AP4AT_HUMAN
ID AP4AT_HUMAN Reviewed; 525 AA.
AC Q96N21; Q6ZQU0; Q6ZSQ9;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=AP-4 complex accessory subunit Tepsin {ECO:0000305};
DE AltName: Full=ENTH domain-containing protein 2 {ECO:0000312|HGNC:HGNC:26458};
DE AltName: Full=Epsin for AP-4;
DE AltName: Full=Tetra-epsin {ECO:0000303|PubMed:22472443};
GN Name=TEPSIN {ECO:0000303|PubMed:22472443, ECO:0000312|HGNC:HGNC:26458};
GN Synonyms=C17orf56 {ECO:0000312|HGNC:HGNC:26458},
GN ENTHD2 {ECO:0000312|HGNC:HGNC:26458};
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] (ISOFORMS 1 AND 2).
RC TISSUE=Hippocampus, Teratocarcinoma, and Uterus;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333 AND SER-356, AND
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356, AND IDENTIFICATION BY
RP 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 [6]
RP FUNCTION, INTERACTION WITH AP4B1, SUBUNIT, SUBCELLULAR LOCATION, AND
RP TOPOLOGY.
RX PubMed=22472443; DOI=10.1083/jcb.201111049;
RA Borner G.H., Antrobus R., Hirst J., Bhumbra G.S., Kozik P., Jackson L.P.,
RA Sahlender D.A., Robinson M.S.;
RT "Multivariate proteomic profiling identifies novel accessory proteins of
RT coated vesicles.";
RL J. Cell Biol. 197:141-160(2012).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333 AND SER-356, 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 [8]
RP FUNCTION, INTERACTION WITH AP4B1 AND AP4E1, SUBCELLULAR LOCATION, REGION,
RP AND MUTAGENESIS OF ARG-467; ASP-468; SER-469; LEU-470; PHE-471; ALA-472;
RP GLY-473; MET-474; GLU-475; LEU-476; VAL-477; GLU-516; PRO-517; SER-518;
RP ALA-519; PHE-520; ALA-521; PHE-522; LEU-523; ASN-524 AND ALA-525.
RX PubMed=26542808; DOI=10.1074/jbc.m115.683409;
RA Mattera R., Guardia C.M., Sidhu S.S., Bonifacino J.S.;
RT "Bivalent motif-ear interactions mediate the association of the accessory
RT protein tepsin with the AP-4 adaptor complex.";
RL J. Biol. Chem. 290:30736-30749(2015).
RN [9]
RP INTERACTION WITH AP4B1, SUBCELLULAR LOCATION, TOPOLOGY, REGION, AND
RP MUTAGENESIS OF LEU-470; PHE-471; GLY-473; MET-474; LEU-476 AND VAL-477.
RX PubMed=26756312; DOI=10.1111/tra.12375;
RA Frazier M.N., Davies A.K., Voehler M., Kendall A.K., Borner G.H.,
RA Chazin W.J., Robinson M.S., Jackson L.P.;
RT "Molecular basis for the interaction between AP4 beta4 and its accessory
RT protein, tepsin.";
RL Traffic 17:400-415(2016).
CC -!- FUNCTION: Associates with the adapter-like complex 4 (AP-4) and may
CC therefore play a role in vesicular trafficking of proteins at the
CC trans-Golgi network. {ECO:0000305|PubMed:22472443,
CC ECO:0000305|PubMed:26542808}.
CC -!- SUBUNIT: Interacts with AP4B1 and AP4E1; the interaction is direct and
CC mediates the association of TEPSIN with the adapter-like complex 4 (AP-
CC 4), a heterotetramer composed of AP4B1, AP4E1, AP4M1 and AP4S1.
CC {ECO:0000269|PubMed:22472443, ECO:0000269|PubMed:26542808,
CC ECO:0000269|PubMed:26756312}.
