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P60330

- ESPL1_MOUSE

UniProt

P60330 - ESPL1_MOUSE

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Protein

Separin

Gene

Espl1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Display
All None

  • Function
  • Names & Taxonomy
  • Subcellular locationSubcell. location
  • Pathology & BiotechPathol./Biotech
  • PTM / Processing
  • Expression
  • Interaction
  • Structure
  • Family & Domains
  • Sequence
  • Cross-references
  • Publications
  • Entry information
  • Miscellaneous
  • Similar proteins
Top

Functioni

Caspase-like protease, which plays a central role in the chromosome segregation by cleaving the SCC1/RAD21 subunit of the cohesin complex at the onset of anaphase. During most of the cell cycle, it is inactivated by different mechanisms (By similarity).By similarity

Catalytic activityi

All bonds known to be hydrolyzed by this endopeptidase have arginine in P1 and an acidic residue in P4. P6 is often occupied by an acidic residue or by a hydroxy-amino-acid residue, the phosphorylation of which enhances cleavage.

Enzyme regulationi

Regulated by at least two independent mechanisms. First, it is inactivated via its interaction with securin/PTTG1, which probably covers its active site. The association with PTTG1 is not only inhibitory, since PTTG1 is also required for activating it, the enzyme being inactive in cells in which PTTG1 is absent. PTTG1 degradation at anaphase, liberates it and triggers RAD21 cleavage. Second, phosphorylation at Ser-1121 inactivates it. The complete phosphorylation during mitosis, is removed when cells undergo anaphase. Activation of the enzyme at the metaphase-anaphase transition probably requires the removal of both securin and inhibitory phosphate (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei1502 – 15032Cleavage; by autolysisBy similarity
Sitei1531 – 15322Cleavage; by autolysisBy similarity
Active sitei2025 – 20251By similarity

GO - Molecular functioni

  1. cysteine-type peptidase activity Source: MGI
  2. peptidase activity Source: MGI

GO - Biological processi

  1. chromosome segregation Source: MGI
  2. homologous chromosome segregation Source: MGI
  3. meiosis I Source: MGI
  4. meiotic spindle organization Source: MGI
  5. mitotic nuclear division Source: MGI
  6. mitotic sister chromatid segregation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Chromosome partition

Enzyme and pathway databases

ReactomeiREACT_207679. Separation of Sister Chromatids.

Protein family/group databases

MEROPSiC50.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Separin (EC:3.4.22.49)
Alternative name(s):
Caspase-like protein ESPL1
Extra spindle poles-like 1 protein
Separase
Gene namesi
Name:Espl1
Synonyms:Esp1, Kiaa0165
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus
ProteomesiUP000000589: Chromosome 15

Organism-specific databases

MGIiMGI:2146156. Espl1.

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity

GO - Cellular componenti

  1. centrosome Source: Ensembl
  2. cytoplasm Source: UniProtKB-SubCell
  3. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 21182118SeparinPRO_0000205901Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1121 – 11211PhosphoserineBy similarity
Modified residuei1391 – 13911PhosphoserineBy similarity
Modified residuei1394 – 13941PhosphoserineBy similarity
Modified residuei1504 – 15041PhosphoserineBy similarity

Post-translational modificationi

Autocleaves. This function, which is not essential for its protease activity, is unknown (By similarity).By similarity
Phosphorylated by CDK1. There is 8 Ser/Thr phosphorylation sites. Among them, only Ser-1121 phosphorylation is the major site, which conducts to the enzyme inactivation (By similarity).By similarity

Keywords - PTMi

Autocatalytic cleavage, Phosphoprotein

Proteomic databases

MaxQBiP60330.
PaxDbiP60330.
PRIDEiP60330.

PTM databases

PhosphoSiteiP60330.

Expressioni

Gene expression databases

BgeeiP60330.
CleanExiMM_ESPL1.
GenevestigatoriP60330.

Interactioni

Subunit structurei

Interacts with PTTG1. Interacts with RAD21 (By similarity).By similarity

Protein-protein interaction databases

BioGridi222968. 5 interactions.
IntActiP60330. 5 interactions.
STRINGi10090.ENSMUSP00000064465.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1941 – 203696Peptidase C50Add
BLAST

Sequence similaritiesi

Contains 1 peptidase C50 domain.Curated

Phylogenomic databases

eggNOGiCOG5155.
GeneTreeiENSGT00390000004990.
HOGENOMiHOG000290657.
HOVERGENiHBG051510.
InParanoidiP60330.
KOiK02365.
OMAiELAQVLC.
OrthoDBiEOG7PCJGQ.
PhylomeDBiP60330.
TreeFamiTF101169.

