PACS1_HUMAN
ID PACS1_HUMAN Reviewed; 963 AA.
AC Q6VY07; Q6PJY6; Q6PKB6; Q7Z590; Q7Z5W4; Q8N8K6; Q96MW0; Q9NW92; Q9ULP5;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Phosphofurin acidic cluster sorting protein 1;
DE Short=PACS-1;
GN Name=PACS1; Synonyms=KIAA1175;
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).
RA Wan L., Xiang Y., Simmen T., Thomas G.;
RT "Human PACS-1, a endosome-TGN sorting connector.";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Embryo, and Fetal 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, Kidney, and Uterus;
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 323-963 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10574461; DOI=10.1093/dnares/6.5.329;
RA Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.;
RT "Characterization of cDNA clones selected by the GeneMark analysis from
RT size-fractionated cDNA libraries from human brain.";
RL DNA Res. 6:329-336(1999).
RN [5]
RP FUNCTION, AND SUBUNIT.
RX PubMed=11331585; DOI=10.1093/emboj/20.9.2191;
RA Crump C.M., Xiang Y., Thomas L., Gu F., Austin C., Tooze S.A., Thomas G.;
RT "PACS-1 binding to adaptors is required for acidic cluster motif-mediated
RT protein traffic.";
RL EMBO J. 20:2191-2201(2001).
RN [6]
RP INTERACTION WITH HIV-1 NEF (MICROBIAL INFECTION).
RX PubMed=10707087; DOI=10.1038/35004038;
RA Piguet V., Wan L., Borel C., Mangasarian A., Demaurex N., Thomas G.,
RA Trono D.;
RT "HIV-1 Nef protein binds to the cellular protein PACS-1 to downregulate
RT class I major histocompatibility complexes.";
RL Nat. Cell Biol. 2:163-167(2000).
RN [7]
RP INTERACTION WITH HIV-1 NEF (MICROBIAL INFECTION).
RX PubMed=12526811; DOI=10.1016/s0092-8674(02)01162-5;
RA Blagoveshchenskaya A.D., Thomas L., Feliciangeli S.F., Hung C.-H.,
RA Thomas G.;
RT "HIV-1 Nef downregulates MHC-I by a PACS-1- and PI3K-regulated ARF6
RT endocytic pathway.";
RL Cell 111:853-866(2002).
RN [8]
RP INTERACTION WITH PKD2, AND FUNCTION.
RX PubMed=15692563; DOI=10.1038/sj.emboj.7600566;
RA Koettgen M., Benzing T., Simmen T., Tauber R., Buchholz B.,
RA Feliciangeli S., Huber T.B., Schermer B., Kramer-Zucker A., Hoepker K.,
RA Simmen K.C., Tschucke C.C., Sandford R., Kim E., Thomas G., Walz G.;
RT "Trafficking of TRPP2 by PACS proteins represents a novel mechanism of ion
RT channel regulation.";
RL EMBO J. 24:705-716(2005).
RN [9]
RP INTERACTION WITH NPHP1.
RX PubMed=16308564; DOI=10.1038/sj.emboj.7600885;
RA Schermer B., Hoepker K., Omran H., Ghenoiu C., Fliegauf M., Fekete A.,
RA Horvath J., Koettgen M., Hackl M., Zschiedrich S., Huber T.B.,
RA Kramer-Zucker A., Zentgraf H., Blaukat A., Walz G., Benzing T.;
RT "Phosphorylation by casein kinase 2 induces PACS-1 binding of nephrocystin
RT and targeting to cilia.";
RL EMBO J. 24:4415-4424(2005).
RN [10]
RP INTERACTION WITH SORL1.
RX PubMed=17855360; DOI=10.1074/jbc.m705073200;
RA Schmidt V., Sporbert A., Rohe M., Reimer T., Rehm A., Andersen O.M.,
RA Willnow T.E.;
RT "SorLA/LR11 regulates processing of amyloid precursor protein via
RT interaction with adaptors GGA and PACS-1.";
RL J. Biol. Chem. 282:32956-32964(2007).
