AP1M2_HUMAN
ID AP1M2_HUMAN Reviewed; 423 AA.
AC Q9Y6Q5; B2RDV5; Q9BSI8;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=AP-1 complex subunit mu-2;
DE AltName: Full=AP-mu chain family member mu1B;
DE AltName: Full=Adaptor protein complex AP-1 subunit mu-2;
DE AltName: Full=Adaptor-related protein complex 1 subunit mu-2;
DE AltName: Full=Clathrin assembly protein complex 1 mu-2 medium chain 2;
DE AltName: Full=Golgi adaptor HA1/AP1 adaptin mu-2 subunit;
DE AltName: Full=Mu-adaptin 2;
DE AltName: Full=Mu1B-adaptin;
GN Name=AP1M2;
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] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=10338135; DOI=10.1016/s0014-5793(99)00432-9;
RA Ohno H., Tomemori T., Nakatsu F., Okazaki Y., Aguilar R.C., Foelsch H.,
RA Mellman I., Saito T., Shirasawa T., Bonifacino J.S.;
RT "Mu1B, a novel adaptor medium chain expressed in polarized epithelial
RT cells.";
RL FEBS Lett. 449:215-220(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Colon, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
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).
CC -!- FUNCTION: Subunit of clathrin-associated adaptor protein complex 1 that
CC plays a role in protein sorting in the trans-Golgi network (TGN) and
CC endosomes. The AP complexes mediate the recruitment of clathrin to
CC membranes and the recognition of sorting signals within the cytosolic
CC tails of transmembrane cargo molecules.
CC -!- SUBUNIT: Adaptor protein complex 1 (AP-1) is a heterotetramer composed
CC of two large adaptins (gamma-type subunit AP1G1 and beta-type subunit
CC AP1B1), a medium adaptin (mu-type subunit AP1M1 or AP1M2) and a small
CC adaptin (sigma-type subunit AP1S1 or AP1S2 or AP1S3). Interacts with
CC P2X4 (By similarity). {ECO:0000250|UniProtKB:D3ZRP6}.
CC -!- INTERACTION:
CC Q9Y6Q5; P63010: AP2B1; NbExp=4; IntAct=EBI-752250, EBI-432924;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus. Cytoplasmic vesicle, clathrin-
CC coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side.
CC Note=Component of the coat surrounding the cytoplasmic face of coated
CC vesicles located at the Golgi complex.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y6Q5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y6Q5-2; Sequence=VSP_000169;
CC -!- PTM: Phosphorylation of membrane-bound AP1M1/AP1M2 increases its
CC affinity for sorting signals. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the adaptor complexes medium subunit family.
CC {ECO:0000305}.
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DR EMBL; AF020797; AAD25870.2; -; mRNA.
DR EMBL; AK315689; BAG38052.1; -; mRNA.
DR EMBL; CH471106; EAW84124.1; -; Genomic_DNA.
DR EMBL; BC003387; AAH03387.1; -; mRNA.
DR EMBL; BC003612; AAH03612.1; -; mRNA.
DR EMBL; BC005021; AAH05021.1; -; mRNA.
DR CCDS; CCDS45964.1; -. [Q9Y6Q5-1]
DR CCDS; CCDS77234.1; -. [Q9Y6Q5-2]
DR RefSeq; NP_001287816.1; NM_001300887.1. [Q9Y6Q5-2]
DR RefSeq; NP_005489.2; NM_005498.4. [Q9Y6Q5-1]
DR AlphaFoldDB; Q9Y6Q5; -.
DR SMR; Q9Y6Q5; -.
DR BioGRID; 115364; 80.
DR ComplexPortal; CPX-5050; Endothelial AP-1 Adaptor complex, sigma1a variant.
DR CORUM; Q9Y6Q5; -.
DR IntAct; Q9Y6Q5; 20.
DR MINT; Q9Y6Q5; -.
DR STRING; 9606.ENSP00000250244; -.
DR iPTMnet; Q9Y6Q5; -.
DR PhosphoSitePlus; Q9Y6Q5; -.
DR BioMuta; AP1M2; -.
DR DMDM; 13123953; -.
DR EPD; Q9Y6Q5; -.
DR jPOST; Q9Y6Q5; -.
DR MassIVE; Q9Y6Q5; -.
DR MaxQB; Q9Y6Q5; -.
DR PaxDb; Q9Y6Q5; -.
DR PeptideAtlas; Q9Y6Q5; -.
DR PRIDE; Q9Y6Q5; -.
DR ProteomicsDB; 86763; -. [Q9Y6Q5-1]
DR ProteomicsDB; 86764; -. [Q9Y6Q5-2]
DR Antibodypedia; 25388; 133 antibodies from 25 providers.
DR DNASU; 10053; -.
DR Ensembl; ENST00000250244.11; ENSP00000250244.5; ENSG00000129354.12. [Q9Y6Q5-1]
DR Ensembl; ENST00000590923.5; ENSP00000465685.1; ENSG00000129354.12. [Q9Y6Q5-2]
DR GeneID; 10053; -.
DR KEGG; hsa:10053; -.
