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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

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
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-KW
  3. nucleus Source: UniProtKB-KW
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.
[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.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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.
[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].

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: October 29, 2014
This is version 86 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