RN [11]
RP INTERACTION WITH SORL1.
RX PubMed=17646382; DOI=10.1128/mcb.00815-07;
RA Nielsen M.S., Gustafsen C., Madsen P., Nyengaard J.R., Hermey G., Bakke O.,
RA Mari M., Schu P., Pohlmann R., Dennes A., Petersen C.M.;
RT "Sorting by the cytoplasmic domain of the amyloid precursor protein binding
RT receptor SorLA.";
RL Mol. Cell. Biol. 27:6842-6851(2007).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [13]
RP INTERACTION WITH HIV-1 NEF (MICROBIAL INFECTION).
RX PubMed=18296443; DOI=10.1074/jbc.m707572200;
RA Atkins K.M., Thomas L., Youker R.T., Harriff M.J., Pissani F., You H.,
RA Thomas G.;
RT "HIV-1 Nef binds PACS-2 to assemble a multikinase cascade that triggers
RT major histocompatibility complex class I (MHC-I) down-regulation: analysis
RT using short interfering RNA and knock-out mice.";
RL J. Biol. Chem. 283:11772-11784(2008).
RN [14]
RP IDENTIFICATION BY 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-379; SER-430; THR-504;
RP SER-529 AND SER-534, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [17]
RP 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 [18]
RP 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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-531, AND IDENTIFICATION BY
RP 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 [20]
RP INTERACTION WITH EPSTEIN-BARR VIRUS PROTEIN BBLF1 (MICROBIAL INFECTION).
RX PubMed=22740416; DOI=10.1128/jvi.01126-12;
RA Chiu Y.F., Sugden B., Chang P.J., Chen L.W., Lin Y.J., Lan Y.C., Lai C.H.,
RA Liou J.Y., Liu S.T., Hung C.H.;
RT "Characterization and intracellular trafficking of Epstein-Barr virus
RT BBLF1, a protein involved in virion maturation.";
RL J. Virol. 86:9647-9655(2012).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-430; SER-495; THR-504;
RP SER-519; SER-529 AND SER-534, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE 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 [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-381, AND IDENTIFICATION BY
RP 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 [23]
RP VARIANT SHMS TRP-203.
RX PubMed=23159249; DOI=10.1016/j.ajhg.2012.10.013;
RA Schuurs-Hoeijmakers J.H., Oh E.C., Vissers L.E., Swinkels M.E.,
RA Gilissen C., Willemsen M.A., Holvoet M., Steehouwer M., Veltman J.A.,
RA de Vries B.B., van Bokhoven H., de Brouwer A.P., Katsanis N., Devriendt K.,
RA Brunner H.G.;
RT "Recurrent de novo mutations in PACS1 cause defective cranial-neural-crest
RT migration and define a recognizable intellectual-disability syndrome.";
RL Am. J. Hum. Genet. 91:1122-1127(2012).
CC -!- FUNCTION: Coat protein that is involved in the localization of trans-
CC Golgi network (TGN) membrane proteins that contain acidic cluster
CC sorting motifs. Controls the endosome-to-Golgi trafficking of furin and
CC mannose-6-phosphate receptor by connecting the acidic-cluster-
CC containing cytoplasmic domain of these molecules with the adapter-
CC protein complex-1 (AP-1) of endosomal clathrin-coated membrane pits.
CC Involved in HIV-1 nef-mediated removal of MHC-I from the cell surface
CC to the TGN. {ECO:0000269|PubMed:11331585, ECO:0000269|PubMed:15692563}.
