AUXI_HUMAN
ID AUXI_HUMAN Reviewed; 913 AA.
AC O75061; B7Z3V8; D3DQ65; D3DQ66; Q32M66; Q4G0K1; Q5T614; Q5T615;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 3.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Putative tyrosine-protein phosphatase auxilin {ECO:0000305};
DE EC=3.1.3.48;
DE AltName: Full=DnaJ homolog subfamily C member 6 {ECO:0000312|HGNC:HGNC:15469};
GN Name=DNAJC6 {ECO:0000312|HGNC:HGNC:15469};
GN Synonyms=KIAA0473 {ECO:0000312|EMBL:BAA32318.2};
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9455484; DOI=10.1093/dnares/4.5.345;
RA Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D.,
RA Nomura N., Ohara O.;
RT "Characterization of cDNA clones in size-fractionated cDNA libraries from
RT human brain.";
RL DNA Res. 4:345-349(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Thalamus;
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].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Brain;
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-563 AND SER-570, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [7]
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 [8]
RP INVOLVEMENT IN PARK19A.
RX PubMed=22563501; DOI=10.1371/journal.pone.0036458;
RA Edvardson S., Cinnamon Y., Ta-Shma A., Shaag A., Yim Y.I., Zenvirt S.,
RA Jalas C., Lesage S., Brice A., Taraboulos A., Kaestner K.H., Greene L.E.,
RA Elpeleg O.;
RT "A deleterious mutation in DNAJC6 encoding the neuronal-specific clathrin-
RT uncoating co-chaperone auxilin, is associated with juvenile parkinsonism.";
RL PLoS ONE 7:E36458-E36458(2012).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 (ISOFORMS 3 AND 4), AND
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112 AND SER-570, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [11]
RP TISSUE SPECIFICITY, AND INVOLVEMENT IN PARK19A.
RX PubMed=23211418; DOI=10.1016/j.parkreldis.2012.11.006;
RA Koroglu C., Baysal L., Cetinkaya M., Karasoy H., Tolun A.;
RT "DNAJC6 is responsible for juvenile parkinsonism with phenotypic
RT variability.";
RL Parkinsonism Relat. Disord. 19:320-324(2013).
RN [12]
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 [13]
RP INVOLVEMENT IN PARK19B, VARIANT PARK19B GLY-870, VARIANTS LEU-76; PRO-152;
RP VAL-264; SER-441 AND CYS-562, AND CHARACTERIZATION OF VARIANT PARK19B
RP GLY-870.
RX PubMed=26528954; DOI=10.1002/ana.24553;
RG International Parkinsonism Genetics Network;
RA Olgiati S., Quadri M., Fang M., Rood J.P., Saute J.A., Chien H.F.,
RA Bouwkamp C.G., Graafland J., Minneboo M., Breedveld G.J., Zhang J.,
RA Verheijen F.W., Boon A.J., Kievit A.J., Jardim L.B., Mandemakers W.,
RA Barbosa E.R., Rieder C.R., Leenders K.L., Wang J., Bonifati V.;
RT "DNAJC6 mutations associated with early-onset Parkinson's disease.";
RL Ann. Neurol. 79:244-256(2016).
RN [14]
RP INVOLVEMENT IN PARK19A.
RX PubMed=26703368; DOI=10.1002/ana.24591;
RA Elsayed L.E., Drouet V., Usenko T., Mohammed I.N., Hamed A.A., Elseed M.A.,
RA Salih M.A., Koko M.E., Mohamed A.Y., Siddig R.A., Elbashir M.I.,
RA Ibrahim M.E., Durr A., Stevanin G., Lesage S., Ahmed A.E., Brice A.;
RT "A novel nonsense mutation in DNAJC6 expands the phenotype of autosomal-
RT recessive juvenile-onset Parkinson's disease.";
RL Ann. Neurol. 79:335-337(2016).
CC -!- FUNCTION: Recruits HSPA8/HSC70 to clathrin-coated vesicles and promotes
CC uncoating of clathrin-coated vesicles. Plays a role in clathrin-
CC mediated endocytosis in neurons (By similarity).
