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Q14674 (ESPL1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Separin

EC=3.4.22.49
Alternative name(s):
Caspase-like protein ESPL1
Extra spindle poles-like 1 protein
Separase
Gene names
Name:ESPL1
Synonyms:ESP1, KIAA0165
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2120 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.4 Ref.7

Catalytic activity

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 regulation

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-1126 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. Ref.1 Ref.5 Ref.6

Subunit structure

Interacts with PTTG1. Interacts with RAD21. Ref.4 Ref.7

Subcellular location

Cytoplasm. Nucleus.

Post-translational modification

Autocleaves. This function, which is not essential for its protease activity, is unknown.

Phosphorylated by CDK1. There are 8 Ser/Thr phosphorylation sites. Among them, Ser-1126 phosphorylation is the major site, which conducts to the enzyme inactivation. Ref.5

Sequence similarities

Contains 1 peptidase C50 domain.

Ontologies

Keywords
   Biological processChromosome partition
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   Molecular functionHydrolase
Protease
Thiol protease
   PTMAutocatalytic cleavage
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic process

Traceable author statement PubMed 11875078. Source: UniProtKB

cytokinesis

Non-traceable author statement Ref.7. Source: UniProtKB

establishment of mitotic spindle localization

Non-traceable author statement PubMed 12672959. Source: UniProtKB

homologous chromosome segregation

Inferred from electronic annotation. Source: Ensembl

meiotic spindle organization

Inferred from electronic annotation. Source: Ensembl

mitotic cell cycle

Traceable author statement. Source: Reactome

mitotic sister chromatid segregation

Inferred from mutant phenotype PubMed 12672959. Source: UniProtKB

negative regulation of sister chromatid cohesion

Non-traceable author statement Ref.1. Source: UniProtKB

positive regulation of mitotic metaphase/anaphase transition

Non-traceable author statement PubMed 12672959. Source: UniProtKB

   Cellular_componentcentrosome

Inferred from direct assay PubMed 12672959. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncatalytic activity

Non-traceable author statement PubMed 12672959. Source: UniProtKB

cysteine-type peptidase activity

Non-traceable author statement PubMed 12672959. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.1PubMed 12672959. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q14674-1)

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.
Isoform 2 (identifier: Q14674-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-325: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 21202120Separin
PRO_0000205900

Regions

Domain1945 – 204096Peptidase C50

Sites

Active site20291
Site1506 – 15072Cleavage; by autolysis
Site1535 – 15362Cleavage; by autolysis

Amino acid modifications

Modified residue11261Phosphoserine Ref.5
Modified residue13961Phosphoserine Ref.8 Ref.10
Modified residue13991Phosphoserine Ref.8 Ref.10
Modified residue15081Phosphoserine Ref.8 Ref.11

Natural variations

Alternative sequence1 – 325325Missing in isoform 2.
VSP_009361
Natural variant6141S → R.
Corresponds to variant rs1318648 [ dbSNP | Ensembl ].
VAR_057703
Natural variant6991R → Q.
Corresponds to variant rs34424268 [ dbSNP | Ensembl ].
VAR_057704
Natural variant11361I → V.
Corresponds to variant rs34130634 [ dbSNP | Ensembl ].
VAR_057705
Natural variant11571T → A.
Corresponds to variant rs35428211 [ dbSNP | Ensembl ].
VAR_057706
Natural variant12371Q → H.
Corresponds to variant rs34396464 [ dbSNP | Ensembl ].
VAR_057707
Natural variant14351K → M.
Corresponds to variant rs1110719 [ dbSNP | Ensembl ].
VAR_057708