Family and domain databases

InterProiIPR005314. Peptidase_C50.
IPR030397. SEPARIN_core_dom.
[Graphical view]
PANTHERiPTHR12792. PTHR12792. 1 hit.
PfamiPF03568. Peptidase_C50. 1 hit.
[Graphical view]
PROSITEiPS51700. SEPARIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P60330-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRNFKGVNFA TLLCSKEETQ QLLPDLKEFL SRSRTDFPSS RTDAERRQIC 
        60         70         80         90        100
DTILRACTQQ LTAKLDCPGH LRSILDLAEL ACDGYLLSTP QRPPLYLERI 
       110        120        130        140        150
LFILLRNGST QGSPDTVLRL AQPLHACLVQ NSGEAAPQDY EAVTRGSFSL 
       160        170        180        190        200
FWKGAEALLE RRAAFSTRLN ALSFLVLLED GSVPCEVPHF ASPTACRLVA 
       210        220        230        240        250
AYQLYDATGQ GLDEADADFL YEVLSRHLIR VLVGEGGSSP GPLSPQRALC 
       260        270        280        290        300
LLEITLEHCR RLCWNHHHRQ AARAVERARN HLEKTSVAPS LQLCQMGVEL 
       310        320        330        340        350
LEAVEERPGA VAQLLRKAAA VLINSIEAPS PPLRALYDSC QFFLSGLERG 
       360        370        380        390        400
IRRHCGLDAI LSLFAFLGGY SSLVRHLREV SEASSKQQQC LLQMHFQGFH 
       410        420        430        440        450
LFTGIVYDFA QGCQATELAQ LVDGCRSAAV WMLEALEGLS GGELADYLSM 
       460        470        480        490        500
TASYTSNLAY SFFSQKLYEE ACVISEPVCQ HLGSATSGAC PEVPPEKLHR 
       510        520        530        540        550
CFRLHVESLK KLGKQAQGCK MVTLWLAALK PYSLEHMVEP VTFWVRVKMD 
       560        570        580        590        600
ASRAGDKELQ LQTLRDSLSC WDPETQSLLL REELRAYKSV RADTGQERFN 
       610        620        630        640        650
IICDLLELSP EETAAGAWAR ATYLVELAQV LCYHNFTQQT NCSALDAVQE 
       660        670        680        690        700
ALQLLESVSP EAQEQDRLLD DKAQALLWLY ICTLEAKMQE GIERDRRAQA 
       710        720        730        740        750
PSNLEEFEVN DLNYEDKLQE DRFLYSSIAF NLAADAAQSK CLDQALTLWK 
       760        770        780        790        800
EVLTKGRAPA VRCLQQTAAS LQILAAVYQL VAKPLQALET LLLLQIVSKR 
       810        820        830        840        850
LQDHAKAASS SCQLTQLLLN LGCPSYAQLY LEEAESSLRS LDQTSDACQL 
       860        870        880        890        900
LSLTCALLGS QLCWACQKVT AGVSLLLSVL RDPALQKSSK AWYLLRVQAL 
       910        920        930        940        950
QVLAFYLSLS SNLLSSALRE QLWDQGWQTP ETALIDAHKL LRSIIILLMG 
       960        970        980        990       1000
SDVLSIQKAA TESPFLDYGE NLVQKWQVLT EVLTCSERLV GRLGRLGNVS 
      1010       1020       1030       1040       1050
EAKAFCLEAL KLTTKLQIPR QCALFLVLKG ELELARGDID LCQSDLQQVL 
      1060       1070       1080       1090       1100
FLLESSTEFG VVTQHPDSVK KVHTQKGKHK AQGPCFPPLS EEEPFLKGPA 
      1110       1120       1130       1140       1150
LELVDTVLNE PGPIQSSVNS SPVLKTKPPP NPGFLSHLPS CDCLLCASPA 
      1160       1170       1180       1190       1200
LSAVCLRWVL VTAGVRLATG HKAQGLDLLQ AVLTRCPAAT KRFTQSLQAS 
      1210       1220       1230       1240       1250
LNHRTTPSCV PSLFDEIMAQ VYTHLALEFL NQTSEKSLGK VLASGLKFVA 
      1260       1270       1280       1290       1300
TRIQSLEIWR AHLLLVQALA KLAHFSCCTS ELFASSWGWH PPLVKSLPVL 
      1310       1320       1330       1340       1350
EPAKIRRQKC SGRGRRRIAS VPPPLHNSSQ KGLEEEGPPC TPKPPGRARQ 
      1360       1370       1380       1390       1400
AGPRVPFTIF EEVHPTKSKL QVPLAPRVHR RAQTRLKVIF SDDSDLEDLV 
      1410       1420       1430       1440       1450
SADTQLVEEP KRRGTASRTR GQTRKGRSLK TDAVVAIEST PGHSSVSGRT 
      1460       1470       1480       1490       1500
RRARKVASRN CEEESPKAPL CVWASQGPEI MRSIPEEEPV DNHLEKSFEI 
      1510       1520       1530       1540       1550
LRGSDGEDSA SGEKAAAADT GLPVGECEVL RRDSSKAERP VLYSDTEANS 
      1560       1570       1580       1590       1600
DPSPWLPPFS VPAPIDLSTL DSISDSLSIA FRGVSHCPPS GLYAHLCRFL 
      1610       1620       1630       1640       1650
ALCLGHRDPY ATAFLVAESI SITCRHQLLT HLHRQLSKAQ KQQESPELAE 
      1660       1670       1680       1690       1700
HLQRLDLKER PGGVPLARIQ RLFSFKALGS GCFPQAEKES FQERLALIPS 
      1710       1720       1730       1740       1750
GVTVCVLALA TLQPGTLSNT LLLTRLEKDN PPITVKIPTA QNKLPLSAVL 
      1760       1770       1780       1790       1800
KEFDAIQKDQ KENSSCTEKR VWWTGRLALD QRMEALITAL EEQVLGCWRG 
      1810       1820       1830       1840       1850
LLLPCSADPS LAQEASKLQE LLRECGWEYP DSTLLKVILS GARILTSQDV 
      1860       1870       1880       1890       1900
QALACGLCPA QPDRAQVLLS EAVGQVQSQE APRSQHLVLV LDKDLQKLPW 
      1910       1920       1930       1940       1950
ESTPILQAQP VTRLPSFRFL LSYTVTKEAG ASSVLSQGVD PQNTFYVLNP 
      1960       1970       1980       1990       2000
HSNLSSTEER FRASFSSETG WKGVIGEVPS LDQVQAALTE RDLYIYAGHG 
      2010       2020       2030       2040       2050
AGARFLDGQA VLRLSCRAVA LLFGCSSAAL AVHGNLEGAG IVLKYIMAGC 
      2060       2070       2080       2090       2100
PLFLGNLWDV TDRDIDRYTE ALLQGWLGAG PGAPFLYYAS QARQAPRLKY 
      2110 
LIGAAPVAYG LPISLQTP
Length:2,118
Mass (Da):233,035
Last modified:February 2, 2004 - v1
Checksum:i484FCE178C0984B6
GO

