ID SPB6_HUMAN Reviewed; 376 AA. AC P35237; B2RBA8; Q59F97; Q5TD06; Q7Z2Y7; Q96J44; Q9UDI7; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 04-DEC-2007, sequence version 3. DT 02-SEP-2026, entry version 220. DE RecName: Full=Serpin B6; DE AltName: Full=Cytoplasmic antiproteinase; DE Short=CAP; DE AltName: Full=Peptidase inhibitor 6; DE Short=PI-6; DE AltName: Full=Placental thrombin inhibitor; GN Name=SERPINB6; Synonyms=PI6, PTI; 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], VARIANT VAL-90, AND FUNCTION. RC TISSUE=Placenta; RX PubMed=8415716; DOI=10.1073/pnas.90.20.9417; RA Coughlin P., Sun J., Cerruti L., Salem H.H., Bird P.; RT "Cloning and molecular characterization of a human intracellular serine RT proteinase inhibitor."; RL Proc. Natl. Acad. Sci. U.S.A. 90:9417-9421(1993). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 67-73 AND 144-149, VARIANT RP VAL-90, AND FUNCTION. RC TISSUE=Placenta; RX PubMed=8136380; DOI=10.1021/bi00177a037; RA Morgenstern K.A., Sprecher C.A., Holth L., Foster D., Grant F.J., Ching A., RA Kisiel W.; RT "Complementary DNA cloning and kinetic characterization of a novel RT intracellular serine proteinase inhibitor: mechanism of action with trypsin RT and factor Xa as model proteinases."; RL Biochemistry 33:3432-3441(1994). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-90. RC TISSUE=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 MRNA], AND VARIANT VAL-90. RC TISSUE=Small intestine; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [6] 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Chondrosarcoma, and Colon; 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 [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-372. RC TISSUE=Brain; RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., RA Ohara O., Nagase T., Kikuno R.F.; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP PROTEIN SEQUENCE OF 47-60; 63-81 AND 91-98, AND SUBCELLULAR LOCATION. RC TISSUE=Leukemia; RX PubMed=8486644; DOI=10.1016/s0021-9258(18)98385-7; RA Coughlin P.B., Tetaz T., Salem H.H.; RT "Identification and purification of a novel serine proteinase inhibitor."; RL J. Biol. Chem. 268:9541-9547(1993). RN [10] RP FUNCTION. RX PubMed=10068683; DOI=10.1182/blood.v93.6.2089.406k10_2089_2097; RA Scott F.L., Hirst C.E., Sun J., Bird C.H., Bottomley S.P., Bird P.I.; RT "The intracellular serpin proteinase inhibitor 6 is expressed in monocytes RT and granulocytes and is a potent inhibitor of the azurophilic granule RT protease, cathepsin G."; RL Blood 93:2089-2097(1999). RN [11] RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND COMPLEX FORMATION WITH RP BETA-TRYPTASE. RX PubMed=14670919; DOI=10.1182/blood-2003-08-2981; RA Strik M.C., Wolbink A., Wouters D., Bladergroen B.A., Verlaan A.R., RA van Houdt I.S., Hijlkema S., Hack C.E., Kummer J.A.; RT "Intracellular serpin SERPINB6 (PI6) is abundantly expressed by human mast RT cells and forms complexes with beta-tryptase monomers."; RL Blood 103:2710-2717(2004). RN [12] RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=17761692; DOI=10.1093/jb/mvm156; RA Scott F.L., Sun J., Whisstock J.C., Kato K., Bird P.I.; RT "SerpinB6 is an inhibitor of kallikrein-8 in keratinocytes."; RL J. Biochem. 