CC -!- INTERACTION:
CC Q96N21; Q6ZMQ8: AATK; NbExp=3; IntAct=EBI-11139477, EBI-2008380;
CC Q96N21; Q8N6N7: ACBD7; NbExp=3; IntAct=EBI-11139477, EBI-18657673;
CC Q96N21; O00468-6: AGRN; NbExp=3; IntAct=EBI-11139477, EBI-17740588;
CC Q96N21; Q9BXS5: AP1M1; NbExp=3; IntAct=EBI-11139477, EBI-541426;
CC Q96N21; Q9Y6B7: AP4B1; NbExp=3; IntAct=EBI-11139477, EBI-1047606;
CC Q96N21; Q9BWW8: APOL6; NbExp=3; IntAct=EBI-11139477, EBI-11574440;
CC Q96N21; Q8TDY4: ASAP3; NbExp=3; IntAct=EBI-11139477, EBI-2609717;
CC Q96N21; Q9Y575-3: ASB3; NbExp=3; IntAct=EBI-11139477, EBI-14199987;
CC Q96N21; Q9BZR8: BCL2L14; NbExp=3; IntAct=EBI-11139477, EBI-1385773;
CC Q96N21; Q5TBC7: BCL2L15; NbExp=3; IntAct=EBI-11139477, EBI-10247136;
CC Q96N21; Q6PI77: BHLHB9; NbExp=3; IntAct=EBI-11139477, EBI-11519926;
CC Q96N21; Q96CA5: BIRC7; NbExp=3; IntAct=EBI-11139477, EBI-517623;
CC Q96N21; Q9NP55: BPIFA1; NbExp=3; IntAct=EBI-11139477, EBI-953896;
CC Q96N21; Q9Y2F9: BTBD3; NbExp=3; IntAct=EBI-11139477, EBI-311155;
CC Q96N21; Q9NX04: C1orf109; NbExp=3; IntAct=EBI-11139477, EBI-8643161;
CC Q96N21; Q9BXJ3: C1QTNF4; NbExp=3; IntAct=EBI-11139477, EBI-11955105;
CC Q96N21; Q9HC52: CBX8; NbExp=3; IntAct=EBI-11139477, EBI-712912;
CC Q96N21; Q8IYE0: CCDC146; NbExp=3; IntAct=EBI-11139477, EBI-10749669;
CC Q96N21; P24863: CCNC; NbExp=3; IntAct=EBI-11139477, EBI-395261;
CC Q96N21; Q9UJX2: CDC23; NbExp=3; IntAct=EBI-11139477, EBI-396137;
CC Q96N21; Q9BW66: CINP; NbExp=3; IntAct=EBI-11139477, EBI-739784;
CC Q96N21; P51800-3: CLCNKA; NbExp=3; IntAct=EBI-11139477, EBI-11980535;
CC Q96N21; O95833: CLIC3; NbExp=3; IntAct=EBI-11139477, EBI-10192241;
CC Q96N21; P26441: CNTF; NbExp=3; IntAct=EBI-11139477, EBI-1050897;
CC Q96N21; Q9UBL6-2: CPNE7; NbExp=3; IntAct=EBI-11139477, EBI-12012272;
CC Q96N21; P68400: CSNK2A1; NbExp=3; IntAct=EBI-11139477, EBI-347804;
CC Q96N21; P78358: CTAG1B; NbExp=3; IntAct=EBI-11139477, EBI-1188472;
CC Q96N21; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-11139477, EBI-3867333;
CC Q96N21; Q9H4E7: DEF6; NbExp=3; IntAct=EBI-11139477, EBI-745369;
CC Q96N21; Q68J44: DUSP29; NbExp=3; IntAct=EBI-11139477, EBI-1054321;
CC Q96N21; Q13115: DUSP4; NbExp=3; IntAct=EBI-11139477, EBI-6591081;
CC Q96N21; Q8IYY4: DZIP1L; NbExp=3; IntAct=EBI-11139477, EBI-10264440;
CC Q96N21; Q8N9N8: EIF1AD; NbExp=3; IntAct=EBI-11139477, EBI-750700;
CC Q96N21; Q7L5A3: FAM214B; NbExp=3; IntAct=EBI-11139477, EBI-745689;
