ID PSA6_HUMAN Reviewed; 246 AA. AC P60900; B2R7J9; B4DQR4; B4DXJ9; P34062; Q6IB60; DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 13-APR-2004, sequence version 1. DT 27-MAR-2024, entry version 204. DE RecName: Full=Proteasome subunit alpha type-6; DE AltName: Full=27 kDa prosomal protein; DE Short=PROS-27; DE Short=p27K; DE AltName: Full=Macropain iota chain; DE AltName: Full=Multicatalytic endopeptidase complex iota chain; DE AltName: Full=Proteasome iota chain; GN Name=PSMA6; Synonyms=PROS27; 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). RX PubMed=7681138; DOI=10.1007/bf00282801; RA Bey F., Pereira I.S., Coux O., Viegas-Pequignot E., Targa F.R., RA Nothwang H.G., Dutrillaux B., Scherrer K.; RT "The prosomal RNA-binding protein p27K is a member of the alpha-type human RT prosomal gene family."; RL Mol. Gen. Genet. 237:193-205(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3). RC TISSUE=Cerebellum, and Testis; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12508121; DOI=10.1038/nature01348; RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., RA Waterston R., Hood L., Weissenbach J.; RT "The DNA sequence and analysis of human chromosome 14."; RL Nature 421:601-607(2003). RN [5] 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain, Lymph, Skeletal muscle, and Skin; 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 [7] RP PROTEIN SEQUENCE OF 12-43; 60-88; 105-116; 154-164; 172-181 AND 229-246, RP AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Fetal brain cortex; RA Lubec G., Chen W.-Q., Sun Y.; RL Submitted (DEC-2008) to UniProtKB. RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 26-246 (ISOFORM 1), AND PARTIAL PROTEIN RP SEQUENCE. RX PubMed=1888762; DOI=10.1016/0167-4838(91)90020-z; RA DeMartino G.N., Orth K., McCullough M.L., Lee L.W., Munn T.Z., Moomaw C.R., RA Dawson P.A., Slaughter C.A.; RT "The primary structures of four subunits of the human, high-molecular- RT weight proteinase, macropain (proteasome), are distinct but homologous."; RL Biochim. Biophys. Acta 1079:29-38(1991). RN [9] RP PARTIAL PROTEIN SEQUENCE. RX PubMed=7811265; DOI=10.1006/bbrc.1994.2876; RA Kristensen P., Johnsen A.H., Uerkvitz W., Tanaka K., Hendil K.B.; RT "Human proteasome subunits from 2-dimensional gels identified by partial RT sequencing."; RL Biochem. Biophys. Res. Commun. 205:1785-1789(1994). RN [10] RP FUNCTION IN ANTIGEN PRESENTATION. RX PubMed=8610016; DOI=10.1038/381166a0; RA Groettrup M., Soza A., Eggers M., Kuehn L., Dick T.P., Schild H., RA Rammensee H.G., Koszinowski U.H., Kloetzel P.M.; RT "A role for the proteasome regulator PA28alpha in antigen presentation."; RL Nature 381:166-168(1996). RN [11] RP SUBCELLULAR LOCATION. RX PubMed=12181345; DOI=10.1091/mbc.e02-03-0122; RA Lafarga M., Berciano M.T., Pena E., Mayo I., Castano J.G., Bohmann D., RA Rodrigues J.P., Tavanez J.P., Carmo-Fonseca M.; RT "Clastosome: a subtype of nuclear body enriched in 19S and 20S proteasomes, RT ubiquitin, and protein substrates of proteasome."; RL Mol. Biol. Cell 13:2771-2782(2002). RN [12] RP FUNCTION. RX PubMed=15244466; DOI=10.1021/bm049957a; RA Yano M., Koumoto Y., Kanesaki Y., Wu X., Kido H.; RT "20S proteasome prevents aggregation of heat-denatured proteins without RT PA700 regulatory subcomplex like a molecular chaperone."; RL Biomacromolecules 5:1465-1469(2004). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17323924; DOI=10.1021/bi061994u; RA Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.; RT "Mass spectrometric characterization of the affinity-purified human 26S RT proteasome complex."; RL Biochemistry 46:3553-3565(2007). RN [14] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-102 AND LYS-104, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [16] RP INTERACTION WITH ALKBH4. RX PubMed=23145062; DOI=10.1371/journal.pone.0049045; RA Bjornstad L.G., Meza T.J., Otterlei M., Olafsrud S.M., Meza-Zepeda L.A., RA Falnes P.O.; RT "Human ALKBH4 interacts with proteins associated with transcription."; RL PLoS ONE 7:E49045-E49045(2012). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-63 AND SER-64, 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 [18] 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 [19] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=27176742; DOI=10.1515/hsz-2016-0176; RA Rut W., Drag M.; RT "Human 20S proteasome activity towards fluorogenic peptides of various RT chain lengths."; RL Biol. Chem. 397:921-926(2016). RN [20] RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), AND SUBUNIT. RX PubMed=26133119; DOI=10.1038/ncomms8573; RA da Fonseca P.C., Morris E.P.; RT "Cryo-EM reveals the conformation of a substrate analogue in the human 20S RT proteasome core."; RL Nat. Commun. 6:7573-7573(2015). RN [21] RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 2-245, AND SUBUNIT. RX PubMed=25599644; DOI=10.1016/j.str.2014.11.017; RA Harshbarger W., Miller C., Diedrich C., Sacchettini J.; RT "Crystal structure of the human 20S proteasome in complex with RT carfilzomib."; RL Structure 23:418-424(2015). RN [22] RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), AND SUBUNIT. RX PubMed=27428775; DOI=10.1038/nsmb.3273; RA Huang X., Luan B., Wu J., Shi Y.; RT "An atomic structure of the human 26S proteasome."; RL Nat. Struct. Mol. Biol. 23:778-785(2016). RN [23] RP STRUCTURE BY ELECTRON MICROSCOPY (4.02 ANGSTROMS), AND SUBUNIT. RX PubMed=27342858; DOI=10.1073/pnas.1608050113; RA Schweitzer A., Aufderheide A., Rudack T., Beck F., Pfeifer G., RA Plitzko J.M., Sakata E., Schulten K., Foerster F., Baumeister W.; RT "Structure of the human 26S proteasome at a resolution of 3.9 Aa."; RL Proc. Natl. Acad. Sci. U.S.A. 113:7816-7821(2016). RN [24] RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS), AND SUBUNIT. RX PubMed=27493187; DOI=10.1126/science.aaf8993; RA Schrader J., Henneberg F., Mata R.A., Tittmann K., Schneider T.R., RA Stark H., Bourenkov G., Chari A.; RT "The inhibition mechanism of human 20S proteasomes enables next-generation RT inhibitor design."; RL Science 353:594-598(2016). RN [25] RP STRUCTURE BY ELECTRON MICROSCOPY (2.80 ANGSTROMS) IN COMPLEX WITH AKIRIN2, RP SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=34711951; DOI=10.1038/s41586-021-04035-8; RA de Almeida M., Hinterndorfer M., Brunner H., Grishkovskaya I., Singh K., RA Schleiffer A., Jude J., Deswal S., Kalis R., Vunjak M., Lendl T., Imre R., RA Roitinger E., Neumann T., Kandolf S., Schutzbier M., Mechtler K., RA Versteeg G.A., Haselbach D., Zuber J.; RT "AKIRIN2 controls the nuclear import of proteasomes in vertebrates."; RL Nature 599:491-496(2021). CC -!- FUNCTION: Component of the 20S core proteasome complex involved in the CC proteolytic degradation of most intracellular proteins. This complex CC plays numerous essential roles within the cell by associating with CC different regulatory particles. Associated with two 19S regulatory CC particles, forms the 26S proteasome and thus participates in the ATP- CC dependent degradation of ubiquitinated proteins. The 26S proteasome CC plays a key role in the maintenance of protein homeostasis by removing CC misfolded or damaged proteins that could impair cellular functions, and CC by removing proteins whose functions are no longer required. Associated CC with the PA200 or PA28, the 20S proteasome mediates ubiquitin- CC independent protein degradation. This type of proteolysis is required CC in several pathways including spermatogenesis (20S-PA200 complex) or CC generation of a subset of MHC class I-presented antigenic peptides CC (20S-PA28 complex). {ECO:0000269|PubMed:15244466, CC ECO:0000269|PubMed:27176742, ECO:0000269|PubMed:8610016}. CC -!