142:435-442(2007). RN [13] 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 [14] RP INVOLVEMENT IN DFNB91, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. RX PubMed=20451170; DOI=10.1016/j.ajhg.2010.04.004; RA Sirmaci A., Erbek S., Price J., Huang M., Duman D., Cengiz F.B., RA Bademci G., Tokgoz-Yilmaz S., Hismi B., Ozdag H., Ozturk B., RA Kulaksizoglu S., Yildirim E., Kokotas H., Grigoriadou M., Petersen M.B., RA Shahin H., Kanaan M., King M.C., Chen Z.Y., Blanton S.H., Liu X.Z., RA Zuchner S., Akar N., Tekin M.; RT "A truncating mutation in SERPINB6 is associated with autosomal-recessive RT nonsyndromic sensorineural hearing loss."; RL Am. J. Hum. Genet. 86:797-804(2010). 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 ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151, AND IDENTIFICATION BY RP 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). CC -!- FUNCTION: May be involved in the regulation of serine proteinases CC present in the brain or extravasated from the blood (By similarity). CC Inhibitor of cathepsin G, kallikrein-8 and thrombin. May play an CC important role in the inner ear in the protection against leakage of CC lysosomal content during stress and loss of this protection results in CC cell death and sensorineural hearing loss. {ECO:0000250, CC ECO:0000269|PubMed:10068683, ECO:0000269|PubMed:17761692, CC ECO:0000269|PubMed:20451170, ECO:0000269|PubMed:8136380, CC ECO:0000269|PubMed:8415716}. CC -!- SUBUNIT: Forms a complex with the monomeric form of beta-tryptase. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14670919, CC ECO:0000269|PubMed:17761692, ECO:0000269|PubMed:20451170, CC ECO:0000269|PubMed:8486644}. CC -!- TISSUE SPECIFICITY: Expressed in keratinocytes (at protein level). CC Highest levels in skeletal muscle. Also found in placenta, cardiac CC muscle, lung, liver, kidney and pancreas. Expressed in the inner ear CC hair cells. Expressed abundantly by normal mast cells in different CC tissues and by mast cells in mastocytoma lesions. CC {ECO:0000269|PubMed:14670919, ECO:0000269|PubMed:17761692, CC ECO:0000269|PubMed:20451170}. CC -!- DISEASE: Deafness, autosomal recessive, 91 (DFNB91) [MIM:613453]: A CC form of non-syndromic deafness characterized by progressive and age- CC dependent sensorineural hearing loss. Vestibular function is normal. CC {ECO:0000269|PubMed:20451170}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the serpin family. Ov-serpin subfamily. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAD92800.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=CAD98106.1; Type=Erroneous initiation; 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; Z22658; CAA80373.1; -; mRNA. DR EMBL; S69272; AAB30320.1; -; mRNA. DR EMBL; AK314578; BAG37155.1; -; mRNA. DR EMBL; BX538343; CAD98106.1; ALT_INIT; mRNA. DR EMBL; AL133351; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471087; EAW55097.1; -; Genomic_DNA. DR EMBL; BC001394; AAH01394.1; -; mRNA. DR EMBL; BC098564; AAH98564.1; -; mRNA. DR EMBL; AB209563; BAD92800.1; ALT_INIT; mRNA. DR CCDS; CCDS4479.1; -. DR PIR; A48681; A48681. DR RefSeq; NP_001182220.2; NM_001195291.3. DR RefSeq; NP_001258751.1; NM_001271822.2. DR RefSeq; NP_001258752.1; NM_001271823.2. DR RefSeq; NP_001258753.1; NM_001271824.2. DR RefSeq; NP_001258754.1; NM_001271825.2. DR RefSeq; NP_001284628.1; NM_001297699.2. DR RefSeq; NP_001284629.1; NM_001297700.2. DR RefSeq; NP_001361445.1; NM_001374516.1. DR RefSeq; NP_004559.4; NM_004568.6. DR RefSeq; XP_047274847.1; XM_047418891.1. DR RefSeq; XP_047274848.1; XM_047418892.1. DR RefSeq; XP_054211612.1; XM_054355637.1. DR AlphaFoldDB; P35237; -. DR