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Protein

Serpin B10

Gene

SERPINB10

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Protease inhibitor that may play a role in the regulation of protease activities during hematopoiesis and apoptosis induced by TNF. May regulate protease activities in the cytoplasm and in the nucleus.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei362 – 3632Reactive bondBy similarity

GO - Molecular functioni

  • serine-type endopeptidase inhibitor activity Source: ProtInc

GO - Biological processi

  • activation of mitophagy in response to mitochondrial depolarization Source: ParkinsonsUK-UCL
  • negative regulation of endopeptidase activity Source: GO_Central
  • positive regulation of defense response to virus by host Source: ParkinsonsUK-UCL
Complete GO annotation...

Keywords - Molecular functioni

Protease inhibitor, Serine protease inhibitor

Protein family/group databases

MEROPSiI04.015.

Names & Taxonomyi

Protein namesi
Recommended name:
Serpin B10
Alternative name(s):
Bomapin
Peptidase inhibitor 10
Short name:
PI-10
Gene namesi
Name:SERPINB10
Synonyms:PI10
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 18

Organism-specific databases

HGNCiHGNC:8942. SERPINB10.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi74 – 774KKRK → AAAA: Abolishes nuclear localization.
Mutagenesisi395 – 3951C → S: No effect on cell proliferation. 1 Publication

Organism-specific databases

PharmGKBiPA35510.

Polymorphism and mutation databases

BioMutaiSERPINB10.
DMDMi1345616.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 397397Serpin B10PRO_0000094114Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi68 ↔ 395Redox-active1 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP48595.
PRIDEiP48595.

PTM databases

PhosphoSiteiP48595.

Expressioni

Tissue specificityi

Expressed specifically in myeloid cells and the bone marrow.2 Publications

Gene expression databases

BgeeiP48595.
CleanExiHS_SERPINB10.
ExpressionAtlasiP48595. baseline and differential.
GenevisibleiP48595. HS.

Organism-specific databases

HPAiHPA059582.

Interactioni

Protein-protein interaction databases

BioGridi111291. 1 interaction.
IntActiP48595. 1 interaction.
STRINGi9606.ENSP00000238508.

Structurei

3D structure databases

ProteinModelPortaliP48595.
SMRiP48595. Positions 1-397.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi74 – 774Nuclear localization signal

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG4826.
GeneTreeiENSGT00760000118789.
HOGENOMiHOG000238519.
HOVERGENiHBG005957.
InParanoidiP48595.
KOiK13963.
OMAiNSEEIHS.
PhylomeDBiP48595.
TreeFamiTF352619.

Family and domain databases

InterProiIPR023795. Serpin_CS.
IPR023796. Serpin_dom.
IPR000215. Serpin_fam.
[Graphical view]
PANTHERiPTHR11461. PTHR11461. 1 hit.
PfamiPF00079. Serpin. 1 hit.
[Graphical view]
SMARTiSM00093. SERPIN. 1 hit.
[Graphical view]
SUPFAMiSSF56574. SSF56574. 1 hit.
PROSITEiPS00284. SERPIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P48595-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDSLATSINQ FALELSKKLA ESAQGKNIFF SSWSISTSLT IVYLGAKGTT
60 70 80 90 100
AAQMAQVLQF NRDQGVKCDP ESEKKRKMEF NLSNSEEIHS DFQTLISEIL
110 120 130 140 150
KPNDDYLLKT ANAIYGEKTY AFHNKYLEDM KTYFGAEPQP VNFVEASDQI
160 170 180 190 200
RKDINSWVER QTEGKIQNLL PDDSVDSTTR MILVNALYFK GIWEHQFLVQ
210 220 230 240 250
NTTEKPFRIN ETTSKPVQMM FMKKKLHIFH IEKPKAVGLQ LYYKSRDLSL
260 270 280 290 300
LILLPEDING LEQLEKAITY EKLNEWTSAD MMELYEVQLH LPKFKLEDSY
310 320 330 340 350
DLKSTLSSMG MSDAFSQSKA DFSGMSSARN LFLSNVFHKA FVEINEQGTE
360 370 380 390
AAAGSGSEID IRIRVPSIEF NANHPFLFFI RHNKTNTILF YGRLCSP
Length:397
Mass (Da):45,403
Last modified:February 1, 1996 - v1
Checksum:i8CE01246867154DF
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti3 – 31S → A.
Corresponds to variant rs17072097 [ dbSNP | Ensembl ].
VAR_051949
Natural varianti41 – 411I → M.
Corresponds to variant rs8097425 [ dbSNP | Ensembl ].
VAR_024353
Natural varianti99 – 991I → T.
Corresponds to variant rs724558 [ dbSNP | Ensembl ].
VAR_024354
Natural varianti135 – 1351G → D.
Corresponds to variant rs17072146 [ dbSNP | Ensembl ].
VAR_051950
Natural varianti140 – 1401P → S.
Corresponds to variant rs9967382 [ dbSNP | Ensembl ].
VAR_024355
Natural varianti246 – 2461R → C.
Corresponds to variant rs963075 [ dbSNP | Ensembl ].
VAR_022116
Natural varianti360 – 3601D → N.1 Publication
Corresponds to variant rs35453062 [ dbSNP | Ensembl ].
VAR_051951