CC {ECO:0000250|UniProtKB:Q80TZ3}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48;
CC -!- SUBUNIT: Interacts with HSPA8/HSC70. Interacts with CLTC. Interacts
CC with AP2A2 (By similarity). {ECO:0000250|UniProtKB:Q27974}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=O75061-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75061-2; Sequence=VSP_019580;
CC Name=3;
CC IsoId=O75061-3; Sequence=VSP_019579, VSP_019581;
CC Name=4;
CC IsoId=O75061-4; Sequence=VSP_019579;
CC -!- TISSUE SPECIFICITY: Expressed in various brain regions, including
CC cerebellum, corpus callosum, cortex, striatum, brainstem, pons,
CC putamen, spinal cord and substantia nigra. Very low expression in non-
CC neural tissues such as leukocytes, liver, adipose tissue, skeletal
CC muscle and bone marrow. {ECO:0000269|PubMed:23211418}.
CC -!- DISEASE: Parkinson disease 19A, juvenile-onset (PARK19A) [MIM:615528]:
CC A juvenile form of Parkinson disease, a complex neurodegenerative
CC disorder characterized by bradykinesia, resting tremor, muscular
CC rigidity and postural instability, as well as by a clinically
CC significant response to treatment with levodopa. The pathology involves
CC the loss of dopaminergic neurons in the substantia nigra and the
CC presence of Lewy bodies (intraneuronal accumulations of aggregated
CC proteins), in surviving neurons in various areas of the brain. PARK19A
CC is characterized by onset of parkinsonian symptoms in the first or
CC second decade of life. Some patients may have additional neurologic
CC features, including intellectual disability and seizures.
CC {ECO:0000269|PubMed:22563501, ECO:0000269|PubMed:23211418,
CC ECO:0000269|PubMed:26703368}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Parkinson disease 19B, early-onset (PARK19B) [MIM:615528]: An
CC early-onset form of Parkinson disease, a complex neurodegenerative
CC disorder characterized by bradykinesia, resting tremor, muscular
CC rigidity and postural instability, as well as by a clinically
CC significant response to treatment with levodopa. The pathology involves
CC the loss of dopaminergic neurons in the substantia nigra and the
CC presence of Lewy bodies (intraneuronal accumulations of aggregated
CC proteins), in surviving neurons in various areas of the brain. PARK19B
CC is characterized by symptoms onset in the third-to-fifth decade, slow
CC disease progression, and prominent. response to dopaminergic therapies.
CC Inheritance is autosomal recessive. {ECO:0000269|PubMed:26528954}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA32318.2; Type=Erroneous initiation; Note=Extended 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; AB007942; BAA32318.2; ALT_INIT; mRNA.
DR EMBL; AK296408; BAH12344.1; -; mRNA.
DR EMBL; AC119800; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL139294; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL355487; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL356212; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX06533.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX06534.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX06536.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX06537.1; -; Genomic_DNA.
DR EMBL; BC051722; AAH51722.1; -; mRNA.
DR EMBL; BC109279; AAI09280.2; -; mRNA.
DR EMBL; BC109280; AAI09281.2; -; mRNA.
DR CCDS; CCDS30739.1; -. [O75061-1]
DR CCDS; CCDS58004.1; -. [O75061-2]
DR CCDS; CCDS58005.1; -. [O75061-4]
DR RefSeq; NP_001243793.1; NM_001256864.1. [O75061-2]
DR RefSeq; NP_001243794.1; NM_001256865.1. [O75061-4]
DR RefSeq; NP_055602.1; NM_014787.3. [O75061-1]
DR AlphaFoldDB; O75061; -.
DR BMRB; O75061; -.
DR SMR; O75061; -.
DR BioGRID; 115167; 62.
DR IntAct; O75061; 9.
DR MINT; O75061; -.
DR STRING; 9606.ENSP00000360108; -.
DR DEPOD; DNAJC6; -.
DR iPTMnet; O75061; -.
DR PhosphoSitePlus; O75061; -.
DR BioMuta; DNAJC6; -.
DR EPD; O75061; -.
DR jPOST; O75061; -.
DR MassIVE; O75061; -.
DR MaxQB; O75061; -.
DR PaxDb; O75061; -.
DR PeptideAtlas; O75061; -.
DR PRIDE; O75061; -.
DR ProteomicsDB; 12747; -.
DR ProteomicsDB; 49731; -. [O75061-1]
DR ProteomicsDB; 49732; -. [O75061-2]
DR ProteomicsDB; 49733; -. [O75061-3]
DR Antibodypedia; 33368; 134 antibodies from 26 providers.
DR DNASU; 9829; -.