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two CC 19S regulatory subunits (PubMed:25599644, PubMed:26133119, CC PubMed:27342858, PubMed:27428775, PubMed:27493187, PubMed:34711951). CC The 20S proteasome core is a barrel-shaped complex made of 28 subunits CC that are arranged in four stacked rings (PubMed:25599644, CC PubMed:26133119, PubMed:27342858, PubMed:27428775, PubMed:27493187, CC PubMed:34711951). The two outer rings are each formed by seven alpha CC subunits, and the two inner rings are formed by seven beta subunits CC (PubMed:25599644, PubMed:26133119, PubMed:27342858, PubMed:27428775, CC PubMed:27493187, PubMed:34711951). The proteolytic activity is exerted CC by three beta-subunits PSMB5, PSMB6 and PSMB7 (PubMed:25599644, CC PubMed:26133119, PubMed:27342858, PubMed:27428775, PubMed:27493187, CC PubMed:34711951). Interacts with ALKBH4 (PubMed:23145062). CC {ECO:0000269|PubMed:23145062, ECO:0000269|PubMed:25599644, CC ECO:0000269|PubMed:26133119, ECO:0000269|PubMed:27342858, CC ECO:0000269|PubMed:27428775, ECO:0000269|PubMed:27493187, CC ECO:0000269|PubMed:34711951}. CC -!- INTERACTION: CC P60900; Q0VDD7: BRME1; NbExp=3; IntAct=EBI-357793, EBI-741210; CC P60900; Q8N9M1-2: C19orf47; NbExp=3; IntAct=EBI-357793, EBI-10979594; CC P60900; Q9BY67: CADM1; NbExp=3; IntAct=EBI-357793, EBI-5652260; CC P60900; P84090: ERH; NbExp=3; IntAct=EBI-357793, EBI-711389; CC P60900; P42858: HTT; NbExp=4; IntAct=EBI-357793, EBI-466029; CC P60900; Q9BYR5: KRTAP4-2; NbExp=3; IntAct=EBI-357793, EBI-10172511; CC P60900; Q9BT23: LIMD2; NbExp=3; IntAct=EBI-357793, EBI-2805292; CC P60900; P62875: POLR2L; NbExp=3; IntAct=EBI-357793, EBI-359527; CC P60900; P25787: PSMA2; NbExp=6; IntAct=EBI-357793, EBI-603262; CC P60900; P25788: PSMA3; NbExp=10; IntAct=EBI-357793, EBI-348380; CC P60900; P25789: PSMA4; NbExp=5; IntAct=EBI-357793, EBI-359310; CC P60900; O14818: PSMA7; NbExp=11; IntAct=EBI-357793, EBI-603272; CC P60900; O43242: PSMD3; NbExp=3; IntAct=EBI-357793, EBI-357622; CC P60900; Q96K19: RNF170; NbExp=3; IntAct=EBI-357793, EBI-2130336; CC P60900; Q14D33: RTP5; NbExp=3; IntAct=EBI-357793, EBI-10217913; CC P60900; A2RU48: SMCO3; NbExp=3; IntAct=EBI-357793, EBI-10173195; CC P60900; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-357793, EBI-11139477; CC P60900; Q9HCM9: TRIM39; NbExp=3; IntAct=EBI-357793, EBI-739510; CC P60900; Q9HCM9-2: TRIM39; NbExp=5; IntAct=EBI-357793, EBI-11523450; CC P60900; Q6FI91: TSPYL; NbExp=3; IntAct=EBI-357793, EBI-723389; CC P60900; Q9Y5K5: UCHL5; NbExp=4; IntAct=EBI-357793, EBI-1051183; CC P60900; Q8NCP5: ZBTB44; NbExp=3; IntAct=EBI-357793, EBI-5658292; CC P60900; Q969J2: ZKSCAN4; NbExp=3; IntAct=EBI-357793, EBI-2818641; CC P60900; Q8TC21: ZNF596; NbExp=3; IntAct=EBI-357793, EBI-3923453; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9QUM9, CC ECO:0000269|PubMed:12181345}. Nucleus {ECO:0000269|PubMed:12181345, CC ECO:0000269|PubMed:34711951}. Note=Translocated from the cytoplasm into CC the nucleus following interaction with AKIRIN2, which bridges the CC proteasome with the nuclear import receptor IPO9 (PubMed:34711951). CC Colocalizes with TRIM5 in cytoplasmic bodies (By similarity). CC {ECO:0000250|UniProtKB:Q9QUM9, ECO:0000269|PubMed:34711951}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=P60900-1; Sequence=Displayed; CC Name=2; CC IsoId=P60900-2; Sequence=VSP_054587; CC Name=3; CC IsoId=P60900-3; Sequence=VSP_054586; CC -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000255|PROSITE- CC ProRule:PRU00808}. 