SPB13_HUMAN
ID SPB13_HUMAN Reviewed; 391 AA.
AC Q9UIV8; A8K2Q8; Q3MII2; Q9HCX1; Q9UBW1; Q9UKG0;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Serpin B13;
DE AltName: Full=HaCaT UV-repressible serpin;
DE Short=Hurpin;
DE AltName: Full=Headpin;
DE AltName: Full=Peptidase inhibitor 13;
DE Short=PI-13;
DE AltName: Full=Proteinase inhibitor 13;
GN Name=SERPINB13; Synonyms=PI13;
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).
RC TISSUE=Skin;
RX PubMed=10512713; DOI=10.1006/jmbi.1999.3159;
RA Abts H.F., Welss T., Mirmohammadsadegh A., Koehrer K., Michel G.,
RA Ruzicka T.;
RT "Cloning and characterization of hurpin (Protease Inhibitor 13): a new skin
RT specific, UV-repressible serine proteinase inhibitor of the ovalbumin
RT serpin family.";
RL J. Mol. Biol. 293:29-39(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT SER-293.
RX PubMed=10527881; DOI=10.1006/bbrc.1999.1453;
RA Spring P., Nakashima T., Frederick M., Henderson Y., Clayman G.;
RT "Identification and cDNA cloning of headpin, a novel differentially
RT expressed serpin that maps to chromosome 18q.";
RL Biochem. Biophys. Res. Commun. 264:299-304(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX PubMed=11004515; DOI=10.1016/s0167-4781(00)00100-7;
RA Nakashima T., Pak S.C., Silverman G.A., Spring P.M., Frederick M.J.,
RA Clayman G.L.;
RT "Genomic cloning, mapping, structure and promoter analysis of HEADPIN, a
RT serpin which is down-regulated in head and neck cancer cells.";
RL Biochim. Biophys. Acta 1492:441-446(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
RC TISSUE=Placenta;
RX PubMed=11313015; DOI=10.1089/104454901300068924;
RA Abts H.F., Welss T., Scheuring S., Scott F.L., Irving J.A., Michel G.,
RA Bird P.I., Ruzicka T.;
RT "Sequence, organization, chromosomal localization and alternative splicing
RT of the human serine protease inhibitor gene hurpin (PI13), which is up-
RT regulated in psoriasis.";
RL DNA Cell Biol. 20:123-131(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-293.
RC TISSUE=Tongue;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT SER-293.
RA Mural R.J., Istrail S., Sutton 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] (ISOFORM 1).
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 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).
CC -!- FUNCTION: May play a role in the proliferation or differentiation of
CC keratinocytes.
CC -!- INTERACTION:
CC Q9UIV8; Q15700: DLG2; NbExp=3; IntAct=EBI-3048588, EBI-80426;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UIV8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UIV8-2; Sequence=VSP_006058;
CC -!- TISSUE SPECIFICITY: Skin specific.
CC -!- SIMILARITY: Belongs to the serpin family. Ov-serpin subfamily.
CC {ECO:0000305}.
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DR EMBL; AJ001696; CAA04935.2; -; mRNA.
DR EMBL; AJ001697; CAA04936.2; -; mRNA.
DR EMBL; AJ001698; CAA04937.1; -; mRNA.
DR EMBL; AF169949; AAD55765.1; -; mRNA.
DR EMBL; AF216854; AAF72879.1; -; Genomic_DNA.
DR EMBL; AJ278717; CAC03569.1; -; Genomic_DNA.
DR EMBL; AK290323; BAF83012.1; -; mRNA.
DR EMBL; AK313486; BAG36269.1; -; mRNA.
DR EMBL; CH471096; EAW63153.1; -; Genomic_DNA.
DR EMBL; BC101821; AAI01822.1; -; mRNA.
DR CCDS; CCDS11985.1; -. [Q9UIV8-1]
DR PIR; JC7118; JC7118.
DR RefSeq; NP_001294852.1; NM_001307923.1.
DR RefSeq; NP_036529.1; NM_012397.3. [Q9UIV8-1]
DR AlphaFoldDB; Q9UIV8; -.
DR SMR; Q9UIV8; -.
DR BioGRID; 111293; 122.
DR IntAct; Q9UIV8; 24.
DR STRING; 9606.ENSP00000341584; -.
DR MEROPS; I04.017; -.
DR iPTMnet; Q9UIV8; -.
DR PhosphoSitePlus; Q9UIV8; -.
DR BioMuta; SERPINB13; -.
DR DMDM; 12643252; -.
DR EPD; Q9UIV8; -.
DR MassIVE; Q9UIV8; -.
DR MaxQB; Q9UIV8; -.
DR PaxDb; Q9UIV8; -.
DR PeptideAtlas; Q9UIV8; -.
DR PRIDE; Q9UIV8; -.
DR ProteomicsDB; 84570; -. [Q9UIV8-1]
DR ProteomicsDB; 84571; -. [Q9UIV8-2]
DR Antibodypedia; 10046; 230 antibodies from 28 providers.
