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P36952

- SPB5_HUMAN

UniProt

P36952 - SPB5_HUMAN

Protein

Serpin B5

Gene

SERPINB5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 2 (05 May 2009)
      Previous versions | rss
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    Functioni

    Tumor suppressor. It blocks the growth, invasion, and metastatic properties of mammary tumors. As it does not undergo the S (stressed) to R (relaxed) conformational transition characteristic of active serpins, it exhibits no serine protease inhibitory activity.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei340 – 3412Reactive bond homologBy similarity

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. serine-type endopeptidase inhibitor activity Source: RefGenome

    GO - Biological processi

    1. cellular component movement Source: ProtInc
    2. extracellular matrix organization Source: Ensembl
    3. morphogenesis of an epithelium Source: Ensembl
    4. negative regulation of endopeptidase activity Source: RefGenome
    5. prostate gland morphogenesis Source: Ensembl
    6. regulation of epithelial cell proliferation Source: Ensembl
    7. regulation of proteolysis Source: RefGenome

    Protein family/group databases

    MEROPSiI04.980.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serpin B5
    Alternative name(s):
    Maspin
    Peptidase inhibitor 5
    Short name:
    PI-5
    Gene namesi
    Name:SERPINB5
    Synonyms:PI5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 18

    Organism-specific databases

    HGNCiHGNC:8949. SERPINB5.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. extracellular space Source: UniProtKB-SubCell
    3. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA35515.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 375375Serpin B5PRO_0000032486Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi99 – 991N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi133 – 1331N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi188 – 1881N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi361 – 3611N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    MaxQBiP36952.
    PaxDbiP36952.
    PRIDEiP36952.

    PTM databases

    PhosphoSiteiP36952.

    Expressioni

    Tissue specificityi

    Normal mammary epithelial cells.

    Gene expression databases

    ArrayExpressiP36952.
    BgeeiP36952.
    CleanExiHS_SERPINB5.
    GenevestigatoriP36952.

    Organism-specific databases

    HPAiCAB009570.
    HPA019025.
    HPA019132.
    HPA020136.

    Interactioni

    Subunit structurei

    Interacts with IRF6.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PRSS21Q9Y6M07EBI-2371394,EBI-7054564

    Protein-protein interaction databases

    BioGridi111286. 8 interactions.
    IntActiP36952. 3 interactions.
    MINTiMINT-7712082.
    STRINGi9606.ENSP00000372221.

    Structurei

    Secondary structure

    1
    375
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi2 – 2221
    Beta strandi28 – 303
    Helixi32 – 4514
    Helixi48 – 5710
    Helixi60 – 623
    Helixi66 – 8015
    Turni81 – 833
    Beta strandi84 – 9512
    Helixi96 – 983
    Helixi102 – 1087
    Turni109 – 1157
    Beta strandi116 – 1194
    Turni121 – 1233
    Helixi125 – 13915
    Turni140 – 1423
    Turni147 – 1504
    Beta strandi159 – 16810
    Beta strandi171 – 1733
    Helixi177 – 1793
    Beta strandi181 – 19010
    Beta strandi192 – 20918
    Turni210 – 2134
    Beta strandi214 – 2218
    Helixi222 – 2243
    Beta strandi225 – 23511
    Helixi239 – 24911
    Helixi252 – 2587
    Helixi261 – 2633
    Beta strandi265 – 27410
    Beta strandi276 – 2827
    Helixi284 – 2918
    Turni295 – 2973
    Turni299 – 3013
    Turni305 – 3073
    Beta strandi315 – 32612
    Turni337 – 3415
    Beta strandi344 – 3496
    Beta strandi354 – 3607
    Turni361 – 3644
    Beta strandi365 – 3728

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1WZ9X-ray2.10A/B1-375[»]
    1XQGX-ray3.10A/B1-375[»]
    1XQJX-ray3.10A1-375[»]
    1XU8X-ray2.80A/B1-375[»]
    ProteinModelPortaliP36952.
    SMRiP36952. Positions 1-375.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP36952.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the serpin family. Ov-serpin subfamily.Curated

    Phylogenomic databases

    eggNOGiCOG4826.
    HOGENOMiHOG000238519.
    HOVERGENiHBG005957.
    InParanoidiP36952.
    KOiK10139.
    OMAiDTADQMK.
    OrthoDBiEOG7327PB.
    PhylomeDBiP36952.
    TreeFamiTF352619.