SMR; P35237; -. DR BioGRID; 111287; 56. DR FunCoup; P35237; 222. DR IntAct; P35237; 25. DR MINT; P35237; -. DR NDEx; IQUERY-CP-SERPINB6; 1 NDEx IQuery Curated Pathway. DR STRING; 9606.ENSP00000484343; -. DR BindingDB; P35237; -. DR ChEMBL; CHEMBL6066433; -. DR DrugBank; DB00055; Drotrecogin alfa. DR MEROPS; I04.011; -. DR GlyGen; P35237; 3 sites, 2 N-linked glycans (2 sites), 1 O-linked glycan (1 site). DR iPTMnet; P35237; -. DR MetOSite; P35237; -. DR PhosphoSitePlus; P35237; -. DR SwissPalm; P35237; -. DR BioMuta; SERPINB6; -. DR DMDM; 161784343; -. DR OGP; P35237; -. DR jPOST; P35237; -. DR MassIVE; P35237; -. DR PaxDb; 9606-ENSP00000484343; -. DR PeptideAtlas; P35237; -. DR PRIDE; P35237; -. DR ProteomicsDB; 54998; -. DR Pumba; P35237; -. DR Antibodypedia; 1702; 299 antibodies from 38 providers. DR DNASU; 5269; -. DR Ensembl; ENST00000380520.6; ENSP00000369891.1; ENSG00000124570.22. DR Ensembl; ENST00000380524.5; ENSP00000369896.1; ENSG00000124570.22. DR Ensembl; ENST00000380529.5; ENSP00000369901.1; ENSG00000124570.22. DR Ensembl; ENST00000380539.7; ENSP00000369912.2; ENSG00000124570.22. DR Ensembl; ENST00000380546.7; ENSP00000369919.3; ENSG00000124570.22. DR Ensembl; ENST00000643098.1; ENSP00000493936.1; ENSG00000124570.22. DR Ensembl; ENST00000644178.1; ENSP00000496073.1; ENSG00000124570.22. DR Ensembl; ENST00000644388.1; ENSP00000494650.1; ENSG00000124570.22. DR Ensembl; ENST00000860477.1; ENSP00000530536.1; ENSG00000124570.22. DR Ensembl; ENST00000860478.1; ENSP00000530537.1; ENSG00000124570.22. DR Ensembl; ENST00000860480.1; ENSP00000530539.1; ENSG00000124570.22. DR Ensembl; ENST00000860481.1; ENSP00000530540.1; ENSG00000124570.22. DR Ensembl; ENST00000860483.1; ENSP00000530542.1; ENSG00000124570.22. DR Ensembl; ENST00000860484.1; ENSP00000530543.1; ENSG00000124570.22. DR Ensembl; ENST00000860485.1; ENSP00000530544.1; ENSG00000124570.22. DR Ensembl; ENST00000860486.1; ENSP00000530545.1; ENSG00000124570.22. DR Ensembl; ENST00000860487.1; ENSP00000530546.1; ENSG00000124570.22. DR Ensembl; ENST00000860488.1; ENSP00000530547.1; ENSG00000124570.22. DR Ensembl; ENST00000860489.1; ENSP00000530548.1; ENSG00000124570.22. DR Ensembl; ENST00000860490.1; ENSP00000530549.1; ENSG00000124570.22. DR Ensembl; ENST00000860491.1; ENSP00000530550.1; ENSG00000124570.22. DR Ensembl; ENST00000860492.1; ENSP00000530551.1; ENSG00000124570.22. DR Ensembl; ENST00000860493.1; ENSP00000530552.1; ENSG00000124570.22. DR Ensembl; ENST00000860494.1; ENSP00000530553.1; ENSG00000124570.22. DR Ensembl; ENST00000860495.1; ENSP00000530554.1; ENSG00000124570.22. DR Ensembl; ENST00000860497.1; ENSP00000530556.1; ENSG00000124570.22. DR Ensembl; ENST00000860498.1; ENSP00000530557.1; ENSG00000124570.22. DR Ensembl; ENST00000860499.1; ENSP00000530558.1; ENSG00000124570.22. DR Ensembl; ENST00000860500.1; ENSP00000530559.1; ENSG00000124570.22. DR Ensembl; ENST00000860501.1; ENSP00000530560.1; ENSG00000124570.22. DR Ensembl; ENST00000860502.1; ENSP00000530561.1; ENSG00000124570.22. DR Ensembl; ENST00000860503.1; ENSP00000530562.1; ENSG00000124570.22. DR Ensembl; ENST00000860504.1; ENSP00000530563.1; ENSG00000124570.22. DR Ensembl; ENST00000860505.1; ENSP00000530564.1; ENSG00000124570.22. DR Ensembl; ENST00000860506.1; ENSP00000530565.1; ENSG00000124570.22. DR Ensembl; ENST00000860508.1; ENSP00000530567.1; ENSG00000124570.22. DR Ensembl; ENST00000860509.1; ENSP00000530568.1; ENSG00000124570.22. DR