DR DNASU; 5275; -.
DR Ensembl; ENST00000344731.10; ENSP00000341584.6; ENSG00000197641.12. [Q9UIV8-1]
DR GeneID; 5275; -.
DR KEGG; hsa:5275; -.
DR MANE-Select; ENST00000344731.10; ENSP00000341584.6; NM_012397.4; NP_036529.1.
DR UCSC; uc002ljc.4; human. [Q9UIV8-1]
DR CTD; 5275; -.
DR DisGeNET; 5275; -.
DR GeneCards; SERPINB13; -.
DR HGNC; HGNC:8944; SERPINB13.
DR HPA; ENSG00000197641; Group enriched (esophagus, vagina).
DR MIM; 604445; gene.
DR neXtProt; NX_Q9UIV8; -.
DR OpenTargets; ENSG00000197641; -.
DR PharmGKB; PA35512; -.
DR VEuPathDB; HostDB:ENSG00000197641; -.
DR eggNOG; KOG2392; Eukaryota.
DR GeneTree; ENSGT00940000162214; -.
DR HOGENOM; CLU_023330_0_2_1; -.
DR InParanoid; Q9UIV8; -.
DR OMA; IHHQFQK; -.
DR OrthoDB; 1124079at2759; -.
DR PhylomeDB; Q9UIV8; -.
DR TreeFam; TF352619; -.
DR PathwayCommons; Q9UIV8; -.
DR Reactome; R-HSA-8939242; RUNX1 regulates transcription of genes involved in differentiation of keratinocytes.
DR SignaLink; Q9UIV8; -.
DR BioGRID-ORCS; 5275; 4 hits in 1070 CRISPR screens.
DR ChiTaRS; SERPINB13; human.
DR GeneWiki; SERPINB13; -.
DR GenomeRNAi; 5275; -.
DR Pharos; Q9UIV8; Tbio.
DR PRO; PR:Q9UIV8; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; Q9UIV8; protein.
DR Bgee; ENSG00000197641; Expressed in tongue squamous epithelium and 109 other tissues.
DR ExpressionAtlas; Q9UIV8; baseline and differential.
DR Genevisible; Q9UIV8; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IDA:UniProtKB.
DR GO; GO:0002020; F:protease binding; IPI:UniProtKB.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; NAS:UniProtKB.
DR GO; GO:0010951; P:negative regulation of endopeptidase activity; IDA:UniProtKB.
DR GO; GO:1902173; P:negative regulation of keratinocyte apoptotic process; IMP:UniProtKB.
DR GO; GO:0030162; P:regulation of proteolysis; NAS:UniProtKB.
DR GO; GO:0009411; P:response to UV; TAS:ProtInc.
DR Gene3D; 2.30.39.10; -; 1.
DR Gene3D; 3.30.497.10; -; 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; PTHR11461; 1.
DR Pfam; PF00079; Serpin; 1.
DR SMART; SM00093; SERPIN; 1.
DR SUPFAM; SSF56574; SSF56574; 1.
DR PROSITE; PS00284; SERPIN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Protease inhibitor; Reference proteome;
KW Serine protease inhibitor.
FT CHAIN 1..391
FT /note="Serpin B13"
FT /id="PRO_0000094121"
FT SITE 356..357
FT /note="Reactive bond"
FT /evidence="ECO:0000250"
FT VAR_SEQ 206..257
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_006058"
FT VARIANT 293
FT /note="G -> S (in dbSNP:rs1020694)"
FT /evidence="ECO:0000269|PubMed:10527881,
FT ECO:0000269|PubMed:14702039, ECO:0000269|Ref.6"
FT /id="VAR_024356"
FT CONFLICT 8
FT /note="S -> N (in Ref. 4; CAC03569)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="Missing (in Ref. 1; CAA04937)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="E -> Q (in Ref. 1; CAA04937)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 391 AA; 44276 MW; 2CA88558D4BC2B09 CRC64;
MDSLGAVSTR LGFDLFKELK KTNDGNIFFS PVGILTAIGM VLLGTRGATA SQLEEVFHSE
KETKSSRIKA EEKEVIENTE AVHQQFQKFL TEISKLTNDY ELNITNRLFG EKTYLFLQKY
LDYVEKYYHA SLEPVDFVNA ADESRKKINS WVESKTNEKI KDLFPDGSIS SSTKLVLVNM
VYFKGQWDRE FKKENTKEEK FWMNKSTSKS VQMMTQSHSF SFTFLEDLQA KILGIPYKNN
DLSMFVLLPN DIDGLEKIID KISPEKLVEW TSPGHMEERK VNLHLPRFEV EDGYDLEAVL
AAMGMGDAFS EHKADYSGMS SGSGLYAQKF LHSSFVAVTE EGTEAAAATG IGFTVTSAPG
HENVHCNHPF LFFIRHNESN SILFFGRFSS P