DR Ensembl; ENST00000263441.11; ENSP00000263441.7; ENSG00000116675.16. [O75061-4]
DR Ensembl; ENST00000371069.5; ENSP00000360108.4; ENSG00000116675.16. [O75061-2]
DR Ensembl; ENST00000395325.7; ENSP00000378735.3; ENSG00000116675.16. [O75061-1]
DR GeneID; 9829; -.
DR KEGG; hsa:9829; -.
DR MANE-Select; ENST00000371069.5; ENSP00000360108.4; NM_001256864.2; NP_001243793.1. [O75061-2]
DR UCSC; uc001dcd.3; human. [O75061-1]
DR CTD; 9829; -.
DR DisGeNET; 9829; -.
DR GeneCards; DNAJC6; -.
DR GeneReviews; DNAJC6; -.
DR HGNC; HGNC:15469; DNAJC6.
DR HPA; ENSG00000116675; Group enriched (brain, retina).
DR MalaCards; DNAJC6; -.
DR MIM; 608375; gene.
DR MIM; 615528; phenotype.
DR neXtProt; NX_O75061; -.
DR OpenTargets; ENSG00000116675; -.
DR Orphanet; 391411; Atypical juvenile parkinsonism.
DR Orphanet; 2828; Young-onset Parkinson disease.
DR PharmGKB; PA27423; -.
DR VEuPathDB; HostDB:ENSG00000116675; -.
DR eggNOG; KOG0431; Eukaryota.
DR eggNOG; KOG2283; Eukaryota.
DR GeneTree; ENSGT00940000158755; -.
DR HOGENOM; CLU_007537_1_0_1; -.
DR InParanoid; O75061; -.
DR OMA; WHTKPGS; -.
DR OrthoDB; 826336at2759; -.
DR PhylomeDB; O75061; -.
DR TreeFam; TF105165; -.
DR PathwayCommons; O75061; -.
DR Reactome; R-HSA-432720; Lysosome Vesicle Biogenesis.
DR Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis.
DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR SignaLink; O75061; -.
DR SIGNOR; O75061; -.
DR BioGRID-ORCS; 9829; 10 hits in 1073 CRISPR screens.
DR ChiTaRS; DNAJC6; human.
DR GeneWiki; Auxilin; -.
DR GenomeRNAi; 9829; -.
DR Pharos; O75061; Tbio.
DR PRO; PR:O75061; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O75061; protein.
DR Bgee; ENSG00000116675; Expressed in endothelial cell and 152 other tissues.
DR ExpressionAtlas; O75061; baseline and differential.
DR Genevisible; O75061; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; IBA:GO_Central.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0031982; C:vesicle; IBA:GO_Central.
DR GO; GO:0030276; F:clathrin binding; IBA:GO_Central.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0072318; P:clathrin coat disassembly; IBA:GO_Central.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IBA:GO_Central.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR GO; GO:2000369; P:regulation of clathrin-dependent endocytosis; IEA:Ensembl.
DR GO; GO:0016191; P:synaptic vesicle uncoating; ISS:BHF-UCL.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR036869; J_dom_sf.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR014020; Tensin_C2-dom.
DR InterPro; IPR029023; Tensin_phosphatase.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF10409; PTEN_C2; 1.
DR SMART; SM00271; DnaJ; 1.
DR SMART; SM01326; PTEN_C2; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS51182; C2_TENSIN; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS51181; PPASE_TENSIN; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Chaperone; Disease variant; Hydrolase;
KW Neurodegeneration; Parkinson disease; Parkinsonism; Phosphoprotein;
KW Protein phosphatase; Reference proteome; Repeat; SH3-binding.