    Family and domain databases

    InterProiIPR000240. Serpin_B9/Maspin.
    IPR023795. Serpin_CS.
    IPR023796. Serpin_dom.
    IPR000215. Serpin_fam.
    [Graphical view]
    PANTHERiPTHR11461. PTHR11461. 1 hit.
    PfamiPF00079. Serpin. 1 hit.
    [Graphical view]
    PRINTSiPR00676. MASPIN.
    SMARTiSM00093. SERPIN. 1 hit.
    [Graphical view]
    SUPFAMiSSF56574. SSF56574. 1 hit.
    PROSITEiPS00284. SERPIN. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P36952-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MDALQLANSA FAVDLFKQLC EKEPLGNVLF SPICLSTSLS LAQVGAKGDT    50
    ANEIGQVLHF ENVKDVPFGF QTVTSDVNKL SSFYSLKLIK RLYVDKSLNL 100
    STEFISSTKR PYAKELETVD FKDKLEETKG QINNSIKDLT DGHFENILAD 150
    NSVNDQTKIL VVNAAYFVGK WMKKFSESET KECPFRVNKT DTKPVQMMNM 200
    EATFCMGNID SINCKIIELP FQNKHLSMFI LLPKDVEDES TGLEKIEKQL 250
    NSESLSQWTN PSTMANAKVK LSIPKFKVEK MIDPKACLEN LGLKHIFSED 300
    TSDFSGMSET KGVALSNVIH KVCLEITEDG GDSIEVPGAR ILQHKDELNA 350
    DHPFIYIIRH NKTRNIIFFG KFCSP 375
    Length:375
    Mass (Da):42,100
    Last modified:May 5, 2009 - v2
    Checksum:i9F24E18505912804
    GO
    Isoform 2 (identifier: P36952-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         190-231: TDTKPVQMMN...QNKHLSMFIL → VCGAACSSKR...LRARPAKCLS
         232-375: Missing.

    Show »
    Length:231
    Mass (Da):25,763
    Checksum:i62DF767BBA9B5471
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti66 – 661V → I in AAA18957. (PubMed:8290962)Curated
    Sequence conflicti245 – 2451K → Q in CAE45703. (PubMed:17974005)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti176 – 1761S → P.4 Publications
    Corresponds to variant rs2289519 [ dbSNP | Ensembl ].
    VAR_055223
    Natural varianti187 – 1871V → L.1 Publication
    Corresponds to variant rs2289520 [ dbSNP | Ensembl ].
    VAR_055224
    Natural varianti319 – 3191I → V.1 Publication
    Corresponds to variant rs1455555 [ dbSNP | Ensembl ].
    VAR_022115

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei190 – 23142TDTKP…SMFIL → VCGAACSSKRSPIIDVKNDR DRVGHKSIPMRNLRARPAKC LS in isoform 2. 1 PublicationVSP_037145Add
    BLAST
    Alternative sequencei232 – 375144Missing in isoform 2. 1 PublicationVSP_037146Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U04313 mRNA. Translation: AAA18957.1.
    AK312765 mRNA. Translation: BAG35631.1.
    AC036176 Genomic DNA. No translation available.
    BC020713 mRNA. Translation: AAH20713.1.
    BX640597 mRNA. Translation: CAE45703.1.
    CCDSiCCDS32839.1. [P36952-1]
    PIRiA36898.
    RefSeqiNP_002630.2. NM_002639.4. [P36952-1]
    UniGeneiHs.55279.

    Genome annotation databases

    EnsembliENST00000382771; ENSP00000372221; ENSG00000206075. [P36952-1]
    ENST00000489441; ENSP00000467158; ENSG00000206075. [P36952-2]
    GeneIDi5268.
    KEGGihsa:5268.
    UCSCiuc002liy.2. human. [P36952-2]
    uc002liz.4. human. [P36952-1]

    Polymorphism databases

    DMDMi229462757.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U04313 mRNA. Translation: AAA18957.1 .
    AK312765 mRNA. Translation: BAG35631.1 .
    AC036176 Genomic DNA. No translation available.
    BC020713 mRNA. Translation: AAH20713.1 .
    BX640597 mRNA. Translation: CAE45703.1 .
    CCDSi CCDS32839.1. [P36952-1 ]
    PIRi A36898.
    RefSeqi NP_002630.2. NM_002639.4. [P36952-1 ]
    UniGenei Hs.55279.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1WZ9 X-ray 2.10 A/B 1-375 [» ]
    1XQG X-ray 3.10 A/B 1-375 [» ]
    1XQJ X-ray 3.10 A 1-375 [» ]
    1XU8 X-ray 2.80 A/B 1-375 [» ]
    ProteinModelPortali P36952.
    SMRi P36952. Positions 1-375.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111286. 8 interactions.
    IntActi P36952. 3 interactions.
    MINTi MINT-7712082.
    STRINGi 9606.ENSP00000372221.