Experimental info

Mutagenesis11261S → A: Abolishes phosphorylation at this site, as well as the negative regulation due to phosphorylation.
Mutagenesis1483 – 14864EIMR → RIME: Abolishes autocleavage; when associated with R-1178; E-1181; R-1207 and E-1210. Does not affect the protease function. Ref.1 Ref.6
Mutagenesis14861R → A: Abolishes autocleavage; when associated with A-1181 and A-1210. Ref.6
Mutagenesis1503 – 15064EILR → RILE: Does not affect autocleavage. Does not affect the protease function. Ref.1 Ref.6
Mutagenesis15061R → A: Abolishes autocleavage; when associated with A-1161 and A-1210. Ref.6
Mutagenesis1532 – 15354ELLR → RLLE: Strongly reduces autocleavage at this site, but enhances autocleavage at site 1. Does not affect the protease function. Ref.1 Ref.6
Mutagenesis15351R → A: Abolishes autocleavage; when associated with A-1161 and A-1281. Ref.6
Mutagenesis20291C → A: Abolishes protease activity. Ref.1
Sequence conflict251A → D in AAR18247. Ref.1
Sequence conflict1161A → V in AAR18247. Ref.1
Sequence conflict6931M → I in AAR18247. Ref.1
Sequence conflict6931M → I in BAA11482. Ref.2
Sequence conflict13291R → S in AAR18247. Ref.1
Sequence conflict13291R → S in BAA11482. Ref.2
Sequence conflict15611R → Q in AAR18247. Ref.1
Sequence conflict15611R → Q in BAA11482. Ref.2
Sequence conflict20371R → H in AAR18247. Ref.1
Sequence conflict20371R → H in BAA11482. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 5, 2010. Version 3.
Checksum: 0257A69093B4954C

FASTA2,120233,175
        10         20         30         40         50         60 
MRSFKRVNFG TLLSSQKEAE ELLPALKEFL SNPPAGFPSS RSDAERRQAC DAILRACNQQ 

        70         80         90        100        110        120 
LTAKLACPRH LGSLLELAEL ACDGYLVSTP QRPPLYLERI LFVLLRNAAA QGSPEATLRL 

       130        140        150        160        170        180 
AQPLHACLVQ CSREAAPQDY EAVARGSFSL LWKGAEALLE RRAAFAARLK ALSFLVLLED 

       190        200        210        220        230        240 
ESTPCEVPHF ASPTACRAVA AHQLFDASGH GLNEADADFL DDLLSRHVIR ALVGERGSSS 

       250        260        270        280        290        300 
GLLSPQRALC LLELTLEHCR RFCWSRHHDK AISAVEKAHS YLRNTNLAPS LQLCQLGVKL 

       310        320        330        340        350        360 
LQVGEEGPQA VAKLLIKASA VLSKSMEAPS PPLRALYESC QFFLSGLERG TKRRYRLDAI 

       370        380        390        400        410        420 
LSLFAFLGGY CSLLQQLRDD GVYGGSSKQQ QSFLQMYFQG LHLYTVVVYD FAQGCQIVDL 

       430        440        450        460        470        480 
ADLTQLVDSC KSTVVWMLEA LEGLSGQELT DHMGMTASYT SNLAYSFYSH KLYAEACAIS 

       490        500        510        520        530        540 
EPLCQHLGLV KPGTYPEVPP EKLHRCFRLQ VESLKKLGKQ AQGCKMVILW LAALQPCSPE 

       550        560        570        580        590        600 
HMAEPVTFWV RVKMDAARAG DKELQLKTLR DSLSGWDPET LALLLREELQ AYKAVRADTG 

       610        620        630        640        650        660 
QERFNIICDL LELSPEETPA GAWARATHLV ELAQVLCYHD FTQQTNCSAL DAIREALQLL 

       670        680        690        700        710        720 
DSVRPEAQAR DQLLDDKAQA LLWLYICTLE AKMQEGIERD RRAQAPGNLE EFEVNDLNYE 

       730        740        750        760        770        780 
DKLQEDRFLY SNIAFNLAAD AAQSKCLDQA LALWKELLTK GQAPAVRCLQ QTAASLQILA 

       790        800        810        820        830        840 
ALYQLVAKPM QALEVLLLLR IVSERLKDHS KAAGSSCHIT QLLLTLGCPS YAQLHLEEAA 

       850        860        870        880        890        900 
SSLKHLDQTT DTYLLLSLTC DLLRSQLYWT HQKVTKGVSL LLSVLRDPAL QKSSKAWYLL 

       910        920        930        940        950        960 
RVQVLQLVAA YLSLPSNNLS HSLWEQLCAQ GWQTPEIALI DSHKLLRSII LLLMGSDILS 