FT CHAIN 1..913
FT /note="Putative tyrosine-protein phosphatase auxilin"
FT /id="PRO_0000244516"
FT REPEAT 36..39
FT /note="1"
FT REPEAT 40..43
FT /note="2"
FT REPEAT 44..47
FT /note="3"
FT DOMAIN 55..222
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00590"
FT DOMAIN 228..366
FT /note="C2 tensin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00589"
FT DOMAIN 849..913
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT REGION 36..47
FT /note="3 X 4 AA approximate tandem repeats"
FT REGION 451..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 409..417
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
FT COMPBIAS 453..469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..574
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..632
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..696
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..770
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 164
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00590"
FT MOD_RES 112
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 453
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80TZ3"
FT MOD_RES 456
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80TZ3"
FT MOD_RES 563
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 570
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..13
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_019579"
FT VAR_SEQ 1..7
FT /note="MKDSENK -> MSLLGSYRKKTSNDGYESLQLVDSNGDLSAGSGGVGGKQRV
FT NAGAAARSPARQPPDRASTMDSS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019580"
FT VAR_SEQ 456..913
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019581"
FT VARIANT 76
FT /note="M -> L (in dbSNP:rs61757223)"
FT /evidence="ECO:0000269|PubMed:26528954"
FT /id="VAR_077924"
FT VARIANT 152
FT /note="L -> P"
FT /evidence="ECO:0000269|PubMed:26528954"
FT /id="VAR_077925"
FT VARIANT 264
FT /note="I -> V"
FT /evidence="ECO:0000269|PubMed:26528954"
FT /id="VAR_077926"
FT VARIANT 441
FT /note="C -> S (in dbSNP:rs145329294)"
FT /evidence="ECO:0000269|PubMed:26528954"
FT /id="VAR_077927"
FT VARIANT 562
FT /note="R -> C (in dbSNP:rs770127313)"
FT /evidence="ECO:0000269|PubMed:26528954"
FT /id="VAR_077928"
FT VARIANT 671
FT /note="S -> N (in dbSNP:rs4915691)"
FT /id="VAR_026908"
FT VARIANT 870
FT /note="R -> G (in PARK19B; patient fibroblasts show
FT decreased levels of the protein; dbSNP:rs879255630)"
FT /evidence="ECO:0000269|PubMed:26528954"
FT /id="VAR_077929"
FT CONFLICT 178
FT /note="M -> V (in Ref. 2; BAH12344)"
FT /evidence="ECO:0000305"
FT CONFLICT 425
FT /note="F -> S (in Ref. 5; AAH51722)"
FT /evidence="ECO:0000305"
FT MOD_RES O75061-3:1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES O75061-4:1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
SQ SEQUENCE 913 AA; 99997 MW; 7B7187AAC8ADF2E4 CRC64;
MKDSENKGAS SPDMEPSYGG GLFDMVKGGA GRLFSNLKDN LKDTLKDTSS RVIQSVTSYT
KGDLDFTYVT SRIIVMSFPL DNVDIGFRNQ VDDIRSFLDS RHLDHYTVYN LSPKSYRTAK
FHSRVSECSW PIRQAPSLHN LFAVCRNMYN WLLQNPKNVC VVHCLDGRAA SSILVGAMFI
FCNLYSTPGP AIRLLYAKRP GIGLSPSHRR YLGYMCDLLA DKPYRPHFKP LTIKSITVSP
IPFFNKQRNG CRPYCDVLIG ETKIYSTCTD FERMKEYRVQ DGKIFIPLNI TVQGDVVVSM
YHLRSTIGSR LQAKVTNTQI FQLQFHTGFI PLDTTVLKFT KPELDACDVP EKYPQLFQVT
LDVELQPHDK VIDLTPPWEH YCTKDVNPSI LFSSHQEHQD TLALGGQAPI DIPPDNPRHY
GQSGFFASLC WQDQKSEKSF CEEDHAALVN QESEQSDDEL LTLSSPHGNA NGDKPHGVKK
PSKKQQEPAA PPPPEDVDLL GLEGSAMSNS FSPPAAPPTN SELLSDLFGG GGAAGPTQAG
QSGVEDVFHP SGPASTQSTP RRSATSTSAS PTLRVGEGAT FDPFGAPSKP SGQDLLGSFL
NTSSASSDPF LQPTRSPSPT VHASSTPAVN IQPDVSGGWD WHAKPGGFGM GSKSAATSPT
GSSHGTPTHQ SKPQTLDPFA DLGTLGSSSF ASKPTTPTGL GGGFPPLSSP QKASPQPMGG
GWQQGGAYNW QQPQPKPQPS MPHSSPQNRP NYNVSFSAMP GGQNERGKGS SNLEGKQKAA
DFEDLLSGQG FNAHKDKKGP RTIAEMRKEE MAKEMDPEKL KILEWIEGKE RNIRALLSTM
HTVLWAGETK WKPVGMADLV TPEQVKKVYR KAVLVVHPDK ATGQPYEQYA KMIFMELNDA
WSEFENQGQK PLY