CC Q96N21; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-11139477, EBI-6658203;
CC Q96N21; O95363: FARS2; NbExp=3; IntAct=EBI-11139477, EBI-2513774;
CC Q96N21; O75344: FKBP6; NbExp=3; IntAct=EBI-11139477, EBI-744771;
CC Q96N21; Q96Q35-2: FLACC1; NbExp=3; IntAct=EBI-11139477, EBI-11533409;
CC Q96N21; Q53EP0-3: FNDC3B; NbExp=3; IntAct=EBI-11139477, EBI-10242151;
CC Q96N21; Q9P2W3: GNG13; NbExp=3; IntAct=EBI-11139477, EBI-11427343;
CC Q96N21; Q08379: GOLGA2; NbExp=3; IntAct=EBI-11139477, EBI-618309;
CC Q96N21; O95872: GPANK1; NbExp=3; IntAct=EBI-11139477, EBI-751540;
CC Q96N21; Q13322-4: GRB10; NbExp=3; IntAct=EBI-11139477, EBI-12353035;
CC Q96N21; Q4V328: GRIPAP1; NbExp=3; IntAct=EBI-11139477, EBI-717919;
CC Q96N21; Q96NT3-2: GUCD1; NbExp=3; IntAct=EBI-11139477, EBI-11978177;
CC Q96N21; O14929: HAT1; NbExp=3; IntAct=EBI-11139477, EBI-2339359;
CC Q96N21; P08631-2: HCK; NbExp=3; IntAct=EBI-11139477, EBI-9834454;
CC Q96N21; P84074: HPCA; NbExp=3; IntAct=EBI-11139477, EBI-12197079;
CC Q96N21; O75031: HSF2BP; NbExp=3; IntAct=EBI-11139477, EBI-7116203;
CC Q96N21; Q9UBY9: HSPB7; NbExp=3; IntAct=EBI-11139477, EBI-739361;
CC Q96N21; Q14005-2: IL16; NbExp=3; IntAct=EBI-11139477, EBI-17178971;
CC Q96N21; P46940: IQGAP1; NbExp=3; IntAct=EBI-11139477, EBI-297509;
CC Q96N21; Q8NC69: KCTD6; NbExp=3; IntAct=EBI-11139477, EBI-2511344;
CC Q96N21; Q7L273: KCTD9; NbExp=3; IntAct=EBI-11139477, EBI-4397613;
CC Q96N21; O15037: KHNYN; NbExp=3; IntAct=EBI-11139477, EBI-6148525;
CC Q96N21; Q2WGJ6: KLHL38; NbExp=3; IntAct=EBI-11139477, EBI-6426443;
CC Q96N21; Q15323: KRT31; NbExp=3; IntAct=EBI-11139477, EBI-948001;
CC Q96N21; O76011: KRT34; NbExp=3; IntAct=EBI-11139477, EBI-1047093;
CC Q96N21; Q92764: KRT35; NbExp=3; IntAct=EBI-11139477, EBI-1058674;
CC Q96N21; Q3LI66: KRTAP6-2; NbExp=3; IntAct=EBI-11139477, EBI-11962084;
CC Q96N21; Q96BZ8: LENG1; NbExp=3; IntAct=EBI-11139477, EBI-726510;
CC Q96N21; Q8TCE9: LGALS14; NbExp=3; IntAct=EBI-11139477, EBI-10274069;
CC Q96N21; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-11139477, EBI-11742507;
CC Q96N21; P62310: LSM3; NbExp=3; IntAct=EBI-11139477, EBI-348239;
CC Q96N21; Q86SG7: LYG2; NbExp=3; IntAct=EBI-11139477, EBI-18312334;
CC Q96N21; Q9NZL9: MAT2B; NbExp=3; IntAct=EBI-11139477, EBI-10317491;
CC Q96N21; Q9BUE0: MED18; NbExp=3; IntAct=EBI-11139477, EBI-394640;
CC Q96N21; P55081: MFAP1; NbExp=3; IntAct=EBI-11139477, EBI-1048159;
CC Q96N21; Q9UH92-3: MLX; NbExp=3; IntAct=EBI-11139477, EBI-8852072;