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U35459 mRNA. Translation: AAC50282.1.
BC096217 mRNA. Translation: AAH96217.1.
BC096219 mRNA. Translation: AAH96219.1.
BC096220 mRNA. Translation: AAH96220.1.
CCDSiCCDS11990.1.
PIRiI39184.
RefSeqiNP_005015.1. NM_005024.1.
XP_011524328.1. XM_011526026.1.
XP_011524329.1. XM_011526027.1.
UniGeneiHs.158339.

Genome annotation databases

EnsembliENST00000238508; ENSP00000238508; ENSG00000242550.
ENST00000619595; ENSP00000479385; ENSG00000242550.
GeneIDi5273.
KEGGihsa:5273.
UCSCiuc010xev.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U35459 mRNA. Translation: AAC50282.1.
BC096217 mRNA. Translation: AAH96217.1.
BC096219 mRNA. Translation: AAH96219.1.
BC096220 mRNA. Translation: AAH96220.1.
CCDSiCCDS11990.1.
PIRiI39184.
RefSeqiNP_005015.1. NM_005024.1.
XP_011524328.1. XM_011526026.1.
XP_011524329.1. XM_011526027.1.
UniGeneiHs.158339.

3D structure databases

ProteinModelPortaliP48595.
SMRiP48595. Positions 1-397.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111291. 1 interaction.
IntActiP48595. 1 interaction.
STRINGi9606.ENSP00000238508.

Protein family/group databases

MEROPSiI04.015.

PTM databases

PhosphoSiteiP48595.

Polymorphism and mutation databases

BioMutaiSERPINB10.
DMDMi1345616.

Proteomic databases

PaxDbiP48595.
PRIDEiP48595.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000238508; ENSP00000238508; ENSG00000242550.
ENST00000619595; ENSP00000479385; ENSG00000242550.
GeneIDi5273.
KEGGihsa:5273.
UCSCiuc010xev.2. human.

Organism-specific databases

CTDi5273.
GeneCardsiGC18P061556.
HGNCiHGNC:8942. SERPINB10.
HPAiHPA059582.
MIMi602058. gene.
neXtProtiNX_P48595.
PharmGKBiPA35510.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG4826.
GeneTreeiENSGT00760000118789.
HOGENOMiHOG000238519.
HOVERGENiHBG005957.
InParanoidiP48595.
KOiK13963.
OMAiNSEEIHS.
PhylomeDBiP48595.
TreeFamiTF352619.

Miscellaneous databases

GenomeRNAii5273.
NextBioi20376.
PROiP48595.
SOURCEiSearch...

Gene expression databases

BgeeiP48595.
CleanExiHS_SERPINB10.
ExpressionAtlasiP48595. baseline and differential.
GenevisibleiP48595. HS.

Family and domain databases

InterProiIPR023795. Serpin_CS.
IPR023796. Serpin_dom.
IPR000215. Serpin_fam.
[Graphical view]
PANTHERiPTHR11461. PTHR11461. 1 hit.
PfamiPF00079. Serpin. 1 hit.
[Graphical view]
SMARTiSM00093. SERPIN. 1 hit.
[Graphical view]
SUPFAMiSSF56574. SSF56574. 1 hit.
PROSITEiPS00284. SERPIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of bomapin (protease inhibitor 10), a novel human serpin that is expressed specifically in the bone marrow."
    Riewald M., Schleef R.R.
    J. Biol. Chem. 270:26754-26757(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
    Tissue: Bone marrow.
  2. "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], VARIANT ASN-360.
  3. "Identification of a nuclear targeting domain in the insertion between helices C and D in protease inhibitor-10."
    Chuang T.L., Schleef R.R.
    J. Biol. Chem. 274:11194-11198(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF 74-LYS--LYS-78.
  4. "Protease inhibitor 10 inhibits tumor necrosis factor alpha -induced cell death. Evidence for the formation of intracellular high M(r) protease inhibitor 10-containing complexes."
    Schleef R.R., Chuang T.L.
    J. Biol. Chem. 275:26385-26389(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  5. "Bomapin is a redox-sensitive nuclear serpin that affects responsiveness of myeloid progenitor cells to growth environment."
    Przygodzka P., Ramstedt B., Tengel T., Larsson G., Wilczynska M.
    BMC Cell Biol. 11:30-30(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BOND, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-395, TISSUE SPECIFICITY.

Entry informationi

Entry nameiSPB10_HUMAN
AccessioniPrimary (citable) accession number: P48595
Secondary accession number(s): Q4VAX4, Q4VAX7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: July 22, 2015
This is version 130 of the entry and version 1 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

Complete proteome, 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.