CC -!- SUBUNIT: Associates with AP-1 and AP-3 but not with AP-2 complexes
CC (PubMed:11331585). Interacts with FURIN (By similarity). Forms a
CC ternary complex with FURIN and AP-1 (PubMed:11331585). Interacts with
CC NPHP1; the interaction is dependent of NPHP1 phosphorylation by CK2
CC (PubMed:16308564). Interacts with PKD2 (via acidic region)
CC (PubMed:15692563). Interacts with SORL1 (PubMed:17855360,
CC PubMed:17646382). {ECO:0000250|UniProtKB:Q8K212,
CC ECO:0000269|PubMed:11331585, ECO:0000269|PubMed:15692563,
CC ECO:0000269|PubMed:16308564, ECO:0000269|PubMed:17646382,
CC ECO:0000269|PubMed:17855360}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HIV-1 Nef.
CC {ECO:0000269|PubMed:10707087, ECO:0000269|PubMed:12526811,
CC ECO:0000269|PubMed:18296443}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Epstein-barr virus
CC protein BBLF1. {ECO:0000269|PubMed:22740416}.
CC -!- INTERACTION:
CC Q6VY07; Q92870-2: APBB2; NbExp=3; IntAct=EBI-2555014, EBI-21535880;
CC Q6VY07; P54253: ATXN1; NbExp=6; IntAct=EBI-2555014, EBI-930964;
CC Q6VY07; P67870: CSNK2B; NbExp=3; IntAct=EBI-2555014, EBI-348169;
CC Q6VY07; Q9NZ52: GGA3; NbExp=5; IntAct=EBI-2555014, EBI-447404;
CC Q6VY07; P42858: HTT; NbExp=18; IntAct=EBI-2555014, EBI-466029;
CC Q6VY07; P11717: IGF2R; NbExp=2; IntAct=EBI-2555014, EBI-1048580;
CC Q6VY07; D3DTS7: PMP22; NbExp=3; IntAct=EBI-2555014, EBI-25882629;
CC Q6VY07; P37840: SNCA; NbExp=3; IntAct=EBI-2555014, EBI-985879;
CC Q6VY07; Q13148: TARDBP; NbExp=6; IntAct=EBI-2555014, EBI-372899;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
CC {ECO:0000250|UniProtKB:O88588}. Note=Localizes in the perinuclear
CC region, probably the TGN. {ECO:0000305|PubMed:11331585}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6VY07-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6VY07-2; Sequence=VSP_011557;
CC -!- DISEASE: Schuurs-Hoeijmakers syndrome (SHMS) [MIM:615009]: An autosomal
CC dominant intellectual developmental disorder characterized by
CC intellectual disability in combination with distinct craniofacial
CC features and genital abnormalities. {ECO:0000269|PubMed:23159249}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the PACS family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH09936.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB71164.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY320283; AAQ67682.1; -; mRNA.
DR EMBL; AK001071; BAA91491.1; -; mRNA.
DR EMBL; AK056361; BAB71164.1; ALT_INIT; mRNA.
DR EMBL; AK096644; BAC04831.1; -; mRNA.
DR EMBL; BC003173; AAH03173.1; -; mRNA.
DR EMBL; BC010096; AAH10096.1; -; mRNA.
DR EMBL; BC009936; AAH09936.1; ALT_INIT; mRNA.
DR EMBL; BC052577; AAH52577.1; -; mRNA.
DR EMBL; BC055288; AAH55288.1; -; mRNA.
DR EMBL; AB033001; BAA86489.1; -; mRNA.
DR CCDS; CCDS8129.1; -. [Q6VY07-1]
DR RefSeq; NP_060496.2; NM_018026.3. [Q6VY07-1]
DR AlphaFoldDB; Q6VY07; -.
DR BioGRID; 120816; 40.
DR CORUM; Q6VY07; -.
DR IntAct; Q6VY07; 23.
DR MINT; Q6VY07; -.
DR STRING; 9606.ENSP00000316454; -.
DR GlyGen; Q6VY07; 3 sites, 1 O-linked glycan (3 sites).
DR iPTMnet; Q6VY07; -.
DR PhosphoSitePlus; Q6VY07; -.
DR BioMuta; PACS1; -.
DR DMDM; 52000804; -.