Ensembl; ENST00000860510.1; ENSP00000530569.1; ENSG00000124570.22. DR Ensembl; ENST00000860511.1; ENSP00000530570.1; ENSG00000124570.22. DR Ensembl; ENST00000860512.1; ENSP00000530571.1; ENSG00000124570.22. DR Ensembl; ENST00000860513.1; ENSP00000530572.1; ENSG00000124570.22. DR Ensembl; ENST00000860514.1; ENSP00000530573.1; ENSG00000124570.22. DR Ensembl; ENST00000860515.1; ENSP00000530574.1; ENSG00000124570.22. DR Ensembl; ENST00000922588.1; ENSP00000592647.1; ENSG00000124570.22. DR Ensembl; ENST00000922589.1; ENSP00000592648.1; ENSG00000124570.22. DR Ensembl; ENST00000922590.1; ENSP00000592649.1; ENSG00000124570.22. DR Ensembl; ENST00000950811.1; ENSP00000620870.1; ENSG00000124570.22. DR Ensembl; ENST00000950812.1; ENSP00000620871.1; ENSG00000124570.22. DR Ensembl; ENST00000950813.1; ENSP00000620872.1; ENSG00000124570.22. DR Ensembl; ENST00000950814.1; ENSP00000620873.1; ENSG00000124570.22. DR Ensembl; ENST00000950815.1; ENSP00000620874.1; ENSG00000124570.22. DR Ensembl; ENST00000950816.1; ENSP00000620875.1; ENSG00000124570.22. DR Ensembl; ENST00000950817.1; ENSP00000620876.1; ENSG00000124570.22. DR Ensembl; ENST00000950818.1; ENSP00000620877.1; ENSG00000124570.22. DR Ensembl; ENST00000950819.1; ENSP00000620878.1; ENSG00000124570.22. DR Ensembl; ENST00000950820.1; ENSP00000620879.1; ENSG00000124570.22. DR Ensembl; ENST00000950821.1; ENSP00000620880.1; ENSG00000124570.22. DR Ensembl; ENST00000950822.1; ENSP00000620881.1; ENSG00000124570.22. DR Ensembl; ENST00000950823.1; ENSP00000620882.1; ENSG00000124570.22. DR Ensembl; ENST00000950824.1; ENSP00000620883.1; ENSG00000124570.22. DR Ensembl; ENST00000950825.1; ENSP00000620884.1; ENSG00000124570.22. DR Ensembl; ENST00000950826.1; ENSP00000620885.1; ENSG00000124570.22. DR Ensembl; ENST00000950827.1; ENSP00000620886.1; ENSG00000124570.22. DR Ensembl; ENST00000950828.1; ENSP00000620887.1; ENSG00000124570.22. DR Ensembl; ENST00000950829.1; ENSP00000620888.1; ENSG00000124570.22. DR Ensembl; ENST00000950830.1; ENSP00000620889.1; ENSG00000124570.22. DR Ensembl; ENST00000950831.1; ENSP00000620890.1; ENSG00000124570.22. DR Ensembl; ENST00000950832.1; ENSP00000620891.1; ENSG00000124570.22. DR Ensembl; ENST00000950833.1; ENSP00000620892.1; ENSG00000124570.22. DR Ensembl; ENST00000950834.1; ENSP00000620893.1; ENSG00000124570.22. DR Ensembl; ENST00000950835.1; ENSP00000620894.1; ENSG00000124570.22. DR Ensembl; ENST00000950836.1; ENSP00000620895.1; ENSG00000124570.22. DR Ensembl; ENST00000950837.1; ENSP00000620896.1; ENSG00000124570.22. DR GeneID; 5269; -. DR KEGG; hsa:5269; -. DR MANE-Select; ENST00000380539.7; ENSP00000369912.2; NM_004568.6; NP_004559.4. DR UCSC; uc003muk.3; human. DR AGR; HGNC:8950; -. DR ClinPGx; PA35516; -. DR CTD; 5269; -. DR DisGeNET; 5269; -. DR GeneCards; SERPINB6; -. DR HGNC; HGNC:8950; SERPINB6. DR HPA; ENSG00000124570; Low tissue specificity. DR MalaCards; SERPINB6; -. DR MIM; 173321; gene. DR MIM; 613453; phenotype. DR OpenTargets; ENSG00000124570; -. DR Orphanet; 90636; Autosomal recessive non-syndromic genetic deafness. DR VEuPathDB; HostDB:ENSG00000124570; -. DR eggNOG; KOG2392; Eukaryota. DR GeneTree; ENSGT00940000154519; -. DR HOGENOM; CLU_023330_0_2_1; -. DR InParanoid; P35237; -. DR OMA; DSCCKFY; -. DR OrthoDB; 671595at2759; -. DR PAN-GO; P35237; 3 GO annotations based on evolutionary models. DR PhylomeDB; P35237; -. DR PathwayCommons; P35237; -. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR Reactome; R-HSA-75205; Dissolution of Fibrin Clot. DR SignaLink; P35237; -. DR Agora; ENSG00000124570; -. DR BioGRID-ORCS; 5269; 30 hits in 1157 CRISPR screens. DR ChiTaRS; SERPINB6; human. DR GeneWiki; SERPINB6; -. DR GenomeRNAi; 5269; -. DR Pharos; P35237; Tbio. DR PRO; PR:P35237; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; P35237; protein. DR Bgee; ENSG00000124570; Expressed in right testis and 206 other cell types or tissues. DR ExpressionAtlas; P35237; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:ProtInc. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0031012; C:extracellular matrix; HDA:BHF-UCL. DR GO; GO:0005576; C:extracellular region; HDA:BHF-UCL. DR GO; GO:0101003; C:ficolin-1-rich granule membrane; TAS:Reactome. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0030667; C:secretory granule membrane; TAS:Reactome. DR GO; GO:0097180; C:serine protease inhibitor complex; IDA:BHF-UCL. DR GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome. DR GO; GO:0002020; F:protease binding; IPI:UniProtKB. DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:BHF-UCL. DR GO; GO:0071470; P:cellular response to osmotic stress; IMP:UniProtKB. DR GO; GO:0007605; P:sensory perception of sound; IMP:UniProtKB. DR CDD; cd19565; serpinB6_CAP; 1. DR FunFam; 2.30.39.10:FF:000001; Serpin family B member 2; 1. DR FunFam; 3.30.497.10:FF:000018; Serpin family B member 8; 1. DR Gene3D; 2.30.39.10; Alpha-1-antitrypsin, domain 1; 1. DR Gene3D; 3.30.497.10; Antithrombin, subunit I, domain 2; 1. DR InterPro; IPR023795; Serpin_CS. DR InterPro; IPR023796; Serpin_dom. DR InterPro; IPR000215; Serpin_fam. DR InterPro; IPR036186; Serpin_sf. DR InterPro; IPR042178; Serpin_sf_1. DR InterPro; IPR042185; Serpin_sf_2. DR PANTHER; PTHR11461; SERINE PROTEASE INHIBITOR, SERPIN; 1. DR PANTHER; PTHR11461:SF204; SERPIN B6; 1. DR Pfam; PF00079; Serpin; 1. DR SMART; SM00093; SERPIN; 1. DR SUPFAM; SSF56574; Serpins; 1. DR PROSITE; PS00284; SERPIN; 1. PE 1: Evidence at protein level; KW Acetylation; Cytoplasm; Deafness; Direct protein sequencing; KW Non-syndromic deafness; Phosphoprotein; Protease inhibitor; KW Proteomics identification; Reference proteome; Serine protease inhibitor. FT CHAIN 1..376 FT /note="Serpin B6" FT /id="PRO_0000094106" FT SITE 341..342 FT /note="Reactive bond" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:22223895" FT MOD_RES 151 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 195 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q60854" FT VARIANT 90 FT /note="M -> V (in dbSNP:rs2295769)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:17974005, ECO:0000269|PubMed:8136380, FT ECO:0000269|PubMed:8415716" FT /id="VAR_037295" FT VARIANT 153 FT /note="G -> S (in dbSNP:rs2295766)" FT /id="VAR_037296" FT CONFLICT 175 FT /note="E -> G (in Ref. 1; CAA80373)" FT /evidence="ECO:0000305" FT CONFLICT 200 FT /note="M -> V (in Ref. 3; BAG37155)" FT /evidence="ECO:0000305" FT CONFLICT 362 FT /note="S -> R (in Ref. 1; CAA80373)" FT /evidence="ECO:0000305" SQ SEQUENCE 376 AA; 42622 MW; 3A06BC26A7510E1A CRC64; MDVLAEANGT FALNLLKTLG KDNSKNVFFS PMSMSCALAM VYMGAKGNTA AQMAQILSFN KSGGGGDIHQ GFQSLLTEVN KTGTQYLLRM ANRLFGEKSC DFLSSFRDSC QKFYQAEMEE LDFISAVEKS RKHINTWVAE KTEGKIAELL SPGSVDPLTR LVLVNAVYFR GNWDEQFDKE NTEERLFKVS KNEEKPVQMM FKQSTFKKTY IGEIFTQILV LPYVGKELNM IIMLPDETTD LRTVEKELTY EKFVEWTRLD MMDEEEVEVS LPRFKLEESY DMESVLRNLG MTDAFELGKA DFSGMSQTDL SLSKVVHKSF VEVNEEGTEA AAATAAIMMM RCARFVPRFC ADHPFLFFIQ HSKTNGILFC GRFSSP //