Sequence cautioni

The sequence BAC97882.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK129072 mRNA. Translation: BAC97882.1. Different initiation.
BC145846 mRNA. Translation: AAI45847.1.
CCDSiCCDS27878.1.
RefSeqiNP_001014976.1. NM_001014976.2.
XP_006520320.1. XM_006520257.1.
XP_006520321.1. XM_006520258.1.
XP_006520322.1. XM_006520259.1.
UniGeneiMm.288324.

Genome annotation databases

EnsembliENSMUST00000064924; ENSMUSP00000064465; ENSMUSG00000058290.
GeneIDi105988.
KEGGimmu:105988.
UCSCiuc007xvf.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
 AK129072 mRNA. Translation: BAC97882.1 . Different initiation.
BC145846 mRNA. Translation: AAI45847.1 .
CCDSi CCDS27878.1.
RefSeqi NP_001014976.1. NM_001014976.2.
XP_006520320.1. XM_006520257.1.
XP_006520321.1. XM_006520258.1.
XP_006520322.1. XM_006520259.1.
UniGenei Mm.288324.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 222968. 5 interactions.
IntActi P60330. 5 interactions.
STRINGi 10090.ENSMUSP00000064465.

Protein family/group databases

MEROPSi C50.002.

PTM databases

PhosphoSitei P60330.

Proteomic databases

MaxQBi P60330.
PaxDbi P60330.
PRIDEi P60330.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000064924 ; ENSMUSP00000064465 ; ENSMUSG00000058290 .
GeneIDi 105988.
KEGGi mmu:105988.
UCSCi uc007xvf.2. mouse.

Organism-specific databases

CTDi 9700.
MGIi MGI:2146156. Espl1.
Rougei Search...

Phylogenomic databases

eggNOGi COG5155.
GeneTreei ENSGT00390000004990.
HOGENOMi HOG000290657.
HOVERGENi HBG051510.
InParanoidi P60330.
KOi K02365.
OMAi ELAQVLC.
OrthoDBi EOG7PCJGQ.
PhylomeDBi P60330.
TreeFami TF101169.

Enzyme and pathway databases

Reactomei REACT_207679. Separation of Sister Chromatids.

Miscellaneous databases

NextBioi 357998.
PROi P60330.
SOURCEi Search...

Gene expression databases

Bgeei P60330.
CleanExi MM_ESPL1.
Genevestigatori P60330.

Family and domain databases

InterProi IPR005314. Peptidase_C50.
IPR030397. SEPARIN_core_dom.
[Graphical view ]
PANTHERi PTHR12792. PTHR12792. 1 hit.
Pfami PF03568. Peptidase_C50. 1 hit.
[Graphical view ]
PROSITEi PS51700. SEPARIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
    DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Embryonic tail.
  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].
    Tissue: Brain.
  3. Lubec G., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 1241-1260, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  4. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Entry informationi

Entry nameiESPL1_MOUSE
AccessioniPrimary (citable) accession number: P60330
Secondary accession number(s): A6H6E3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 2, 2004
Last sequence update: February 2, 2004
Last modified: January 7, 2015
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. 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.
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