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; X59417; CAA42052.1; -; mRNA. DR EMBL; CR456944; CAG33225.1; -; mRNA. DR EMBL; AK298920; BAG61026.1; -; mRNA. DR EMBL; AK302008; BAG63411.1; -; mRNA. DR EMBL; AK313011; BAG35846.1; -; mRNA. DR EMBL; AK316223; BAH14594.1; -; mRNA. DR EMBL; AL121594; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL133163; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471078; EAW65876.1; -; Genomic_DNA. DR EMBL; CH471078; EAW65877.1; -; Genomic_DNA. DR EMBL; BC002979; AAH02979.1; -; mRNA. DR EMBL; BC017882; AAH17882.1; -; mRNA. DR EMBL; BC022354; AAH22354.1; -; mRNA. DR EMBL; BC023659; AAH23659.1; -; mRNA. DR EMBL; BC070137; AAH70137.1; -; mRNA. DR EMBL; X61972; CAA43964.1; -; mRNA. DR CCDS; CCDS61437.1; -. [P60900-2] DR CCDS; CCDS61438.1; -. [P60900-3] DR CCDS; CCDS9655.1; -. [P60900-1] DR PIR; S30274; S30274. DR RefSeq; NP_001269161.1; NM_001282232.1. [P60900-3] DR RefSeq; NP_001269162.1; NM_001282233.1. [P60900-3] DR RefSeq; NP_001269163.1; NM_001282234.1. [P60900-2] DR RefSeq; NP_002782.1; NM_002791.2. [P60900-1] DR RefSeq; XP_016876957.1; XM_017021468.1. DR PDB; 4R3O; X-ray; 2.60 A; A/O=2-245. DR PDB; 4R67; X-ray; 2.89 A; A/O/c/q=2-245. DR PDB; 5A0Q; EM; 3.50 A; A/O=1-246. DR PDB; 5GJQ; EM; 4.50 A; B/h=1-246. DR PDB; 5GJR; EM; 3.50 A; B/h=1-246. DR PDB; 5L4G; EM; 4.02 A; A/N=1-246. DR PDB; 5LE5; X-ray; 1.80 A; G/U=1-246. DR PDB; 5LEX; X-ray; 2.20 A; G/U=1-246. DR PDB; 5LEY; X-ray; 1.90 A; G/U=1-246. DR PDB; 5LEZ; X-ray; 2.19 A; G/U=1-246. DR PDB; 5LF0; X-ray; 2.41 A; G/U=1-246. DR PDB; 5LF1; X-ray; 2.00 A; G/U=1-246. DR PDB; 5LF3; X-ray; 2.10 A; G/U=1-246. DR PDB; 5LF4; X-ray; 1.99 A; G/U=1-246. DR PDB; 5LF6; X-ray; 2.07 A; G/U=1-246. DR PDB; 5LF7; X-ray; 2.00 A; G/U=1-246. DR PDB; 5LN3; EM; 6.80 A; A=1-246. DR PDB; 5M32; EM; 3.80 A; G/U=1-246. DR PDB; 5T0C; EM; 3.80 A; AG/BG=2-246. DR PDB; 5T0G; EM; 4.40 A; G=2-246. DR PDB; 5T0H; EM; 6.80 A; G=2-246. DR PDB; 5T0I; EM; 8.00 A; G=2-246. DR PDB; 5T0J; EM; 8.00 A; G=2-246. DR PDB; 5VFO; EM; 3.50 A; G/g=5-244. DR PDB; 5VFP; EM; 4.20 A; G/g=5-244. DR PDB; 5VFQ; EM; 4.20 A; G/g=5-244. DR PDB; 5VFR; EM; 4.90 A; G/g=5-244. DR PDB; 5VFS; EM; 3.60 A; G/g=5-244. DR PDB; 5VFT; EM; 7.00 A; G/g=5-244. DR PDB; 5VFU; EM; 5.80 A; G/g=5-244. DR PDB; 6AVO; EM; 3.80 A; K/R=1-246. DR PDB; 6E5B; X-ray; 2.77 A; G/U=1-246. DR PDB; 6KWY; EM; 2.72 A; G/U=1-246. DR PDB; 6MSB; EM; 3.00 A; G/g=2-246. DR PDB; 6MSD; EM; 3.20 A; G/g=2-246. DR PDB; 6MSG; EM; 3.50 A; G/g=2-246. DR PDB; 6MSH; EM; 3.60 A; G/g=2-246. DR PDB; 6MSK; EM; 3.20 A; G/g=2-246. DR PDB; 6R70; EM; 3.50 A; G/U=2-245. DR PDB; 6REY; EM; 3.00 A; A/O=1-246. DR PDB; 6RGQ; EM; 2.60 A; A/O=1-246. DR PDB; 6WJD; EM; 4.80 A; G/g=2-246. DR PDB; 6WJN; EM; 5.70 A; G/g=5-244. DR PDB; 6XMJ; EM; 3.00 A; A=2-245. DR PDB; 7AWE; X-ray; 2.29 A; A/O=4-245. DR PDB; 7B12; X-ray; 2.43 A; A/O=4-245. DR PDB; 7LXV; EM; 3.40 A; G/U=1-246. DR PDB; 7NAN; EM; 2.80 A; G/U=1-246. DR PDB; 7NAO; EM; 2.90 A; G/U=1-246. DR PDB; 7NAP; EM; 3.20 A; G/U=1-246. DR PDB; 7NAQ; EM; 3.20 A; G/U=1-246. DR PDB; 7NHT; EM; 2.80 A; G=1-246. DR PDB; 7PG9; EM; 3.70 A; A/O=1-246. DR PDB; 7QXN; EM; 3.70 A; G/g=2-246. DR PDB; 7QXP; EM; 3.60 A; G/g=2-246. DR PDB; 7QXU; EM; 4.30 A; G/g=2-246. DR PDB; 7QXW; EM; 4.10 A; G/g=2-246. DR PDB; 7QXX; EM; 4.40 A; G/g=2-246. DR PDB; 7QY7; EM; 4.70 A; G/g=2-246. DR PDB; 7QYA; EM; 4.80 A; G/g=2-246. DR PDB; 7QYB; EM; 4.10 