    Protein family/group databases

    MEROPSi I04.980.

    PTM databases

    PhosphoSitei P36952.

    Polymorphism databases

    DMDMi 229462757.

    Proteomic databases

    MaxQBi P36952.
    PaxDbi P36952.
    PRIDEi P36952.

    Protocols and materials databases

    DNASUi 5268.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000382771 ; ENSP00000372221 ; ENSG00000206075 . [P36952-1 ]
    ENST00000489441 ; ENSP00000467158 ; ENSG00000206075 . [P36952-2 ]
    GeneIDi 5268.
    KEGGi hsa:5268.
    UCSCi uc002liy.2. human. [P36952-2 ]
    uc002liz.4. human. [P36952-1 ]

    Organism-specific databases

    CTDi 5268.
    GeneCardsi GC18P061117.
    H-InvDB HIX0014501.
    HGNCi HGNC:8949. SERPINB5.
    HPAi CAB009570.
    HPA019025.
    HPA019132.
    HPA020136.
    MIMi 154790. gene.
    neXtProti NX_P36952.
    PharmGKBi PA35515.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG4826.
    HOGENOMi HOG000238519.
    HOVERGENi HBG005957.
    InParanoidi P36952.
    KOi K10139.
    OMAi DTADQMK.
    OrthoDBi EOG7327PB.
    PhylomeDBi P36952.
    TreeFami TF352619.

    Miscellaneous databases

    ChiTaRSi SERPINB5. human.
    EvolutionaryTracei P36952.
    GeneWikii Maspin.
    GenomeRNAii 5268.
    NextBioi 20352.
    PROi P36952.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P36952.
    Bgeei P36952.
    CleanExi HS_SERPINB5.
    Genevestigatori P36952.

    Family and domain databases

    InterProi IPR000240. Serpin_B9/Maspin.
    IPR023795. Serpin_CS.
    IPR023796. Serpin_dom.
    IPR000215. Serpin_fam.
    [Graphical view ]
    PANTHERi PTHR11461. PTHR11461. 1 hit.
    Pfami PF00079. Serpin. 1 hit.
    [Graphical view ]
    PRINTSi PR00676. MASPIN.
    SMARTi SM00093. SERPIN. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56574. SSF56574. 1 hit.
    PROSITEi PS00284. SERPIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Maspin, a serpin with tumor-suppressing activity in human mammary epithelial cells."
      Zou Z., Anisowicz A., Hendrix M.J.C., Thor A., Neveu M., Sheng S., Rafidi K., Seftor E., Sager R.
      Science 263:526-529(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS PRO-176 AND LEU-187.
      Tissue: Mammary gland.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT PRO-176.
      Tissue: Esophagus.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT PRO-176.
      Tissue: Prostate.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 245-375 (ISOFORM 1), VARIANT VAL-319.
      Tissue: Small intestine.
    6. "The tumor suppressor maspin does not undergo the stressed to relaxed transition or inhibit trypsin-like serine proteases. Evidence that maspin is not a protease inhibitory serpin."
      Pemberton P.A., Wong D.T., Gibson H.L., Kiefer M.C., Fitzpatrick P.A., Sager R., Barr P.J.
      J. Biol. Chem. 270:15832-15837(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 341-360, CHARACTERIZATION.
    7. "Mammary serine protease inhibitor (Maspin) binds directly to interferon regulatory factor 6: identification of a novel serpin partnership."
      Bailey C.M., Khalkhali-Ellis Z., Kondo S., Margaryan N.V., Seftor R.E.B., Wheaton W.W., Amir S., Pins M.R., Schutte B.C., Hendrix M.J.C.
      J. Biol. Chem. 280:34210-34217(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IRF6.
    8. "The high resolution crystal structure of the human tumor suppressor maspin reveals a novel conformational switch in the G-helix."
      Law R.H., Irving J.A., Buckle A.M., Ruzyla K., Buzza M., Bashtannyk-Puhalovich T.A., Beddoe T.C., Nguyen K., Worrall D.M., Bottomley S.P., Bird P.I., Rossjohn J., Whisstock J.C.
      J. Biol. Chem. 280:22356-22364(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
    9. Cited for: VARIANT [LARGE SCALE ANALYSIS] PRO-176, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiSPB5_HUMAN
    AccessioniPrimary (citable) accession number: P36952
    Secondary accession number(s): B2R6Y4, Q6N0B4, Q8WW89
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: May 5, 2009
    Last modified: October 1, 2014
    This is version 134 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 18
      Human chromosome 18: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3