Q14674 (ESPL1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	2120 AA.
Sequence status	Complete.
Protein existence	Evidence 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	Belongs to the peptidase C50 family.

Ontologies

Keywords
Biological process	Chromosome partition
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Molecular function	Hydrolase Protease Thiol protease
PTM	Autocatalytic cleavage Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic 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: Compara meiotic spindle organization Inferred from electronic annotation. Source: Compara mitotic anaphase Inferred from electronic annotation. Source: Compara 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 proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	centrosome Inferred from direct assay PubMed 12672959. Source: UniProtKB cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	cysteine-type peptidase activity Non-traceable author statement PubMed 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 2120	2120	Separin		PRO_0000205900
Sites
	Active site	2029	1
	Site	1506 – 1507	2	Cleavage; by autolysis
	Site	1535 – 1536	2	Cleavage; by autolysis
Amino acid modifications
	Modified residue	1126	1	Phosphoserine Ref.5
	Modified residue	1396	1	Phosphoserine Ref.8 Ref.9
	Modified residue	1399	1	Phosphoserine Ref.8 Ref.9
	Modified residue	1508	1	Phosphoserine Ref.8 Ref.10
Natural variations
	Alternative sequence	1 – 325	325	Missing in isoform 2.		VSP_009361
	Natural variant	614	1	S → R. Corresponds to variant rs1318648 [ dbSNP | Ensembl ].		VAR_057703
	Natural variant	699	1	R → Q. Corresponds to variant rs34424268 [ dbSNP | Ensembl ].		VAR_057704
	Natural variant	1136	1	I → V. Corresponds to variant rs34130634 [ dbSNP | Ensembl ].		VAR_057705
	Natural variant	1157	1	T → A. Corresponds to variant rs35428211 [ dbSNP | Ensembl ].		VAR_057706
	Natural variant	1237	1	Q → H. Corresponds to variant rs34396464 [ dbSNP | Ensembl ].		VAR_057707
	Natural variant	1435	1	K → M. Corresponds to variant rs1110719 [ dbSNP | Ensembl ].		VAR_057708
Experimental info
	Mutagenesis	1126	1	S → A: Abolishes phosphorylation at this site, as well as the negative regulation due to phosphorylation.
	Mutagenesis	1483 – 1486	4	EIMR → 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
	Mutagenesis	1486	1	R → A: Abolishes autocleavage; when associated with A-1181 and A-1210. Ref.6
	Mutagenesis	1503 – 1506	4	EILR → RILE: Does not affect autocleavage. Does not affect the protease function. Ref.1 Ref.6
	Mutagenesis	1506	1	R → A: Abolishes autocleavage; when associated with A-1161 and A-1210. Ref.6
	Mutagenesis	1532 – 1535	4	ELLR → RLLE: Strongly reduces autocleavage at this site, but enhances autocleavage at site 1. Does not affect the protease function. Ref.1 Ref.6
	Mutagenesis	1535	1	R → A: Abolishes autocleavage; when associated with A-1161 and A-1281. Ref.6
	Mutagenesis	2029	1	C → A: Abolishes protease activity. Ref.1
	Sequence conflict	25	1	A → D in AAR18247. Ref.1
	Sequence conflict	116	1	A → V in AAR18247. Ref.1
	Sequence conflict	693	1	M → I in AAR18247. Ref.1
	Sequence conflict	693	1	M → I in BAA11482. Ref.2
	Sequence conflict	1329	1	R → S in AAR18247. Ref.1
	Sequence conflict	1329	1	R → S in BAA11482. Ref.2
	Sequence conflict	1561	1	R → Q in AAR18247. Ref.1
	Sequence conflict	1561	1	R → Q in BAA11482. Ref.2
	Sequence conflict	2037	1	R → H in AAR18247. Ref.1
	Sequence conflict	2037	1	R → H in BAA11482. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 5, 2010. Version 3. Checksum: 0257A69093B4954C	FASTA	2,120	233,175
	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