DR MANE-Select; ENST00000250244.11; ENSP00000250244.5; NM_005498.5; NP_005489.2.
DR UCSC; uc002mpc.4; human. [Q9Y6Q5-1]
DR CTD; 10053; -.
DR DisGeNET; 10053; -.
DR GeneCards; AP1M2; -.
DR HGNC; HGNC:558; AP1M2.
DR HPA; ENSG00000129354; Low tissue specificity.
DR MIM; 607309; gene.
DR neXtProt; NX_Q9Y6Q5; -.
DR OpenTargets; ENSG00000129354; -.
DR PharmGKB; PA24849; -.
DR VEuPathDB; HostDB:ENSG00000129354; -.
DR eggNOG; KOG0937; Eukaryota.
DR GeneTree; ENSGT00940000159089; -.
DR HOGENOM; CLU_026996_0_0_1; -.
DR InParanoid; Q9Y6Q5; -.
DR OMA; FMWIKYS; -.
DR OrthoDB; 725236at2759; -.
DR PhylomeDB; Q9Y6Q5; -.
DR TreeFam; TF300393; -.
DR PathwayCommons; Q9Y6Q5; -.
DR Reactome; R-HSA-164940; Nef mediated downregulation of MHC class I complex cell surface expression.
DR Reactome; R-HSA-2132295; MHC class II antigen presentation.
DR Reactome; R-HSA-432720; Lysosome Vesicle Biogenesis.
DR Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis.
DR SignaLink; Q9Y6Q5; -.
DR BioGRID-ORCS; 10053; 12 hits in 1066 CRISPR screens.
DR ChiTaRS; AP1M2; human.
DR GeneWiki; AP1M2; -.
DR GenomeRNAi; 10053; -.
DR Pharos; Q9Y6Q5; Tbio.
DR PRO; PR:Q9Y6Q5; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9Y6Q5; protein.
DR Bgee; ENSG00000129354; Expressed in mucosa of transverse colon and 124 other tissues.
DR ExpressionAtlas; Q9Y6Q5; baseline and differential.
DR Genevisible; Q9Y6Q5; HS.
DR GO; GO:0030121; C:AP-1 adaptor complex; IC:ComplexPortal.
DR GO; GO:0030136; C:clathrin-coated vesicle; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005765; C:lysosomal membrane; TAS:Reactome.
DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome.
DR GO; GO:0035615; F:clathrin adaptor activity; IBA:GO_Central.
DR GO; GO:0110010; P:basolateral protein secretion; IC:ComplexPortal.
DR GO; GO:0006605; P:protein targeting; TAS:ProtInc.
DR GO; GO:0006903; P:vesicle targeting; TAS:ProtInc.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR InterPro; IPR036168; AP2_Mu_C_sf.
DR InterPro; IPR022775; AP_mu_sigma_su.
DR InterPro; IPR001392; Clathrin_mu.
DR InterPro; IPR018240; Clathrin_mu_CS.
DR InterPro; IPR011012; Longin-like_dom_sf.
DR InterPro; IPR028565; MHD.
DR Pfam; PF00928; Adap_comp_sub; 1.
DR Pfam; PF01217; Clat_adaptor_s; 1.
DR PIRSF; PIRSF005992; Clathrin_mu; 1.
DR PRINTS; PR00314; CLATHRINADPT.
DR SUPFAM; SSF49447; SSF49447; 1.
DR SUPFAM; SSF64356; SSF64356; 1.
DR PROSITE; PS00990; CLAT_ADAPTOR_M_1; 1.
DR PROSITE; PS00991; CLAT_ADAPTOR_M_2; 1.
DR PROSITE; PS51072; MHD; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasmic vesicle; Golgi apparatus; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..423
FT /note="AP-1 complex subunit mu-2"
FT /id="PRO_0000193772"
FT DOMAIN 168..421
FT /note="MHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00404"
FT VAR_SEQ 225
FT /note="R -> LSG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_000169"
FT CONFLICT 364
FT /note="S -> R (in Ref. 4; AAH05021)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 423 AA; 48108 MW; A3F6FDF8659DD6F7 CRC64;
MSASAVFILD VKGKPLISRN YKGDVAMSKI EHFMPLLVQR EEEGALAPLL SHGQVHFLWI
KHSNLYLVAT TSKNANASLV YSFLYKTIEV FCEYFKELEE ESIRDNFVIV YELLDELMDF
GFPQTTDSKI LQEYITQQSN KLETGKSRVP PTVTNAVSWR SEGIKYKKNE VFIDVIESVN
LLVNANGSVL LSEIVGTIKL KVFLSGMPEL RLGLNDRVLF ELTGRSKNKS VELEDVKFHQ
CVRLSRFDND RTISFIPPDG DFELMSYRLS TQVKPLIWIE SVIEKFSHSR VEIMVKAKGQ
FKKQSVANGV EISVPVPSDA DSPRFKTSVG SAKYVPERNV VIWSIKSFPG GKEYLMRAHF
GLPSVEKEEV EGRPPIGVKF EIPYFTVSGI QVRYMKIIEK SGYQALPWVR YITQSGDYQL
RTS