DR EPD; Q6VY07; -.
DR jPOST; Q6VY07; -.
DR MassIVE; Q6VY07; -.
DR MaxQB; Q6VY07; -.
DR PaxDb; Q6VY07; -.
DR PeptideAtlas; Q6VY07; -.
DR PRIDE; Q6VY07; -.
DR ProteomicsDB; 67734; -. [Q6VY07-1]
DR ProteomicsDB; 67735; -. [Q6VY07-2]
DR ABCD; Q6VY07; 12 sequenced antibodies.
DR Antibodypedia; 44366; 97 antibodies from 27 providers.
DR DNASU; 55690; -.
DR Ensembl; ENST00000320580.9; ENSP00000316454.4; ENSG00000175115.13. [Q6VY07-1]
DR GeneID; 55690; -.
DR KEGG; hsa:55690; -.
DR MANE-Select; ENST00000320580.9; ENSP00000316454.4; NM_018026.4; NP_060496.2.
DR UCSC; uc001oha.3; human. [Q6VY07-1]
DR CTD; 55690; -.
DR DisGeNET; 55690; -.
DR GeneCards; PACS1; -.
DR GeneReviews; PACS1; -.
DR HGNC; HGNC:30032; PACS1.
DR HPA; ENSG00000175115; Low tissue specificity.
DR MalaCards; PACS1; -.
DR MIM; 607492; gene.
DR MIM; 615009; phenotype.
DR neXtProt; NX_Q6VY07; -.
DR OpenTargets; ENSG00000175115; -.
DR Orphanet; 329224; Intellectual disability-craniofacial dysmorphism-cryptorchidism syndrome.
DR PharmGKB; PA134989529; -.
DR VEuPathDB; HostDB:ENSG00000175115; -.
DR eggNOG; KOG3709; Eukaryota.
DR GeneTree; ENSGT00950000183209; -.
DR HOGENOM; CLU_013074_0_0_1; -.
DR InParanoid; Q6VY07; -.
DR OMA; LVNATDW; -.
DR PhylomeDB; Q6VY07; -.
DR TreeFam; TF314240; -.
DR PathwayCommons; Q6VY07; -.
DR Reactome; R-HSA-164940; Nef mediated downregulation of MHC class I complex cell surface expression.
DR SignaLink; Q6VY07; -.
DR SIGNOR; Q6VY07; -.
DR BioGRID-ORCS; 55690; 27 hits in 1078 CRISPR screens.
DR ChiTaRS; PACS1; human.
DR GeneWiki; PACS1; -.
DR GenomeRNAi; 55690; -.
DR Pharos; Q6VY07; Tbio.
DR PRO; PR:Q6VY07; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q6VY07; protein.
DR Bgee; ENSG00000175115; Expressed in cortical plate and 177 other tissues.
DR ExpressionAtlas; Q6VY07; baseline and differential.
DR Genevisible; Q6VY07; HS.
DR GO; GO:0030137; C:COPI-coated vesicle; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:BHF-UCL.
DR GO; GO:0034067; P:protein localization to Golgi apparatus; IEA:Ensembl.
DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:BHF-UCL.
DR InterPro; IPR019381; Phosphofurin_acidic_CS-1.
DR PANTHER; PTHR13280; PTHR13280; 1.
DR Pfam; PF10254; Pacs-1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Disease variant;
KW Golgi apparatus; Host-virus interaction; Intellectual disability;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..963
FT /note="Phosphofurin acidic cluster sorting protein 1"
FT /id="PRO_0000058171"
FT REGION 1..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 168..175
FT /note="Involved in binding to AP-1"
FT REGION 262..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 760..804
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 353..377
FT /evidence="ECO:0000255"
FT COMPBIAS 34..48
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..289
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..500
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..532
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 767..804
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K212"
FT MOD_RES 46
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8K212"
FT MOD_RES 251
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8K212"
FT MOD_RES 379
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 381
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 430
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 495
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 504
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 519
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 528
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88588"
FT MOD_RES 529
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 531
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 534
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 917..963
FT /note="AKQQQTMLRVSIDGVEWSDIKFFQLAAQWPTHVKHFPVGLFSGSKAT -> S
FT PSLGPSLGPDPSSQPGFPPAGSFPPCHLPLTNPGSEPLIPDRPCSQEWLRTQGPSPALC
FT TPQPGHLRPTAPLELFSCPLTPSQKFLHRTSF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_011557"
FT VARIANT 203
FT /note="R -> W (in SHMS; dbSNP:rs398123009)"
FT /evidence="ECO:0000269|PubMed:23159249"
FT /id="VAR_069534"
FT VARIANT 302
FT /note="F -> L (in dbSNP:rs12798852)"
FT /id="VAR_053797"
FT CONFLICT 171..220
FT /note="Missing (in Ref. 2; BAC04831)"
FT /evidence="ECO:0000305"
FT CONFLICT 649
FT /note="K -> M (in Ref. 2; BAA91491)"
FT /evidence="ECO:0000305"
FT CONFLICT 771
FT /note="P -> S (in Ref. 2; BAC04831)"
FT /evidence="ECO:0000305"
FT CONFLICT 803
FT /note="S -> N (in Ref. 1; AAQ67682)"
FT /evidence="ECO:0000305"
FT CONFLICT 882
FT /note="K -> L (in Ref. 1; AAQ67682)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 963 AA; 104898 MW; 0F6B2CA24F7CD567 CRC64;
MAERGGAGGG PGGAGGGSGQ RGSGVAQSPQ QPPPQQQQQQ PPQQPTPPKL AQATSSSSST
SAAAASSSSS STSTSMAVAV ASGSAPPGGP GPGRTPAPVQ MNLYATWEVD RSSSSCVPRL
FSLTLKKLVM LKEMDKDLNS VVIAVKLQGS KRILRSNEIV LPASGLVETE LQLTFSLQYP
HFLKRDANKL QIMLQRRKRY KNRTILGYKT LAVGLINMAE VMQHPNEGAL VLGLHSNVKD
VSVPVAEIKI YSLSSQPIDH EGIKSKLSDR SPDIDNYSEE EEESFSSEQE GSDDPLHGQD
LFYEDEDLRK VKKTRRKLTS TSAITRQPNI KQKFVALLKR FKVSDEVGFG LEHVSREQIR
EVEEDLDELY DSLEMYNPSD SGPEMEETES ILSTPKPKLK PFFEGMSQSS SQTEIGSLNS
KGSLGKDTTS PMELAALEKI KSTWIKNQDD SLTETDTLEI TDQDMFGDAS TSLVVPEKVK
TPMKSSKTDL QGSASPSKVE GVHTPRQKRS TPLKERQLSK PLSERTNSSD SERSPDLGHS
TQIPRKVVYD QLNQILVSDA ALPENVILVN TTDWQGQYVA ELLQDQRKPV VCTCSTVEVQ
AVLSALLTRI QRYCNCNSSM PRPVKVAAVG GQSYLSSILR FFVKSLANKT SDWLGYMRFL
IIPLGSHPVA KYLGSVDSKY SSSFLDSGWR DLFSRSEPPV SEQLDVAGRV MQYVNGAATT
HQLPVAEAML TCRHKFPDED SYQKFIPFIG VVKVGLVEDS PSTAGDGDDS PVVSLTVPST
SPPSSSGLSR DATATPPSSP SMSSALAIVG SPNSPYGDVI GLQVDYWLGH PGERRREGDK
RDASSKNTLK SVFRSVQVSR LPHSGEAQLS GTMAMTVVTK EKNKKVPTIF LSKKPREKEV
DSKSQVIEGI SRLICSAKQQ QTMLRVSIDG VEWSDIKFFQ LAAQWPTHVK HFPVGLFSGS
KAT