CC Q96N21; Q9UBU8-2: MORF4L1; NbExp=3; IntAct=EBI-11139477, EBI-10288852;
CC Q96N21; A6NI15: MSGN1; NbExp=3; IntAct=EBI-11139477, EBI-11991020;
CC Q96N21; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-11139477, EBI-11522433;
CC Q96N21; Q9UHB4: NDOR1; NbExp=3; IntAct=EBI-11139477, EBI-10249760;
CC Q96N21; Q9HC98-4: NEK6; NbExp=3; IntAct=EBI-11139477, EBI-11750983;
CC Q96N21; Q9NPG2: NGB; NbExp=3; IntAct=EBI-11139477, EBI-10311409;
CC Q96N21; Q9Y5B8: NME7; NbExp=3; IntAct=EBI-11139477, EBI-744782;
CC Q96N21; Q86WQ0: NR2C2AP; NbExp=3; IntAct=EBI-11139477, EBI-10260040;
CC Q96N21; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-11139477, EBI-741158;
CC Q96N21; O95848: NUDT14; NbExp=3; IntAct=EBI-11139477, EBI-536866;
CC Q96N21; O43809: NUDT21; NbExp=3; IntAct=EBI-11139477, EBI-355720;
CC Q96N21; Q9UMX2-2: OAZ3; NbExp=3; IntAct=EBI-11139477, EBI-12049527;
CC Q96N21; O95007: OR6B1; NbExp=3; IntAct=EBI-11139477, EBI-12176191;
CC Q96N21; P55771: PAX9; NbExp=3; IntAct=EBI-11139477, EBI-12111000;
CC Q96N21; Q9Y5E6: PCDHB3; NbExp=3; IntAct=EBI-11139477, EBI-24224850;
CC Q96N21; Q9HB19: PLEKHA2; NbExp=3; IntAct=EBI-11139477, EBI-4401947;
CC Q96N21; P60900: PSMA6; NbExp=3; IntAct=EBI-11139477, EBI-357793;
CC Q96N21; Q96QF0-7: RAB3IP; NbExp=3; IntAct=EBI-11139477, EBI-11984839;
CC Q96N21; O75771: RAD51D; NbExp=3; IntAct=EBI-11139477, EBI-1055693;
CC Q96N21; Q8IUD6: RNF135; NbExp=3; IntAct=EBI-11139477, EBI-9916363;
CC Q96N21; Q9UDX3: SEC14L4; NbExp=3; IntAct=EBI-11139477, EBI-10320311;
CC Q96N21; O95391: SLU7; NbExp=3; IntAct=EBI-11139477, EBI-750559;
CC Q96N21; Q9BV90: SNRNP25; NbExp=3; IntAct=EBI-11139477, EBI-9675976;
CC Q96N21; O94875-10: SORBS2; NbExp=3; IntAct=EBI-11139477, EBI-12037893;
CC Q96N21; O60504: SORBS3; NbExp=3; IntAct=EBI-11139477, EBI-741237;
CC Q96N21; Q5T011-5: SZT2; NbExp=3; IntAct=EBI-11139477, EBI-10245139;
CC Q96N21; Q9BX59: TAPBPL; NbExp=3; IntAct=EBI-11139477, EBI-12017416;
CC Q96N21; Q9NVG8: TBC1D13; NbExp=3; IntAct=EBI-11139477, EBI-12264956;
CC Q96N21; Q9NU19: TBC1D22B; NbExp=3; IntAct=EBI-11139477, EBI-8787464;
CC Q96N21; Q15560: TCEA2; NbExp=3; IntAct=EBI-11139477, EBI-710310;
CC Q96N21; P56279: TCL1A; NbExp=3; IntAct=EBI-11139477, EBI-749995;
CC Q96N21; Q7Z6R9: TFAP2D; NbExp=3; IntAct=EBI-11139477, EBI-11952651;
CC Q96N21; Q92748: THRSP; NbExp=3; IntAct=EBI-11139477, EBI-1749955;
CC Q96N21; P0DI81-3: TRAPPC2; NbExp=3; IntAct=EBI-11139477, EBI-11961968;
CC Q96N21; O75865-2: TRAPPC6A; NbExp=3; IntAct=EBI-11139477, EBI-8451480;
CC Q96N21; P36406: TRIM23; NbExp=3; IntAct=EBI-11139477, EBI-740098;
CC Q96N21; Q9H8W5-2: TRIM45; NbExp=3; IntAct=EBI-11139477, EBI-11993364;
CC Q96N21; Q86XT4: TRIM50; NbExp=3; IntAct=EBI-11139477, EBI-9867283;
CC Q96N21; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-11139477, EBI-2130429;
CC Q96N21; Q6AZZ1: TRIM68; NbExp=3; IntAct=EBI-11139477, EBI-2130449;
CC Q96N21; Q8WW01: TSEN15; NbExp=3; IntAct=EBI-11139477, EBI-372432;
CC Q96N21; Q8NCE0: TSEN2; NbExp=3; IntAct=EBI-11139477, EBI-2559818;
CC Q96N21; Q63HK5: TSHZ3; NbExp=3; IntAct=EBI-11139477, EBI-9053916;
CC Q96N21; Q96PN8: TSSK3; NbExp=3; IntAct=EBI-11139477, EBI-3918381;
CC Q96N21; Q8TF42: UBASH3B; NbExp=3; IntAct=EBI-11139477, EBI-1380492;
CC Q96N21; Q9BRU9: UTP23; NbExp=3; IntAct=EBI-11139477, EBI-5457544;
CC Q96N21; O14972: VPS26C; NbExp=3; IntAct=EBI-11139477, EBI-7207091;
CC Q96N21; Q64LD2-2: WDR25; NbExp=3; IntAct=EBI-11139477, EBI-12032042;
CC Q96N21; Q15915: ZIC1; NbExp=3; IntAct=EBI-11139477, EBI-11963196;
CC Q96N21; Q9H0C1: ZMYND12; NbExp=3; IntAct=EBI-11139477, EBI-12030590;
CC Q96N21; Q6P1L6: ZNF343; NbExp=3; IntAct=EBI-11139477, EBI-10252492;
CC Q96N21; Q9UEG4: ZNF629; NbExp=3; IntAct=EBI-11139477, EBI-9977294;
CC Q96N21; Q15696: ZRSR2; NbExp=3; IntAct=EBI-11139477, EBI-6657923;
CC Q96N21; A0A384ME25; NbExp=3; IntAct=EBI-11139477, EBI-10211777;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000269|PubMed:26542808, ECO:0000269|PubMed:26756312}; Peripheral
CC membrane protein {ECO:0000269|PubMed:26756312}. Cytoplasmic vesicle
CC {ECO:0000269|PubMed:22472443}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:22472443}. Note=Extensively colocalizes with AP-4
CC which mediates the recruitment of TEPSIN to the trans-Golgi network.
CC {ECO:0000269|PubMed:22472443, ECO:0000269|PubMed:26542808}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96N21-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96N21-2; Sequence=VSP_025141, VSP_025142;
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DR EMBL; AK056090; BAB71091.1; -; mRNA.
DR EMBL; AK127221; BAC86888.1; -; mRNA.
DR EMBL; AK128728; BAC87593.1; -; mRNA.
DR EMBL; BC064483; AAH64483.1; -; mRNA.
DR CCDS; CCDS11779.1; -. [Q96N21-1]
DR RefSeq; NP_653280.1; NM_144679.2. [Q96N21-1]
DR RefSeq; XP_006721775.1; XM_006721712.2. [Q96N21-2]
DR PDB; 5WF9; X-ray; 1.80 A; A=1-153.
DR PDB; 5WFB; X-ray; 1.38 A; A/B=1-140.
DR PDBsum; 5WF9; -.
DR PDBsum; 5WFB; -.
DR AlphaFoldDB; Q96N21; -.
DR SMR; Q96N21; -.
DR BioGRID; 127002; 170.
DR IntAct; Q96N21; 153.
DR STRING; 9606.ENSP00000300714; -.
DR TCDB; 9.B.278.1.5; the organellar-targeting adaptor protein complex (o-apc) family.
DR GlyGen; Q96N21; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96N21; -.
DR PhosphoSitePlus; Q96N21; -.
DR BioMuta; TEPSIN; -.
DR DMDM; 74732479; -.
DR EPD; Q96N21; -.
DR jPOST; Q96N21; -.
DR MassIVE; Q96N21; -.
DR MaxQB; Q96N21; -.
DR PaxDb; Q96N21; -.
DR PeptideAtlas; Q96N21; -.
DR PRIDE; Q96N21; -.
DR ProteomicsDB; 77454; -. [Q96N21-1]
DR ProteomicsDB; 77455; -. [Q96N21-2]
DR Antibodypedia; 53274; 13 antibodies from 6 providers.
DR DNASU; 146705; -.
DR Ensembl; ENST00000300714.7; ENSP00000300714.3; ENSG00000167302.11. [Q96N21-1]
DR GeneID; 146705; -.
DR KEGG; hsa:146705; -.
DR UCSC; uc002jzu.2; human. [Q96N21-1]
DR CTD; 146705; -.
DR DisGeNET; 146705; -.
DR GeneCards; TEPSIN; -.
DR HGNC; HGNC:26458; TEPSIN.
DR HPA; ENSG00000167302; Low tissue specificity.
DR neXtProt; NX_Q96N21; -.
DR OpenTargets; ENSG00000167302; -.
DR PharmGKB; PA142672239; -.
DR VEuPathDB; HostDB:ENSG00000167302; -.
DR eggNOG; ENOG502QV38; Eukaryota.
DR GeneTree; ENSGT00390000015076; -.
DR HOGENOM; CLU_030958_0_0_1; -.
DR InParanoid; Q96N21; -.
DR OrthoDB; 693000at2759; -.
DR PhylomeDB; Q96N21; -.
DR TreeFam; TF331354; -.
DR PathwayCommons; Q96N21; -.
DR SignaLink; Q96N21; -.
DR BioGRID-ORCS; 146705; 102 hits in 1076 CRISPR screens.
DR ChiTaRS; TEPSIN; human.
DR GenomeRNAi; 146705; -.
DR Pharos; Q96N21; Tdark.
DR PRO; PR:Q96N21; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q96N21; protein.
DR Bgee; ENSG00000167302; Expressed in granulocyte and 143 other tissues.
DR ExpressionAtlas; Q96N21; baseline and differential.
DR Genevisible; Q96N21; HS.
DR GO; GO:0030662; C:coated vesicle membrane; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0031312; C:extrinsic component of organelle membrane; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0032588; C:trans-Golgi network membrane; IDA:UniProtKB.
DR CDD; cd03572; ENTH_like_Tepsin; 1.
DR DisProt; DP02404; -.
DR Gene3D; 1.25.40.90; -; 1.
DR InterPro; IPR013809; ENTH.
DR InterPro; IPR035802; ENTH/VHS_tepsin.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR039273; TEPSIN.
DR PANTHER; PTHR21514; PTHR21514; 2.
DR Pfam; PF01417; ENTH; 1.
DR SUPFAM; SSF48464; SSF48464; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Cytoplasmic vesicle;
KW Golgi apparatus; Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..525
FT /note="AP-4 complex accessory subunit Tepsin"
FT /id="PRO_0000286678"
FT DOMAIN 8..141
FT /note="ENTH"
FT REGION 139..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..477
FT /note="Interaction with AP4B1"
FT /evidence="ECO:0000269|PubMed:26542808,
FT ECO:0000269|PubMed:26756312"
FT REGION 487..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 515..525
FT /note="Interaction with AP4E1"
FT /evidence="ECO:0000269|PubMed:26542808"
FT COMPBIAS 148..163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..223
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..408
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..427
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..452
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..511
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 356
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..85
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_025141"
FT VAR_SEQ 86..175
FT /note="FFLLILKRNSAFIQEAAAFAGPPDPLHGNSLYQKVRAAAQDLGSTLFSDTVL
FT PLAPSQPLGTPPATGMGSQARPHSTLQGFGYSKEHGRT -> MGSQARPHSTLQGFGYS
FT KEHGRTGSAGEAFLSTIQKAAEVVASAMRPGPESPSTRRLLPRGDTYQPAMMPSASHGP
FT PTLGNLLPGAIPGPR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_025142"
FT MUTAGEN 467
FT /note="R->A: No effect on interaction with AP4B1 in vitro."
FT /evidence="ECO:0000269|PubMed:26542808"
FT MUTAGEN 468
FT /note="D->A: No effect on interaction with AP4B1 in vitro."
FT /evidence="ECO:0000269|PubMed:26542808"
FT MUTAGEN 469
FT /note="S->A,P: No effect on interaction with AP4B1 in
FT vitro."
FT /evidence="ECO:0000269|PubMed:26542808"
FT MUTAGEN 470
FT /note="L->A: Loss of interaction with AP4B1 n vitro."
FT /evidence="ECO:0000269|PubMed:26542808"
FT MUTAGEN 470
FT /note="L->S: Loss of interaction with AP4B1 in vitro; when
FT associated with S-471."
FT /evidence="ECO:0000269|PubMed:26756312"
FT MUTAGEN 471
FT /note="F->A: Loss of interaction with AP4B1 in vitro."
FT /evidence="ECO:0000269|PubMed:26542808"
FT MUTAGEN 471
FT /note="F->S: Loss of interaction with AP4B1 in vitro; when
FT associated with S-470."
FT /evidence="ECO:0000269|PubMed:26756312"
FT MUTAGEN 472
FT /note="A->D,P: No effect on interaction with AP4B1 in
FT vitro."
FT /evidence="ECO:0000269|PubMed:26542808"
FT MUTAGEN 473
FT /note="G->A: No effect on interaction with AP4B1 in vitro."
FT /evidence="ECO:0000269|PubMed:26542808"
FT MUTAGEN 473
FT /note="G->I: Loss of interaction with AP4B1 in vitro; when
FT associated with Q-474."
FT /evidence="ECO:0000269|PubMed:26756312"
FT MUTAGEN 474
FT /note="M->A: Decreased interaction with AP4B1 in vitro."
FT /evidence="ECO:0000269|PubMed:26542808"
FT MUTAGEN 474
FT /note="M->D: Decreased interaction with AP4B1 in vitro;
FT when associated with A-476."
FT /evidence="ECO:0000269|PubMed:26756312"
FT MUTAGEN 474
FT /note="M->Q: Loss of interaction with AP4B1 in vitro; when
FT associated with I-473."
FT /evidence="ECO:0000269|PubMed:26756312"
FT MUTAGEN 475
FT /note="E->A: No effect on interaction with AP4B1 in vitro."
FT /evidence="ECO:0000269|PubMed:26542808"
FT MUTAGEN 476
FT /note="L->A: No effect on interaction with AP4B1 in vitro.
FT Decreased interaction with AP4B1; when associated with D-
FT 474."
FT /evidence="ECO:0000269|PubMed:26542808,
FT ECO:0000269|PubMed:26756312"
FT MUTAGEN 476
FT /note="L->S: Decreased interaction with AP4B1 in vitro;
FT when associated with S-477."
FT /evidence="ECO:0000269|PubMed:26756312"
FT MUTAGEN 477
FT /note="V->A: No effect on interaction with AP4B1 in vitro."
FT /evidence="ECO:0000269|PubMed:26542808"
FT MUTAGEN 477
FT /note="V->S: Decreased interaction with AP4B1 in vitro;
FT when associated with S-476."