       970        980        990       1000       1010       1020 
TQKAAVETSF LDYGENLVQK WQVLSEVLSC SEKLVCHLGR LGSVSEAKAF CLEALKLTTK 

      1030       1040       1050       1060       1070       1080 
LQIPRQCALF LVLKGELELA RNDIDLCQSD LQQVLFLLES CTEFGGVTQH LDSVKKVHLQ 

      1090       1100       1110       1120       1130       1140 
KGKQQAQVPC PPQLPEEELF LRGPALELVA TVAKEPGPIA PSTNSSPVLK TKPQPIPNFL 

      1150       1160       1170       1180       1190       1200 
SHSPTCDCSL CASPVLTAVC LRWVLVTAGV RLAMGHQAQG LDLLQVVLKG CPEAAERLTQ 

      1210       1220       1230       1240       1250       1260 
ALQASLNHKT PPSLVPSLLD EILAQAYTLL ALEGLNQPSN ESLQKVLQSG LKFVAARIPH 

      1270       1280       1290       1300       1310       1320 
LEPWRASLLL IWALTKLGGL SCCTTQLFAS SWGWQPPLIK SVPGSEPSKT QGQKRSGRGR 

      1330       1340       1350       1360       1370       1380 
QKLASAPLRL NNTSQKGLEG RGLPCTPKPP DRIRQAGPHV PFTVFEEVCP TESKPEVPQA 

      1390       1400       1410       1420       1430       1440 
PRVQQRVQTR LKVNFSDDSD LEDPVSAEAW LAEEPKRRGT ASRGRGRARK GLSLKTDAVV 

      1450       1460       1470       1480       1490       1500 
APGSAPGNPG LNGRSRRAKK VASRHCEERR PQRASDQARP GPEIMRTIPE EELTDNWRKM 

      1510       1520       1530       1540       1550       1560 
SFEILRGSDG EDSASGGKTP APGPEAASGE WELLRLDSSK KKLPSPCPDK ESDKDLGPRL 

      1570       1580       1590       1600       1610       1620 
RLPSAPVATG LSTLDSICDS LSVAFRGISH CPPSGLYAHL CRFLALCLGH RDPYATAFLV 

      1630       1640       1650       1660       1670       1680 
TESVSITCRH QLLTHLHRQL SKAQKHRGSL EIADQLQGLS LQEMPGDVPL ARIQRLFSFR 

      1690       1700       1710       1720       1730       1740 
ALESGHFPQP EKESFQERLA LIPSGVTVCV LALATLQPGT VGNTLLLTRL EKDSPPVSVQ 

      1750       1760       1770       1780       1790       1800 
IPTGQNKLHL RSVLNEFDAI QKAQKENSSC TDKREWWTGR LALDHRMEVL IASLEKSVLG 

      1810       1820       1830       1840       1850       1860 
CWKGLLLPSS EEPGPAQEAS RLQELLQDCG WKYPDRTLLK IMLSGAGALT PQDIQALAYG 

      1870       1880       1890       1900       1910       1920 
LCPTQPERAQ ELLNEAVGRL QGLTVPSNSH LVLVLDKDLQ KLPWESMPSL QALPVTRLPS 

      1930       1940       1950       1960       1970       1980 
FRFLLSYSII KEYGASPVLS QGVDPRSTFY VLNPHNNLSS TEEQFRANFS SEAGWRGVVG 

      1990       2000       2010       2020       2030       2040 
EVPRPEQVQE ALTKHDLYIY AGHGAGARFL DGQAVLRLSC RAVALLFGCS SAALAVRGNL 

      2050       2060       2070       2080       2090       2100 
EGAGIVLKYI MAGCPLFLGN LWDVTDRDID RYTEALLQGW LGAGPGAPLL YYVNQARQAP 

      2110       2120 
RLKYLIGAAP IAYGLPVSLR 

« Hide

Isoform 2 [UniParc].