A; G/g=2-246. DR PDB; 7V5G; EM; 4.47 A; O/V=1-246. DR PDB; 7V5M; EM; 3.88 A; A/O=1-246. DR PDB; 7W37; EM; 3.00 A; G/g=1-246. DR PDB; 7W38; EM; 3.10 A; G/g=1-246. DR PDB; 7W39; EM; 3.20 A; G/g=1-246. DR PDB; 7W3A; EM; 3.50 A; G/g=1-246. DR PDB; 7W3B; EM; 3.60 A; G/g=1-246. DR PDB; 7W3C; EM; 3.40 A; G/g=1-246. DR PDB; 7W3F; EM; 3.30 A; G/g=1-246. DR PDB; 7W3G; EM; 3.20 A; G/g=1-246. DR PDB; 7W3H; EM; 3.20 A; G/g=1-246. DR PDB; 7W3I; EM; 3.50 A; G/g=1-246. DR PDB; 7W3J; EM; 3.50 A; G/g=1-246. DR PDB; 7W3K; EM; 3.60 A; G/g=1-246. DR PDB; 7W3M; EM; 3.50 A; G/g=1-246. DR PDB; 8CVR; EM; 2.70 A; A/O=1-246. DR PDB; 8CVS; EM; 3.10 A; G/U=1-246. DR PDB; 8CVT; EM; 3.00 A; G/g=1-246. DR PDB; 8CXB; EM; 2.90 A; G/U=1-246. DR PDBsum; 4R3O; -. DR PDBsum; 4R67; -. DR PDBsum; 5A0Q; -. DR PDBsum; 5GJQ; -. DR PDBsum; 5GJR; -. DR PDBsum; 5L4G; -. DR PDBsum; 5LE5; -. DR PDBsum; 5LEX; -. DR PDBsum; 5LEY; -. DR PDBsum; 5LEZ; -. DR PDBsum; 5LF0; -. DR PDBsum; 5LF1; -. DR PDBsum; 5LF3; -. DR PDBsum; 5LF4; -. DR PDBsum; 5LF6; -. DR PDBsum; 5LF7; -. DR PDBsum; 5LN3; -. DR PDBsum; 5M32; -. DR PDBsum; 5T0C; -. DR PDBsum; 5T0G; -. DR PDBsum; 5T0H; -. DR PDBsum; 5T0I; -. DR PDBsum; 5T0J; -. DR PDBsum; 5VFO; -. DR PDBsum; 5VFP; -. DR PDBsum; 5VFQ; -. DR PDBsum; 5VFR; -. DR PDBsum; 5VFS; -. DR PDBsum; 5VFT; -. DR PDBsum; 5VFU; -. DR PDBsum; 6AVO; -. DR PDBsum; 6E5B; -. DR PDBsum; 6KWY; -. DR PDBsum; 6MSB; -. DR PDBsum; 6MSD; -. DR PDBsum; 6MSG; -. DR PDBsum; 6MSH; -. DR PDBsum; 6MSK; -. DR PDBsum; 6R70; -. DR PDBsum; 6REY; -. DR PDBsum; 6RGQ; -. DR PDBsum; 6WJD; -. DR PDBsum; 6WJN; -. DR PDBsum; 6XMJ; -. DR PDBsum; 7AWE; -. DR PDBsum; 7B12; -. DR PDBsum; 7LXV; -. DR PDBsum; 7NAN; -. DR PDBsum; 7NAO; -. DR PDBsum; 7NAP; -. DR PDBsum; 7NAQ; -. DR PDBsum; 7NHT; -. DR PDBsum; 7PG9; -. DR PDBsum; 7QXN; -. DR PDBsum; 7QXP; -. DR PDBsum; 7QXU; -. DR PDBsum; 7QXW; -. DR PDBsum; 7QXX; -. DR PDBsum; 7QY7; -. DR PDBsum; 7QYA; -. DR PDBsum; 7QYB; -. DR PDBsum; 7V5G; -. DR PDBsum; 7V5M; -. DR PDBsum; 7W37; -. DR PDBsum; 7W38; -. DR PDBsum; 7W39; -. DR PDBsum; 7W3A; -. DR PDBsum; 7W3B; -. DR PDBsum; 7W3C; -. DR PDBsum; 7W3F; -. DR PDBsum; 7W3G; -. DR PDBsum; 7W3H; -. DR PDBsum; 7W3I; -. DR PDBsum; 7W3J; -. DR PDBsum; 7W3K; -. DR PDBsum; 7W3M; -. DR PDBsum; 8CVR; -. DR PDBsum; 8CVS; -. DR PDBsum; 8CVT; -. DR PDBsum; 8CXB; -. DR AlphaFoldDB; P60900; -. DR EMDB; EMD-0781; -. DR EMDB; EMD-12341; -. DR EMDB; EMD-13389; -. DR EMDB; EMD-14201; -. DR EMDB; EMD-14202; -. DR EMDB; EMD-14203; -. DR EMDB; EMD-14204; -. DR EMDB; EMD-14205; -. DR EMDB; EMD-14209; -. DR EMDB; EMD-14210; -. DR EMDB; EMD-14211; -. DR EMDB; EMD-21691; -. DR EMDB; EMD-21696; -. DR EMDB; EMD-22259; -. DR EMDB; EMD-23576; -. DR EMDB; EMD-24275; -. DR EMDB; EMD-24276; -. DR EMDB; EMD-24277; -. DR EMDB; EMD-24278; -. DR EMDB; EMD-27013; -. DR EMDB; EMD-27015; -. DR EMDB; EMD-27018; -. DR EMDB; EMD-2981; -. DR EMDB; EMD-31724; -. DR EMDB; EMD-31727; -. DR EMDB; EMD-32272; -. DR EMDB; EMD-32273; -. DR EMDB; EMD-32274; -. DR EMDB; EMD-32275; -. DR EMDB; EMD-32276; -. DR EMDB; EMD-32277; -. DR EMDB; EMD-32278; -. DR EMDB; EMD-32279; -. DR EMDB; EMD-32280; -. DR EMDB; EMD-32281; -. DR EMDB; EMD-32282; -. DR EMDB; EMD-32283; -. DR EMDB; EMD-32284; -. DR EMDB; EMD-4089; -. DR EMDB; EMD-4146; -. DR EMDB; EMD-4738; -. DR EMDB; EMD-4860; -. DR EMDB; EMD-4877; -. DR EMDB; EMD-7010; -. DR EMDB; EMD-8662; -. DR EMDB; EMD-8663; -. DR EMDB; EMD-8664; -. DR EMDB; EMD-8665; -. DR EMDB; EMD-8666; -. DR EMDB; EMD-8667; -. DR EMDB; EMD-8668; -. DR EMDB; EMD-9216; -. DR EMDB; EMD-9217; -. DR EMDB; EMD-9219; -. DR EMDB; EMD-9220; -. DR EMDB; EMD-9222; -. DR EMDB; EMD-9511; -. DR EMDB; EMD-9512; -. DR