FT /evidence="ECO:0000269|PubMed:26756312"
FT MUTAGEN 516
FT /note="E->A: No effect on interaction with AP4E1 in vitro."
FT /evidence="ECO:0000269|PubMed:26542808"
FT MUTAGEN 517
FT /note="P->A: No effect on interaction with AP4E1 in vitro."
FT /evidence="ECO:0000269|PubMed:26542808"
FT MUTAGEN 518
FT /note="S->A: Loss of interaction with AP4E1 in vitro."
FT /evidence="ECO:0000269|PubMed:26542808"
FT MUTAGEN 519
FT /note="A->D: Loss of interaction with AP4E1 in vitro."
FT /evidence="ECO:0000269|PubMed:26542808"
FT MUTAGEN 520
FT /note="F->A: Loss of interaction with AP4E1 in vitro."
FT /evidence="ECO:0000269|PubMed:26542808"
FT MUTAGEN 521
FT /note="A->D: No effect on interaction with AP4E1 in vitro."
FT /evidence="ECO:0000269|PubMed:26542808"
FT MUTAGEN 522
FT /note="F->A: Loss of interaction with AP4E1 in vitro."
FT /evidence="ECO:0000269|PubMed:26542808"
FT MUTAGEN 523
FT /note="L->A: Loss of interaction with AP4E1 in vitro."
FT /evidence="ECO:0000269|PubMed:26542808"
FT MUTAGEN 524
FT /note="N->A: Decreased interaction with AP4E1 in vitro."
FT /evidence="ECO:0000269|PubMed:26542808"
FT MUTAGEN 525
FT /note="A->D: No effect on interaction with AP4E1 in vitro."
FT /evidence="ECO:0000269|PubMed:26542808"
FT HELIX 7..24
FT /evidence="ECO:0007829|PDB:5WFB"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:5WFB"
FT HELIX 35..45
FT /evidence="ECO:0007829|PDB:5WFB"
FT HELIX 47..63
FT /evidence="ECO:0007829|PDB:5WFB"
FT HELIX 66..82
FT /evidence="ECO:0007829|PDB:5WFB"
FT HELIX 85..93
FT /evidence="ECO:0007829|PDB:5WFB"
FT HELIX 95..102
FT /evidence="ECO:0007829|PDB:5WFB"
FT TURN 110..112
FT /evidence="ECO:0007829|PDB:5WFB"
FT HELIX 115..131
FT /evidence="ECO:0007829|PDB:5WFB"
FT CONFLICT Q96N21-2:22
FT /note="R -> H (in Ref. 1; BAC87593)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 525 AA; 55137 MW; B79970A37B801549 CRC64;
MAAAPPLRDR LSFLHRLPIL LKGTSDDDVP CPGYLFEEIA KISHESPGSS QCLLEYLLSR
LHSSSGHGKL KVLKILLYLC SHGSSFFLLI LKRNSAFIQE AAAFAGPPDP LHGNSLYQKV
RAAAQDLGST LFSDTVLPLA PSQPLGTPPA TGMGSQARPH STLQGFGYSK EHGRTAVRHQ
PGQAGGGWDE LDSGPSSQNS SQNSDLSRVS DSGSHSGSDS HSGASREPGD LAERVEVVAL
SDCQQELSLV RTVTRGPRAF LSREEAQHFI KACGLLNCEA VLQLLTCHLR GTSECTQLRA
LCAIASLGSS DLLPQEHILL RTRPWLQELS MGSPGPVTNK ATKILRHFEA SCGQLSPARG
TSAEPGPTAA LPGPSDLLTD AVPLPGSQVF LQPLSSTPVS SRSPAPSSGM PSSPVPTPPP
DASPIPAPGD PSEAEARLAE SRRWRPERIP GGTDSPKRGP SSCAWSRDSL FAGMELVACP
RLVGAGAAAG ESCPDAPRAP QTSSQRTAAK EPPGSEPSAF AFLNA