Checksum: 47FC0C2740C5A400
Show »

FASTA1,795197,745

References

« Hide 'large scale' references
[1]"Regulation of human separase by securin binding and autocleavage."
Waizenegger I., Gimenez-Abian J.F., Wernic D., Peters J.-M.
Curr. Biol. 12:1368-1378(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ENZYME REGULATION, AUTOCATALYTIC CLEAVAGE, MUTAGENESIS OF CYS-2029; 1483-GLU--ARG-1486; 1503-GLU--ARG-1506 AND 1532-GLU--ARG-1535.
[2]"Prediction of the coding sequences of unidentified human genes. V. The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of cDNA clones from human cell line KG-1."
Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.
DNA Res. 3:17-24(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Bone marrow.
[3]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"Identification of a vertebrate sister-chromatid separation inhibitor involved in transformation and tumorigenesis."
Zou H., McGarry T.J., Bernal T., Kirschner M.W.
Science 285:418-422(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH PTTG1.
[5]"Dual inhibition of sister chromatid separation at metaphase."
Stemmann O., Zou H., Gerber S.A., Gygi S.P., Kirschner M.W.
Cell 107:715-726(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1117-1130, ENZYME REGULATION, PHOSPHORYLATION AT SER-1126.
[6]"Anaphase specific auto-cleavage of separase."
Zou H., Stemman O., Anderson J.S., Mann M., Kirschner M.W.
FEBS Lett. 528:246-250(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1507-1517, ENZYME REGULATION, AUTOCATALYTIC CLEAVAGE, MUTAGENESIS OF ARG-1486; ARG-1506 AND ARG-1535.
[7]"Cohesin cleavage by separase required for anaphase and cytokinesis in human cells."
Hauf S., Waizenegger I.C., Peters J.-M.
Science 293:1320-1323(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RAD21.
[8]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1396; SER-1399 AND SER-1508, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1396 AND SER-1399, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[11]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1508, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY455930 mRNA. Translation: AAR18247.1.
D79987 mRNA. Translation: BAA11482.2.
AC021072 Genomic DNA. No translation available.
AC073611 Genomic DNA. No translation available.
CCDSCCDS8852.1. [Q14674-1]
RefSeqNP_036423.4. NM_012291.4. [Q14674-1]
XP_006719768.1. XM_006719705.1. [Q14674-1]
UniGeneHs.153479.

3D structure databases

ProteinModelPortalQ14674.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115052. 12 interactions.
DIPDIP-46079N.
IntActQ14674. 3 interactions.
STRING9606.ENSP00000257934.

Protein family/group databases

MEROPSC50.002.

PTM databases

PhosphoSiteQ14674.

Polymorphism databases

DMDM308153600.

Proteomic databases

MaxQBQ14674.
PaxDbQ14674.
PRIDEQ14674.

Protocols and materials databases

DNASU9700.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000257934; ENSP00000257934; ENSG00000135476. [Q14674-1]
ENST00000552462; ENSP00000449831; ENSG00000135476. [Q14674-1]
GeneID9700.
KEGGhsa:9700.
UCSCuc001scj.2. human. [Q14674-1]

Organism-specific databases

CTD9700.
GeneCardsGC12P053662.
H-InvDBHIX0201902.
HGNCHGNC:16856. ESPL1.
HPACAB012185.
MIM604143. gene.
neXtProtNX_Q14674.
PharmGKBPA27884.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5155.
HOGENOMHOG000290657.
HOVERGENHBG051510.
InParanoidQ14674.
KOK02365.
OMAELAQVLC.
OrthoDBEOG7PCJGQ.
PhylomeDBQ14674.
TreeFamTF101169.

Enzyme and pathway databases

BioCycMetaCyc:ENSG00000135476-MONOMER.
ReactomeREACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.

Gene expression databases

ArrayExpressQ14674.
BgeeQ14674.
CleanExHS_ESPL1.
GenevestigatorQ14674.

Family and domain databases

InterProIPR005314. Peptidase_C50.
[Graphical view]
PANTHERPTHR12792. PTHR12792. 1 hit.
PfamPF03568. Peptidase_C50. 1 hit.
[Graphical view]
PROSITEPS51700. SEPARIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSESPL1. human.
GeneWikiSeparase.
GenomeRNAi9700.
NextBio36451.
PROQ14674.
SOURCESearch...

Entry information

Entry nameESPL1_HUMAN
AccessionPrimary (citable) accession number: Q14674
Entry history
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: October 5, 2010
Last modified: July 9, 2014
This is version 136 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM