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 24-JAN-2024, entry version 170. 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 INTERACTION WITH WDR37. RX PubMed=34642815; DOI=10.1007/s00439-021-02384-y; RA Sorokina E.A., Reis L.M., Thompson S., Agre K., Babovic-Vuksanovic D., RA Ellingson M.S., Hasadsri L., van Bever Y., Semina E.V.; RT "WDR37 syndrome: identification of a distinct new cluster of disease- RT associated variants and functional analyses of mutant proteins."; RL Hum. Genet. 140:1775-1789(2021). RN [24] 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. Required for normal ER Ca2+ handling in lymphocytes. CC Together with WDR37, it plays an essential role in lymphocyte CC development, quiescence and survival. Required for stabilizing CC peripheral lymphocyte populations (By similarity). CC {ECO:0000250|UniProtKB:Q8K212, ECO:0000269|PubMed:11331585, CC 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). Interacts with WDR37 (PubMed:34642815). CC {ECO:0000250|UniProtKB:Q8K212, ECO:0000269|PubMed:11331585, CC ECO:0000269|PubMed:15692563, ECO:0000269|PubMed:16308564, CC ECO:0000269|PubMed:17646382, ECO:0000269|PubMed:17855360, CC ECO:0000269|PubMed:34642815}. 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}; 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; 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; 46. DR CORUM; Q6VY07; -. DR IntAct; Q6VY07; 25. DR MINT; Q6VY07; -. DR STRING; 9606.ENSP00000316454; -. DR GlyCosmos; Q6VY07; 3 sites, 1 glycan. 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; 9606-ENSP00000316454; -. DR PeptideAtlas; Q6VY07; -. DR ProteomicsDB; 67734; -. [Q6VY07-1] DR ProteomicsDB; 67735; -. [Q6VY07-2] DR Pumba; Q6VY07; -. DR ABCD; Q6VY07; 12 sequenced antibodies. DR Antibodypedia; 44366; 105 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 AGR; HGNC:30032; -. 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; CKHKTRE; -. DR OrthoDB; 2878701at2759; -. 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; 29 hits in 1155 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 179 other cell types or tissues. DR ExpressionAtlas; Q6VY07; baseline and differential. 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:0002260; P:lymphocyte homeostasis; ISS:UniProtKB. 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; PHOSPHOFURIN ACIDIC CLUSTER SORTING PROTEIN; 1. DR PANTHER; PTHR13280:SF16; PHOSPHOFURIN ACIDIC CLUSTER SORTING PROTEIN 1; 1. DR Pfam; PF10254; Pacs-1; 1. DR SUPFAM; SSF81995; beta-sandwich domain of Sec23/24; 1. DR Genevisible; Q6VY07; HS. 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 //