SYNRG_HUMAN
ID SYNRG_HUMAN Reviewed; 1314 AA.
AC Q9UMZ2; A8MWU4; B7ZKZ2; B7ZKZ3; Q17RI2; Q5BKU5; Q6ZT17;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Synergin gamma;
DE AltName: Full=AP1 subunit gamma-binding protein 1;
DE AltName: Full=Gamma-synergin;
GN Name=SYNRG {ECO:0000303|PubMed:28397838, ECO:0000312|HGNC:HGNC:557};
GN Synonyms=AP1GBP1, SYNG;
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), AND INTERACTION WITH AP1G1.
RC TISSUE=Brain;
RX PubMed=10477754; DOI=10.1083/jcb.146.5.993;
RA Page L.J., Sowerby P.J., Lui W.W.Y., Robinson M.S.;
RT "Gamma-synergin: an EH domain-containing protein that interacts with gamma-
RT adaptin.";
RL J. Cell Biol. 146:993-1004(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3; 5 AND 7).
RC TISSUE=Brain, and Lymph;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 27-493 (ISOFORM 1).
RC TISSUE=Brain;
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 [5]
RP INTERACTION WITH GGA1; GGA2; GGA3; AP1G1 AND AP1G2.
RX PubMed=10814529; DOI=10.1006/bbrc.2000.2700;
RA Takatsu H., Yoshino K., Nakayama K.;
RT "Adaptor gamma ear homology domain conserved in gamma-adaptin and GGA
RT proteins that interact with gamma-synergin.";
RL Biochem. Biophys. Res. Commun. 271:719-725(2000).
RN [6]
RP FUNCTION, DOMAIN, AND INTERACTION WITH AP1G1.
RX PubMed=12538641; DOI=10.1083/jcb.200208023;
RA Mills I.G., Praefcke G.J.K., Vallis Y., Peter B.J., Olesen L.E.,
RA Gallop J.L., Butler P.J.G., Evans P.R., McMahon H.T.;
RT "EpsinR: an AP1/clathrin interacting protein involved in vesicle
RT trafficking.";
RL J. Cell Biol. 160:213-222(2003).
RN [7]
RP INTERACTION WITH GGA1; AP1G1 AND AP1G2.
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 [8]
RP FUNCTION, SUBUNIT, IDENTIFICATION IN THE AFTIPHILIN-P200-GAMMA-SYNERGIN
RP COMPLEX, INTERACTION WITH AFTPH; HEATR5B AND GGA1, AND SUBCELLULAR
RP LOCATION.
RX PubMed=15758025; DOI=10.1091/mbc.e04-12-1077;
RA Hirst J., Borner G.H., Harbour M., Robinson M.S.;
RT "The aftiphilin/p200/gamma-synergin complex.";
RL Mol. Biol. Cell 16:2554-2565(2005).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-752, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473; SER-752; SER-909;
RP SER-919; SER-935 AND SER-1075, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473; SER-752; SER-852 AND
RP SER-855, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-513 AND LYS-744, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-720; SER-752 AND SER-1075,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [17]
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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473 AND SER-1075, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473; SER-580; SER-720;
RP SER-752; SER-772; SER-812; SER-919; SER-935; SER-1006; SER-1075; SER-1087;
RP SER-1098 AND THR-1100, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [21]
RP VARIANT HIS-1183.
RX PubMed=28397838; DOI=10.1038/mp.2017.60;
RA Harripaul R., Vasli N., Mikhailov A., Rafiq M.A., Mittal K.,
RA Windpassinger C., Sheikh T.I., Noor A., Mahmood H., Downey S., Johnson M.,
RA Vleuten K., Bell L., Ilyas M., Khan F.S., Khan V., Moradi M., Ayaz M.,
RA Naeem F., Heidari A., Ahmed I., Ghadami S., Agha Z., Zeinali S., Qamar R.,
RA Mozhdehipanah H., John P., Mir A., Ansar M., French L., Ayub M.,
RA Vincent J.B.;
RT "Mapping autosomal recessive intellectual disability: combined microarray
RT and exome sequencing identifies 26 novel candidate genes in 192
RT consanguineous families.";
RL Mol. Psychiatry 23:973-984(2018).
CC -!- FUNCTION: Plays a role in endocytosis and/or membrane trafficking at
CC the trans-Golgi network (TGN) (PubMed:15758025). May act by linking the
CC adapter protein complex AP-1 to other proteins (Probable). Component of
CC clathrin-coated vesicles (PubMed:15758025). Component of the
CC aftiphilin/p200/gamma-synergin complex, which plays roles in AP1G1/AP-
CC 1-mediated protein trafficking including the trafficking of transferrin
CC from early to recycling endosomes, and the membrane trafficking of
CC furin and the lysosomal enzyme cathepsin D between the trans-Golgi
CC network (TGN) and endosomes (PubMed:15758025).
CC {ECO:0000269|PubMed:15758025, ECO:0000305|PubMed:12538641}.
CC -!- SUBUNIT: Self-associates (PubMed:15758025). Interacts with GGA1 (via
CC GAE domain) (PubMed:10814529, PubMed:14665628, PubMed:15758025).
CC Interacts with GGA2 and GGA3 (PubMed:10814529). Interacts with AP1G1
CC (via GAE domain), a subunit of adapter protein complex AP-1
CC (PubMed:10477754, PubMed:10814529, PubMed:12538641, PubMed:14665628).
CC Interacts with AP1G2 (via GAE domain) a subunit of adapter protein
CC complex AP-1 (PubMed:10814529, PubMed:14665628). Component of the
CC aftiphilin/p200/gamma-synergin complex, at least composed of
CC AFTPH/aftiphilin, HEATR5B/p200a and SYNRG/gamma-synergin, which plays a
CC role in the AP1G1/AP-1-mediated trafficking of transferrin from early
CC to recycling endosomes (PubMed:15758025). Within the complex interacts
CC with AFTPH/aftiphilin and HEATR5B/p200a; the interactions are direct
CC (PubMed:15758025). Interacts (via EH domain) with SCAMP1 (By
CC similarity). {ECO:0000250|UniProtKB:Q9JKC9,
CC ECO:0000269|PubMed:10477754, ECO:0000269|PubMed:10814529,
CC ECO:0000269|PubMed:12538641, ECO:0000269|PubMed:14665628,
CC ECO:0000269|PubMed:15758025}.
CC -!- INTERACTION:
CC Q9UMZ2; Q92624: APPBP2; NbExp=3; IntAct=EBI-7240490, EBI-743771;
CC Q9UMZ2-8; Q92624: APPBP2; NbExp=3; IntAct=EBI-12353261, EBI-743771;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9JKC9}. Golgi
CC apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q9JKC9};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q9JKC9}. Cytoplasm,
CC perinuclear region {ECO:0000269|PubMed:15758025}. Cytoplasmic vesicle,
CC clathrin-coated vesicle {ECO:0000269|PubMed:15758025}.
CC Note=Localization at clathrin-coated vesicles depends on
CC AFTPH/aftiphilin (PubMed:15758025). Associates with membranes via the
CC adapter protein complex AP-1 (By similarity). Colocalizes with AP1G1
CC (By similarity). {ECO:0000250|UniProtKB:Q9JKC9,
CC ECO:0000269|PubMed:15758025}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Name=1;
CC IsoId=Q9UMZ2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UMZ2-3; Sequence=VSP_023015;
CC Name=3;
CC IsoId=Q9UMZ2-4; Sequence=VSP_023015, VSP_023016;
CC Name=4;
CC IsoId=Q9UMZ2-5; Sequence=VSP_023016;
CC Name=5;
CC IsoId=Q9UMZ2-6; Sequence=VSP_023015, VSP_043281, VSP_043282;
CC Name=6;
CC IsoId=Q9UMZ2-7; Sequence=VSP_023015, VSP_054733;
CC Name=7;
CC IsoId=Q9UMZ2-8; Sequence=VSP_054732, VSP_023015;
CC Name=8;
CC IsoId=Q9UMZ2-9; Sequence=VSP_023015, VSP_043282, VSP_023016;
CC -!- DOMAIN: The DFXDF motifs mediate the interaction with gamma-appendage
CC subunits AP1G1 and AP1G2. {ECO:0000269|PubMed:12538641}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AK126988; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AF169548; AAD49732.1; -; mRNA.
DR EMBL; AC004099; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC091199; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC090930; AAH90930.1; -; mRNA.
DR EMBL; BC117313; AAI17314.1; -; mRNA.
DR EMBL; BC143476; AAI43477.1; -; mRNA.
DR EMBL; BC143478; AAI43479.1; -; mRNA.
DR EMBL; AK126988; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS11321.1; -. [Q9UMZ2-1]
DR CCDS; CCDS11322.2; -. [Q9UMZ2-4]
DR CCDS; CCDS54113.1; -. [Q9UMZ2-6]
DR CCDS; CCDS54114.1; -. [Q9UMZ2-7]
DR CCDS; CCDS59284.1; -. [Q9UMZ2-8]
DR CCDS; CCDS59285.1; -. [Q9UMZ2-9]
DR RefSeq; NP_001157016.1; NM_001163544.2. [Q9UMZ2-3]
DR RefSeq; NP_001157017.1; NM_001163545.2. [Q9UMZ2-8]
DR RefSeq; NP_001157018.1; NM_001163546.2. [Q9UMZ2-9]
DR RefSeq; NP_001157019.1; NM_001163547.2. [Q9UMZ2-6]
DR RefSeq; NP_009178.3; NM_007247.5. [Q9UMZ2-1]
DR RefSeq; NP_542117.3; NM_080550.4. [Q9UMZ2-4]
DR RefSeq; NP_942583.1; NM_198882.2. [Q9UMZ2-7]
DR RefSeq; XP_016879582.1; XM_017024093.1. [Q9UMZ2-5]
DR PDB; 2MX7; NMR; -; A=279-388.
DR PDBsum; 2MX7; -.
DR AlphaFoldDB; Q9UMZ2; -.
DR SMR; Q9UMZ2; -.
DR BioGRID; 116432; 41.
DR ELM; Q9UMZ2; -.
DR IntAct; Q9UMZ2; 15.
DR MINT; Q9UMZ2; -.
DR STRING; 9606.ENSP00000483453; -.
DR GlyGen; Q9UMZ2; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UMZ2; -.
DR MetOSite; Q9UMZ2; -.
DR PhosphoSitePlus; Q9UMZ2; -.
DR BioMuta; SYNRG; -.
DR DMDM; 143811464; -.
DR EPD; Q9UMZ2; -.
DR jPOST; Q9UMZ2; -.
DR MassIVE; Q9UMZ2; -.
DR MaxQB; Q9UMZ2; -.
DR PaxDb; Q9UMZ2; -.
DR PeptideAtlas; Q9UMZ2; -.
DR PRIDE; Q9UMZ2; -.
DR ProteomicsDB; 2266; -.
DR ProteomicsDB; 85232; -. [Q9UMZ2-1]
DR ProteomicsDB; 85233; -. [Q9UMZ2-3]
DR ProteomicsDB; 85234; -. [Q9UMZ2-4]
DR ProteomicsDB; 85235; -. [Q9UMZ2-5]
DR ProteomicsDB; 85236; -. [Q9UMZ2-6]
DR Antibodypedia; 74878; 35 antibodies from 11 providers.
DR DNASU; 11276; -.
DR Ensembl; ENST00000610513.2; ENSP00000478707.1; ENSG00000274047.4. [Q9UMZ2-6]
DR Ensembl; ENST00000612223.5; ENSP00000483453.1; ENSG00000275066.5. [Q9UMZ2-1]
DR Ensembl; ENST00000613407.4; ENSP00000483152.1; ENSG00000274047.4. [Q9UMZ2-7]
DR Ensembl; ENST00000614941.4; ENSP00000481151.1; ENSG00000275066.5. [Q9UMZ2-6]
DR Ensembl; ENST00000616179.4; ENSP00000482962.1; ENSG00000275066.5. [Q9UMZ2-9]
DR Ensembl; ENST00000618176.4; ENSP00000482597.1; ENSG00000274047.4. [Q9UMZ2-4]
DR Ensembl; ENST00000618402.4; ENSP00000480288.1; ENSG00000274047.4. [Q9UMZ2-1]
DR Ensembl; ENST00000619541.4; ENSP00000477885.1; ENSG00000275066.5. [Q9UMZ2-8]
DR Ensembl; ENST00000621136.4; ENSP00000484529.1; ENSG00000275066.5. [Q9UMZ2-4]
DR Ensembl; ENST00000622045.4; ENSP00000483063.1; ENSG00000275066.5. [Q9UMZ2-7]
DR Ensembl; ENST00000632841.1; ENSP00000487672.1; ENSG00000274047.4. [Q9UMZ2-9]
DR Ensembl; ENST00000633429.1; ENSP00000488473.1; ENSG00000274047.4. [Q9UMZ2-8]
DR GeneID; 11276; -.
DR KEGG; hsa:11276; -.
DR MANE-Select; ENST00000612223.5; ENSP00000483453.1; NM_007247.6; NP_009178.3.
DR UCSC; uc002hoa.4; human. [Q9UMZ2-1]
DR CTD; 11276; -.
DR DisGeNET; 11276; -.
DR GeneCards; SYNRG; -.
DR HGNC; HGNC:557; SYNRG.
DR HPA; ENSG00000275066; Low tissue specificity.
DR MIM; 607291; gene.
DR neXtProt; NX_Q9UMZ2; -.
DR OpenTargets; ENSG00000275066; -.
DR PharmGKB; PA24847; -.
DR VEuPathDB; HostDB:ENSG00000275066; -.
DR eggNOG; KOG0998; Eukaryota.
DR GeneTree; ENSGT00390000010789; -.
DR HOGENOM; CLU_263817_0_0_1; -.
DR InParanoid; Q9UMZ2; -.
DR OMA; GPIAMQX; -.
DR OrthoDB; 226328at2759; -.
DR PhylomeDB; Q9UMZ2; -.
DR TreeFam; TF316700; -.
DR PathwayCommons; Q9UMZ2; -.
DR SignaLink; Q9UMZ2; -.
DR BioGRID-ORCS; 11276; 12 hits in 1072 CRISPR screens.
DR ChiTaRS; SYNRG; human.
DR GeneWiki; Synergin_gamma; -.
DR GenomeRNAi; 11276; -.
DR Pharos; Q9UMZ2; Tdark.
DR PRO; PR:Q9UMZ2; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9UMZ2; protein.
DR Bgee; ENSG00000275066; Expressed in bone marrow cell and 109 other tissues.
DR ExpressionAtlas; Q9UMZ2; baseline and differential.
DR Genevisible; Q9UMZ2; HS.
DR GO; GO:0030121; C:AP-1 adaptor complex; TAS:ProtInc.
DR GO; GO:0030130; C:clathrin coat of trans-Golgi network vesicle; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0005794; C:Golgi apparatus; TAS:ProtInc.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0006886; P:intracellular protein transport; TAS:ProtInc.
DR CDD; cd00052; EH; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR000261; EH_dom.
DR InterPro; IPR039656; SYNRG.
DR PANTHER; PTHR15463; PTHR15463; 1.
DR SMART; SM00027; EH; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS50031; EH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Coiled coil; Cytoplasm;
KW Cytoplasmic vesicle; Endocytosis; Golgi apparatus; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Repeat; Transport.
FT CHAIN 1..1314
FT /note="Synergin gamma"
FT /id="PRO_0000072387"
FT DOMAIN 295..388
FT /note="EH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT REGION 178..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 518..786
FT /note="Interaction with AP1G1"
FT /evidence="ECO:0000269|PubMed:10477754"
FT REGION 666..678
FT /note="Interaction with AP1G1, AP1G2 and GGA1"
FT /evidence="ECO:0000269|PubMed:14665628"
FT REGION 972..1026
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1073..1102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 115..155
FT /evidence="ECO:0000255"
FT MOTIF 457..461
FT /note="DFXDF motif 1"
FT MOTIF 690..694
FT /note="DFXDF motif 2"
FT MOTIF 775..779
FT /note="DFXDF motif 3"
FT COMPBIAS 463..496
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 974..994
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 995..1023
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1079..1096
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 473
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 513
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 580
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 720
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 744
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 752
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 772
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 812
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 852
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 855
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 909
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 919
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 935
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1006
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1073
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JKC9"
FT MOD_RES 1075
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1087
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1098
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1100
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 40
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054732"
FT VAR_SEQ 198..275
FT /note="Missing (in isoform 2, isoform 3, isoform 5, isoform
FT 6, isoform 7 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023015"
FT VAR_SEQ 366..448
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043281"
FT VAR_SEQ 870..914
FT /note="Missing (in isoform 5 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043282"
FT VAR_SEQ 1222
FT /note="T -> TCCWEKMTVITKHLSPYHELLEEK (in isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_054733"
FT VAR_SEQ 1260..1271
FT /note="Missing (in isoform 3, isoform 4 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023016"
FT VARIANT 40
FT /note="A -> G (in dbSNP:rs12944821)"
FT /id="VAR_051395"
FT VARIANT 222
FT /note="T -> A (in dbSNP:rs12602536)"
FT /id="VAR_051396"
FT VARIANT 1183
FT /note="R -> H (found in a consanguineous family with
FT intellectual disability; unknown pathological significance;
FT dbSNP:rs370465279)"
FT /evidence="ECO:0000269|PubMed:28397838"
FT /id="VAR_080768"
FT CONFLICT 213
FT /note="S -> P (in Ref. 4; AK126988)"
FT /evidence="ECO:0000305"
FT CONFLICT 349
FT /note="K -> R (in Ref. 4; AK126988)"
FT /evidence="ECO:0000305"
FT CONFLICT 1123
FT /note="E -> K (in Ref. 1; AAD49732)"
FT /evidence="ECO:0000305"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:2MX7"
FT HELIX 291..294
FT /evidence="ECO:0007829|PDB:2MX7"
FT HELIX 301..309
FT /evidence="ECO:0007829|PDB:2MX7"
FT HELIX 318..327
FT /evidence="ECO:0007829|PDB:2MX7"
FT HELIX 332..340
FT /evidence="ECO:0007829|PDB:2MX7"
FT HELIX 352..366
FT /evidence="ECO:0007829|PDB:2MX7"
FT HELIX 374..378
FT /evidence="ECO:0007829|PDB:2MX7"
SQ SEQUENCE 1314 AA; 140654 MW; 70C105203EF0BBBF CRC64;
MALRPGAGSG GGGAAGAGAG SAGGGGFMFP VAGGIRPPQA GLMPMQQQGF PMVSVMQPNM
QGIMGMNYSS QMSQGPIAMQ AGIPMGPMPA AGMPYLGQAP FLGMRPPGPQ YTPDMQKQFA
EEQQKRFEQQ QKLLEEERKR RQFEEQKQKL RLLSSVKPKT GEKSRDDALE AIKGNLDGFS
RDAKMHPTPA SHPKKPGPSL EEKFLVSCDI STSGQEQIKL NTSEVGHKAL GPGSSKKYPS
LMASNGVAVD GCVSGTTTAE AENTSDQNLS IEESGVGVFP SQDPAQPRMP PWIYNESLVP
DAYKKILETT MTPTGIDTAK LYPILMSSGL PRETLGQIWA LANRTTPGKL TKEELYTVLA
MIAVTQRGVP AMSPDALNQF PAAPIPTLSG FSMTLPTPVS QPTVIPSGPA GSMPLSLGQP
VMGINLVGPV GGAAAQASSG FIPTYPANQV VKPEEDDFQD FQDASKSGSL DDSFSDFQEL
PASSKTSNSQ HGNSAPSLLM PLPGTKALPS MDKYAVFKGI AADKSSENTV PPGDPGDKYS
AFRELEQTAE NKPLGESFAE FRSAGTDDGF TDFKTADSVS PLEPPTKDKT FPPSFPSGTI
QQKQQTQVKN PLNLADLDMF SSVNCSSEKP LSFSAVFSTS KSVSTPQSTG SAATMTALAA
TKTSSLADDF GEFSLFGEYS GLAPVGEQDD FADFMAFSNS SISSEQKPDD KYDALKEEAS
PVPLTSNVGS TVKGGQNSTA ASTKYDVFRQ LSLEGSGLGV EDLKDNTPSG KSDDDFADFH
SSKFSSINSD KSLGEKAVAF RHTKEDSASV KSLDLPSIGG SSVGKEDSED ALSVQFDMKL
ADVGGDLKHV MSDSSLDLPT VSGQHPPAAD IEDLKYAAFG SYSSNFAVST LTSYDWSDRD
DATQGRKLSP FVLSAGSGSP SATSILQKKE TSFGSSENIT MTSLSKVTTF VSEDALPETT
FPALASFKDT IPQTSEQKEY ENRDYKDFTK QDLPTAERSQ EATCPSPASS GASQETPNEC
SDDFGEFQSE KPKISKFDFL VATSQSKMKS SEEMIKSELA TFDLSVQGSH KRSLSLGDKE
ISRSSPSPAL EQPFRDRSNT LNEKPALPVI RDKYKDLTGE VEENERYAYE WQRCLGSALN
VIKKANDTLN GISSSSVCTE VIQSAQGMEY LLGVVEVYRV TKRVELGIKA TAVCSEKLQQ
LLKDIDKVWN NLIGFMSLAT LTPDENSLDF SSCMLRPGIK NAQELACGVC LLNVDSRSRK
EEKPAEEHPK KAFNSETDSF KLAYGGHQYH ASCANFWINC VEPKPPGLVL PDLL
