cis-Golgi-like structures (PubMed:11333915). CC -!- TISSUE SPECIFICITY: Expressed in all but one (skeletal muscle) tissues CC examined. CC -!- SIMILARITY: Belongs to the adaptor complexes large subunit family. CC {ECO:0000305}. CC -!- CAUTION: Does not appear to be a subunit of the clathrin-associated CC adaptor protein complex 1 (AP-1). {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC67390.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB015318; BAA33390.1; -; mRNA. DR EMBL; AF068706; AAC67390.1; ALT_FRAME; mRNA. DR EMBL; CH471078; EAW66132.1; -; Genomic_DNA. DR EMBL; CH471078; EAW66134.1; -; Genomic_DNA. DR EMBL; CH471078; EAW66138.1; -; Genomic_DNA. DR CCDS; CCDS9602.1; -. DR RefSeq; NP_003908.1; NM_003917.4. DR RefSeq; XP_005268229.1; XM_005268172.3. DR RefSeq; XP_005268230.1; XM_005268173.3. DR PDB; 2E9G; NMR; -; A=662-785. DR PDB; 2YMT; X-ray; 1.80 A; A=665-785. DR PDB; 3ZHF; X-ray; 1.70 A; A=665-785. DR PDB; 4BCX; X-ray; 2.00 A; A=665-785. DR PDBsum; 2E9G; -. DR PDBsum; 2YMT; -. DR PDBsum; 3ZHF; -. DR PDBsum; 4BCX; -. DR AlphaFoldDB; O75843; -. DR BMRB; O75843; -. DR SMR; O75843; -. DR BioGRID; 114420; 82. DR CORUM; O75843; -. DR DIP; DIP-31185N; -. DR IntAct; O75843; 28. DR MINT; O75843; -. DR STRING; 9606.ENSP00000312442; -. DR GlyGen; O75843; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; O75843; -. DR PhosphoSitePlus; O75843; -. DR BioMuta; AP1G2; -. DR EPD; O75843; -. DR jPOST; O75843; -. DR MassIVE; O75843; -. DR MaxQB; O75843; -. DR PaxDb; 9606-ENSP00000312442; -. DR PeptideAtlas; O75843; -. DR ProteomicsDB; 50225; -. DR Pumba; O75843; -. DR Antibodypedia; 110; 75 antibodies from 17 providers. DR DNASU; 8906; -. DR Ensembl; ENST00000308724.9; ENSP00000312442.5; ENSG00000213983.12. DR Ensembl; ENST00000397120.8; ENSP00000380309.3; ENSG00000213983.12. DR GeneID; 8906; -. DR KEGG; hsa:8906; -. DR MANE-Select; ENST00000397120.8; ENSP00000380309.3; NM_003917.5; NP_003908.1. DR UCSC; uc001wkl.4; human. DR AGR; HGNC:556; -. DR CTD; 8906; -. DR DisGeNET; 8906; -. DR GeneCards; AP1G2; -. DR HGNC; HGNC:556; AP1G2. DR HPA; ENSG00000213983; Low tissue specificity. DR MIM; 603534; gene. DR neXtProt; NX_O75843; -. DR OpenTargets; ENSG00000213983; -. DR PharmGKB; PA24846; -. DR VEuPathDB; HostDB:ENSG00000213983; -. DR eggNOG; KOG1062; Eukaryota. DR GeneTree; ENSGT00950000182838; -. DR HOGENOM; CLU_003824_0_0_1; -. DR InParanoid; O75843; -. DR OMA; REPNTKK; -. DR OrthoDB; 25313at2759; -. DR PhylomeDB; O75843; -. DR TreeFam; TF300367; -. DR PathwayCommons; O75843; -. DR Reactome; R-HSA-432720; Lysosome Vesicle Biogenesis. DR SignaLink; O75843; -. DR SIGNOR; O75843; -. DR BioGRID-ORCS; 8906; 43 hits in 1157 CRISPR screens. DR ChiTaRS; AP1G2; human. DR EvolutionaryTrace; O75843; -. DR GeneWiki; AP1G2; -. DR GenomeRNAi; 8906; -. DR Pharos; O75843; Tbio. DR PRO; PR:O75843; -. DR Proteomes; UP000005640; Chromosome 14. DR RNAct; O75843; Protein. DR Bgee; ENSG00000213983; Expressed in right hemisphere of cerebellum and 179 other cell types or tissues. DR ExpressionAtlas; O75843; baseline and differential. DR GO; GO:0030121; C:AP-1 adaptor complex; IBA:GO_Central. DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005794; C:Golgi apparatus; TAS:ProtInc. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0005798; C:Golgi-associated vesicle; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; IDA:UniProtKB. DR GO; GO:0030133; C:transport vesicle; IDA:UniProtKB. DR GO; GO:0035615; F:clathrin adaptor activity; IBA:GO_Central. DR GO; GO:0006896; P:Golgi to vacuole transport; IBA:GO_Central. DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro. DR GO; GO:0016192; P:vesicle-mediated transport; NAS:UniProtKB. DR Gene3D; 2.60.40.1230; -; 1. DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1. DR InterPro; IPR017107; AP1_complex_gsu. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR002553; Clathrin/coatomer_adapt-like_N. DR InterPro; IPR008152; Clathrin_a/b/g-adaptin_app_Ig. DR InterPro; IPR013041; Clathrin_app_Ig-like_sf. DR InterPro; IPR008153; GAE_dom. DR PANTHER; PTHR22780; ADAPTIN, ALPHA/GAMMA/EPSILON; 1. DR PANTHER; PTHR22780:SF28; AP-1 COMPLEX SUBUNIT GAMMA-LIKE 2; 1. DR Pfam; PF01602; Adaptin_N; 1. DR Pfam; PF02883; Alpha_adaptinC2; 1. DR PIRSF; PIRSF037094; AP1_complex_gamma; 1. DR SMART; SM00809; Alpha_adaptinC2; 1. DR SUPFAM; SSF48371; ARM repeat; 1. DR SUPFAM; SSF49348; Clathrin adaptor appendage domain; 1. DR PROSITE; PS50180; GAE; 1. DR Genevisible; O75843; HS. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasmic vesicle; Endosome; Golgi apparatus; KW Host-virus interaction; Membrane; Protein transport; Reference proteome; KW Transport. FT CHAIN 1..785 FT /note="AP-1 complex subunit gamma-like 2" FT /id="PRO_0000193760" FT DOMAIN 665..780 FT /note="GAE" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00093" FT REGION 369..379 FT /note="Essential for ubiquitin-binding" FT REGION 592..617 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VARIANT 377 FT /note="S -> F (in dbSNP:rs12897422)" FT /id="VAR_024363" FT MUTAGEN 369 FT /note="L->G: Greatly diminishes interaction with ubiquitin; FT when associated with G-372." FT /evidence="ECO:0000269|PubMed:16867982" FT MUTAGEN 372 FT /note="A->G: Greatly diminishes interaction with ubiquitin; FT when associated with G-369." FT /evidence="ECO:0000269|PubMed:16867982" FT MUTAGEN 372 FT /note="A->G: Greatly diminishes interaction with ubiquitin; FT when associated with G-376." FT /evidence="ECO:0000269|PubMed:16867982" FT MUTAGEN 376 FT /note="S->G: Greatly diminishes interaction with ubiquitin; FT when associated with G-372." FT /evidence="ECO:0000269|PubMed:16867982" FT CONFLICT 204..206 FT /note="ERS -> GRN (in Ref. 2; AAC67390)" FT /evidence="ECO:0000305" FT CONFLICT 399 FT /note="A -> C (in Ref. 2; AAC67390)" FT /evidence="ECO:0000305" FT CONFLICT 402 FT /note="A -> D (in Ref. 2; AAC67390)" FT /evidence="ECO:0000305" FT CONFLICT 416 FT /note="K -> T (in Ref. 2; AAC67390)" FT /evidence="ECO:0000305" FT CONFLICT 429 FT /note="T -> S (in Ref. 2; AAC67390)" FT /evidence="ECO:0000305" FT CONFLICT 439..441 FT /note="VAN -> AGHT (in Ref. 2; AAC67390)" FT /evidence="ECO:0000305" FT STRAND 670..675 FT /evidence="ECO:0007829|PDB:3ZHF" FT STRAND 678..685 FT /evidence="ECO:0007829|PDB:3ZHF" FT STRAND 693..702 FT /evidence="ECO:0007829|PDB:3ZHF" FT STRAND 704..706 FT /evidence="ECO:0007829|PDB:3ZHF" FT STRAND 708..716 FT /evidence="ECO:0007829|PDB:3ZHF" FT STRAND 721..725 FT /evidence="ECO:0007829|PDB:3ZHF" FT STRAND 731..733 FT /evidence="ECO:0007829|PDB:2E9G" FT TURN 735..737 FT /evidence="ECO:0007829|PDB:3ZHF" FT STRAND 741..748 FT /evidence="ECO:0007829|PDB:3ZHF" FT STRAND 758..765 FT /evidence="ECO:0007829|PDB:3ZHF" FT STRAND 768..775 FT /evidence="ECO:0007829|PDB:3ZHF" FT HELIX 781..783 FT /evidence="ECO:0007829|PDB:3ZHF" SQ SEQUENCE 785 AA; 87117 MW; C189192C9811111C CRC64; MVVPSLKLQD LIEEIRGAKT QAQEREVIQK ECAHIRASFR DGDPVHRHRQ LAKLLYVHML GYPAHFGQME CLKLIASSRF TDKRVGYLGA MLLLDERHDA HLLITNSIKN DLSQGIQPVQ GLALCTLSTM GSAEMCRDLA PEVEKLLLQP SPYVRKKAIL TAVHMIRKVP ELSSVFLPPC AQLLHERHHG ILLGTITLIT ELCERSPAAL RHFRKVVPQL VHILRTLVTM GYSTEHSISG VSDPFLQVQI LRLLRILGRN HEESSETMND LLAQVATNTD TSRNAGNAVL FETVLTIMDI RSAAGLRVLA VNILGRFLLN SDRNIRYVAL TSLLRLVQSD HSAVQRHRPT VVECLRETDA SLSRRALELS LALVNSSNVR AMMQELQAFL ESCPPDLRAD CASGILLAAE RFAPTKRWHI DTILHVLTTA GTHVRDDAVA NLTQLIGGAQ ELHAYSVRRL YNALAEDISQ QPLVQVAAWC IGEYGDLLLA GNCEEIEPLQ VDEEEVLALL EKVLQSHMSL PATRGYALTA LMKLSTRLCG DNNRIRQVVS IYGSCLDVEL QQRAVEYDTL FRKYDHMRAA ILEKMPLVER DGPQADEEAK ESKEAAQLSE AAPVPTEPQA SQLLDLLDLL DGASGDVQHP PHLDPSPGGA LVHLLDLPCV PPPPAPIPDL KVFEREGVQL NLSFIRPPEN PALLLITITA TNFSEGDVTH FICQAAVPKS LQLQLQAPSG NTVPARGGLP ITQLFRILNP NKAPLRLKLR LTYDHFHQSV QEIFEVNNLP VESWQ //