SMR; P60900; -. DR BioGRID; 111660; 295. DR ComplexPortal; CPX-5993; 26S Proteasome complex. DR CORUM; P60900; -. DR DIP; DIP-29367N; -. DR IntAct; P60900; 83. DR MINT; P60900; -. DR STRING; 9606.ENSP00000261479; -. DR BindingDB; P60900; -. DR ChEMBL; CHEMBL2364701; -. DR ChEMBL; CHEMBL3831201; -. DR DrugBank; DB08515; (3AR,6R,6AS)-6-((S)-((S)-CYCLOHEX-2-ENYL)(HYDROXY)METHYL)-6A-METHYL-4-OXO-HEXAHYDRO-2H-FURO[3,2-C]PYRROLE-6-CARBALDEHYDE. DR MEROPS; T01.971; -. DR GlyCosmos; P60900; 1 site, No reported glycans. DR GlyGen; P60900; 2 sites, 1 O-linked glycan (1 site). DR iPTMnet; P60900; -. DR MetOSite; P60900; -. DR PhosphoSitePlus; P60900; -. DR SwissPalm; P60900; -. DR BioMuta; PSMA6; -. DR DMDM; 46397659; -. DR REPRODUCTION-2DPAGE; IPI00029623; -. DR EPD; P60900; -. DR jPOST; P60900; -. DR MassIVE; P60900; -. DR MaxQB; P60900; -. DR PaxDb; 9606-ENSP00000261479; -. DR PeptideAtlas; P60900; -. DR ProteomicsDB; 4898; -. DR ProteomicsDB; 5443; -. DR ProteomicsDB; 57236; -. [P60900-1] DR Pumba; P60900; -. DR TopDownProteomics; P60900-1; -. [P60900-1] DR Antibodypedia; 155; 587 antibodies from 34 providers. DR DNASU; 5687; -. DR Ensembl; ENST00000261479.9; ENSP00000261479.4; ENSG00000100902.11. [P60900-1] DR Ensembl; ENST00000540871.5; ENSP00000444844.1; ENSG00000100902.11. [P60900-2] DR Ensembl; ENST00000555764.5; ENSP00000452566.1; ENSG00000100902.11. [P60900-3] DR Ensembl; ENST00000622405.4; ENSP00000479620.1; ENSG00000100902.11. [P60900-3] DR GeneID; 5687; -. DR KEGG; hsa:5687; -. DR MANE-Select; ENST00000261479.9; ENSP00000261479.4; NM_002791.3; NP_002782.1. DR UCSC; uc001wtd.5; human. [P60900-1] DR AGR; HGNC:9535; -. DR CTD; 5687; -. DR DisGeNET; 5687; -. DR GeneCards; PSMA6; -. DR HGNC; HGNC:9535; PSMA6. DR HPA; ENSG00000100902; Low tissue specificity. DR MalaCards; PSMA6; -. DR MIM; 602855; gene. DR neXtProt; NX_P60900; -. DR OpenTargets; ENSG00000100902; -. DR PharmGKB; PA33880; -. DR VEuPathDB; HostDB:ENSG00000100902; -. DR eggNOG; KOG0182; Eukaryota. DR GeneTree; ENSGT00550000074807; -. DR HOGENOM; CLU_035750_6_0_1; -. DR InParanoid; P60900; -. DR OrthoDB; 166567at2759; -. DR PhylomeDB; P60900; -. DR TreeFam; TF106210; -. DR PathwayCommons; P60900; -. DR Reactome; R-HSA-1169091; Activation of NF-kappaB in B cells. DR Reactome; R-HSA-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha. DR Reactome; R-HSA-1236974; ER-Phagosome pathway. DR Reactome; R-HSA-1236978; Cross-presentation of soluble exogenous antigens (endosomes). DR Reactome; R-HSA-174084; Autodegradation of Cdh1 by Cdh1:APC/C. DR Reactome; R-HSA-174113; SCF-beta-TrCP mediated degradation of Emi1. DR Reactome; R-HSA-174154; APC/C:Cdc20 mediated degradation of Securin. DR Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1. DR Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A. DR Reactome; R-HSA-180534; Vpu mediated degradation of CD4. DR Reactome; R-HSA-180585; Vif-mediated degradation of APOBEC3G. DR Reactome; R-HSA-187577; SCF(Skp2)-mediated degradation of p27/p21. DR Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex. DR Reactome; R-HSA-202424; Downstream TCR signaling. DR Reactome; R-HSA-211733; Regulation of activated PAK-2p34 by proteasome mediated degradation. DR Reactome; R-HSA-2467813; Separation of Sister Chromatids. DR Reactome; R-HSA-2871837; FCERI mediated NF-kB activation. DR Reactome; R-HSA-349425; Autodegradation of the E3 ubiquitin ligase COP1. DR Reactome; R-HSA-350562; Regulation of ornithine decarboxylase (ODC). DR Reactome; R-HSA-382556; ABC-family proteins mediated transport. DR Reactome; R-HSA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA. DR Reactome; R-HSA-4608870; Asymmetric localization of PCP proteins. DR Reactome; R-HSA-4641257; Degradation of AXIN. DR Reactome; R-HSA-4641258; Degradation of DVL. DR Reactome; R-HSA-5358346; Hedgehog ligand biogenesis. DR Reactome; R-HSA-5362768; Hh mutants are degraded by ERAD. DR Reactome; R-HSA-5607761; Dectin-1 mediated noncanonical NF-kB signaling. DR Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling. DR Reactome; R-HSA-5610780; Degradation of GLI1 by the proteasome. DR Reactome; R-HSA-5610783; Degradation of GLI2 by the proteasome. DR Reactome; R-HSA-5610785; GLI3 is processed to GLI3R by the proteasome. DR Reactome; R-HSA-5632684; Hedgehog 'on' state. DR Reactome; R-HSA-5658442; Regulation of RAS by GAPs. DR Reactome; R-HSA-5668541; TNFR2 non-canonical NF-kB pathway. DR Reactome; R-HSA-5676590; NIK-->noncanonical NF-kB signaling. DR Reactome; R-HSA-5678895; Defective CFTR causes cystic fibrosis. DR Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling. DR Reactome; R-HSA-5689603; UCH proteinases. DR Reactome; R-HSA-5689880; Ub-specific processing proteases. DR Reactome; R-HSA-68867; Assembly of the pre-replicative complex. DR Reactome; R-HSA-68949; Orc1 removal from chromatin. DR Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6. DR Reactome; R-HSA-69481; G2/M Checkpoints. DR Reactome; R-HSA-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A. DR Reactome; R-HSA-75815; Ubiquitin-dependent degradation of Cyclin D. DR Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint. DR Reactome; R-HSA-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis. DR Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs. DR Reactome; R-HSA-8939902; Regulation of RUNX2 expression and activity. DR Reactome; R-HSA-8941858; Regulation of RUNX3 expression and activity. DR Reactome; R-HSA-8948751; Regulation of PTEN stability and activity. DR Reactome; R-HSA-8951664; Neddylation. DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs. DR Reactome; R-HSA-9020702; Interleukin-1 signaling. DR Reactome; R-HSA-9604323; Negative regulation of NOTCH4 signaling. DR Reactome; R-HSA-9755511; KEAP1-NFE2L2 pathway. DR Reactome; R-HSA-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2. DR Reactome; R-HSA-9824272; Somitogenesis. DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation. DR SignaLink; P60900; -. DR SIGNOR; P60900; -. DR BioGRID-ORCS; 5687; 829 hits in 1134 CRISPR screens. DR ChiTaRS; PSMA6; human. DR GeneWiki; PSMA6; -. DR GenomeRNAi; 5687; -. DR Pharos; P60900; Tbio. DR PRO; PR:P60900; -. DR Proteomes; UP000005640; Chromosome 14. DR RNAct; P60900; Protein. DR Bgee; ENSG00000100902; Expressed in left testis and 103 other cell types or tissues. DR ExpressionAtlas; P60900; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0030016; C:myofibril; ISS:BHF-UCL. DR GO; GO:0016363; C:nuclear matrix; ISS:BHF-UCL. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0000932; C:P-body; ISS:UniProtKB. DR GO; GO:0000502; C:proteasome complex; IDA:UniProtKB. DR GO; GO:0005839; C:proteasome core complex; IDA:UniProtKB. DR GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; IDA:UniProtKB. DR GO; GO:0005840; C:ribosome; IDA:BHF-UCL. DR GO; GO:0030017; C:sarcomere; ISS:BHF-UCL. DR GO; GO:0004175; F:endopeptidase activity; NAS:UniProtKB. DR GO; GO:0051059; F:NF-kappaB binding; IPI:BHF-UCL. DR GO; GO:0035639; F:purine ribonucleoside triphosphate binding; NAS:BHF-UCL. DR GO; GO:0003723; F:RNA binding; IDA:BHF-UCL. DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:BHF-UCL. DR GO; GO:0010498; P:proteasomal protein catabolic process; IBA:GO_Central. DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; NAS:ComplexPortal. DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IMP:BHF-UCL. DR GO; GO:0050727; P:regulation of inflammatory response; IC:BHF-UCL. DR CDD; cd03754; proteasome_alpha_type_6; 1. DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1. DR InterPro; IPR029055; Ntn_hydrolases_N. DR InterPro; IPR023332; Proteasome_alpha-type. DR InterPro; IPR000426; Proteasome_asu_N. DR InterPro; IPR001353; Proteasome_sua/b. DR InterPro; IPR034642; Proteasome_subunit_alpha6. DR PANTHER; PTHR11599:SF11; PROTEASOME SUBUNIT ALPHA TYPE-6; 1. DR PANTHER; PTHR11599; PROTEASOME SUBUNIT ALPHA/BETA; 1. DR Pfam; PF00227; Proteasome; 1. DR Pfam; PF10584; Proteasome_A_N; 1. DR SMART; SM00948; Proteasome_A_N; 1. DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1. DR PROSITE; PS00388; PROTEASOME_ALPHA_1; 1. DR PROSITE; PS51475; PROTEASOME_ALPHA_2; 1. DR SWISS-2DPAGE; P60900; -. DR UCD-2DPAGE; P60900; -. DR Genevisible; P60900; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; KW Direct protein sequencing; Glycoprotein; Nucleus; Phosphoprotein; KW Proteasome; Reference proteome. FT CHAIN 1..246 FT /note="Proteasome subunit alpha type-6" FT /id="PRO_0000124130" FT MOD_RES 17 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 63 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 64 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 102 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 104 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 159 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q9QUM9" FT CARBOHYD 5 FT /note="O-linked (GlcNAc) serine" FT /evidence="ECO:0000250" FT VAR_SEQ 1..79 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_054586" FT VAR_SEQ 1..25 FT /note="MSRGSSAGFDRHITIFSPEGRLYQV -> MAGLRR (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_054587" FT CONFLICT 59 FT /note="K -> C (in Ref. 8; CAA43964)" FT /evidence="ECO:0000305" FT TURN 8..12 FT /evidence="ECO:0007829|PDB:5LE5" FT STRAND 13..15 FT /evidence="ECO:0007829|PDB:7AWE" FT STRAND 18..20 FT /evidence="ECO:0007829|PDB:5VFO" FT HELIX 23..34 FT /evidence="ECO:0007829|PDB:5LE5" FT STRAND 38..42 FT /evidence="ECO:0007829|PDB:5LE5" FT STRAND 49..53 FT /evidence="ECO:0007829|PDB:5LE5" FT STRAND 59..61 FT /evidence="ECO:0007829|PDB:5LF0" FT HELIX 63..65 FT /evidence="ECO:0007829|PDB:5LE5" FT STRAND 68..73 FT /evidence="ECO:0007829|PDB:5LE5" FT STRAND 76..82 FT /evidence="ECO:0007829|PDB:5LE5" FT HELIX 84..105 FT /evidence="ECO:0007829|PDB:5LE5" FT HELIX 111..125 FT /evidence="ECO:0007829|PDB:5LE5" FT STRAND 128..131 FT /evidence="ECO:0007829|PDB:4R3O" FT STRAND 135..144 FT /evidence="ECO:0007829|PDB:5LE5" FT TURN 145..147 FT /evidence="ECO:0007829|PDB:5LE5" FT STRAND 148..154 FT /evidence="ECO:0007829|PDB:5LE5" FT STRAND 156..158 FT /evidence="ECO:0007829|PDB:4R3O" FT STRAND 160..162 FT /evidence="ECO:0007829|PDB:5A0Q" FT STRAND 163..169 FT /evidence="ECO:0007829|PDB:5LE5" FT HELIX 172..185 FT /evidence="ECO:0007829|PDB:5LE5" FT HELIX 187..189 FT /evidence="ECO:0007829|PDB:5LE5" FT STRAND 191..193 FT /evidence="ECO:0007829|PDB:5LE5" FT HELIX 194..206 FT /evidence="ECO:0007829|PDB:5LE5" FT HELIX 212..214 FT /evidence="ECO:0007829|PDB:5LE5" FT STRAND 215..219 FT /evidence="ECO:0007829|PDB:5LE5" FT STRAND 228..230 FT /evidence="ECO:0007829|PDB:6E5B" FT HELIX 232..243 FT /evidence="ECO:0007829|PDB:5LE5" SQ SEQUENCE 246 AA; 27399 MW; 94D1FD3C0A7CC72A CRC64; MSRGSSAGFD RHITIFSPEG RLYQVEYAFK AINQGGLTSV AVRGKDCAVI VTQKKVPDKL LDSSTVTHLF KITENIGCVM TGMTADSRSQ VQRARYEAAN WKYKYGYEIP VDMLCKRIAD ISQVYTQNAE MRPLGCCMIL IGIDEEQGPQ VYKCDPAGYY CGFKATAAGV KQTESTSFLE KKVKKKFDWT FEQTVETAIT CLSTVLSIDF KPSEIEVGVV TVENPKFRIL TEAEIDAHLV ALAERD //