	Isoform 2 [UniParc]. Checksum: 47FC0C2740C5A400	FASTA	1,795	197,745
	10 20 30 40 50 60 MEAPSPPLRA LYESCQFFLS GLERGTKRRY RLDAILSLFA FLGGYCSLLQ QLRDDGVYGG 70 80 90 100 110 120 SSKQQQSFLQ MYFQGLHLYT VVVYDFAQGC QIVDLADLTQ LVDSCKSTVV WMLEALEGLS 130 140 150 160 170 180 GQELTDHMGM TASYTSNLAY SFYSHKLYAE ACAISEPLCQ HLGLVKPGTY PEVPPEKLHR 190 200 210 220 230 240 CFRLQVESLK KLGKQAQGCK MVILWLAALQ PCSPEHMAEP VTFWVRVKMD AARAGDKELQ 250 260 270 280 290 300 LKTLRDSLSG WDPETLALLL REELQAYKAV RADTGQERFN IICDLLELSP EETPAGAWAR 310 320 330 340 350 360 ATHLVELAQV LCYHDFTQQT NCSALDAIRE ALQLLDSVRP EAQARDQLLD DKAQALLWLY 370 380 390 400 410 420 ICTLEAKMQE GIERDRRAQA PGNLEEFEVN DLNYEDKLQE DRFLYSNIAF NLAADAAQSK 430 440 450 460 470 480 CLDQALALWK ELLTKGQAPA VRCLQQTAAS LQILAALYQL VAKPMQALEV LLLLRIVSER 490 500 510 520 530 540 LKDHSKAAGS SCHITQLLLT LGCPSYAQLH LEEAASSLKH LDQTTDTYLL LSLTCDLLRS 550 560 570 580 590 600 QLYWTHQKVT KGVSLLLSVL RDPALQKSSK AWYLLRVQVL QLVAAYLSLP SNNLSHSLWE 610 620 630 640 650 660 QLCAQGWQTP EIALIDSHKL LRSIILLLMG SDILSTQKAA VETSFLDYGE NLVQKWQVLS 670 680 690 700 710 720 EVLSCSEKLV CHLGRLGSVS EAKAFCLEAL KLTTKLQIPR QCALFLVLKG ELELARNDID 730 740 750 760 770 780 LCQSDLQQVL FLLESCTEFG GVTQHLDSVK KVHLQKGKQQ AQVPCPPQLP EEELFLRGPA 790 800 810 820 830 840 LELVATVAKE PGPIAPSTNS SPVLKTKPQP IPNFLSHSPT CDCSLCASPV LTAVCLRWVL 850 860 870 880 890 900 VTAGVRLAMG HQAQGLDLLQ VVLKGCPEAA ERLTQALQAS LNHKTPPSLV PSLLDEILAQ 910 920 930 940 950 960 AYTLLALEGL NQPSNESLQK VLQSGLKFVA ARIPHLEPWR ASLLLIWALT KLGGLSCCTT 970 980 990 1000 1010 1020 QLFASSWGWQ PPLIKSVPGS EPSKTQGQKR SGRGRQKLAS APLRLNNTSQ KGLEGRGLPC 1030 1040 1050 1060 1070 1080 TPKPPDRIRQ AGPHVPFTVF EEVCPTESKP EVPQAPRVQQ RVQTRLKVNF SDDSDLEDPV 1090 1100 1110 1120 1130 1140 SAEAWLAEEP KRRGTASRGR GRARKGLSLK TDAVVAPGSA PGNPGLNGRS RRAKKVASRH 1150 1160 1170 1180 1190 1200 CEERRPQRAS DQARPGPEIM RTIPEEELTD NWRKMSFEIL RGSDGEDSAS GGKTPAPGPE 1210 1220 1230 1240 1250 1260 AASGEWELLR LDSSKKKLPS PCPDKESDKD LGPRLRLPSA PVATGLSTLD SICDSLSVAF 1270 1280 1290 1300 1310 1320 RGISHCPPSG LYAHLCRFLA LCLGHRDPYA TAFLVTESVS ITCRHQLLTH LHRQLSKAQK 1330 1340 1350 1360 1370 1380 HRGSLEIADQ LQGLSLQEMP GDVPLARIQR LFSFRALESG HFPQPEKESF QERLALIPSG 1390 1400 1410 1420 1430 1440 VTVCVLALAT LQPGTVGNTL LLTRLEKDSP PVSVQIPTGQ NKLHLRSVLN EFDAIQKAQK 1450 1460 1470 1480 1490 1500 ENSSCTDKRE WWTGRLALDH RMEVLIASLE KSVLGCWKGL LLPSSEEPGP AQEASRLQEL 1510 1520 1530 1540 1550 1560 LQDCGWKYPD RTLLKIMLSG AGALTPQDIQ ALAYGLCPTQ PERAQELLNE AVGRLQGLTV 1570 1580 1590 1600 1610 1620 PSNSHLVLVL DKDLQKLPWE SMPSLQALPV TRLPSFRFLL SYSIIKEYGA SPVLSQGVDP 1630 1640 1650 1660 1670 1680 RSTFYVLNPH NNLSSTEEQF RANFSSEAGW RGVVGEVPRP EQVQEALTKH DLYIYAGHGA 1690 1700 1710 1720 1730 1740 GARFLDGQAV LRLSCRAVAL LFGCSSAALA VRGNLEGAGI VLKYIMAGCP LFLGNLWDVT 1750 1760 1770 1780 1790 DRDIDRYTEA LLQGWLGAGP GAPLLYYVNQ ARQAPRLKYL IGAAPIAYGL PVSLR

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[10]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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.
IPI	IPI00017538. IPI00397474.
RefSeq	NP_036423.4. NM_012291.4.
UniGene	Hs.153479.
3D structure databases
ProteinModelPortal	Q14674.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-46079N.
IntAct	Q14674. 3 interactions.
STRING	9606.ENSP00000257934.
Protein family/group databases
MEROPS	C50.002.
PTM databases
PhosphoSite	Q14674.
Polymorphism databases
DMDM	308153600.
Proteomic databases
PaxDb	Q14674.
PRIDE	Q14674.
Protocols and materials databases
DNASU	9700.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000257934; ENSP00000257934; ENSG00000135476. ENST00000552462; ENSP00000449831; ENSG00000135476.
GeneID	9700.
KEGG	hsa:9700.
UCSC	uc001scj.2. human.
Organism-specific databases
CTD	9700.
GeneCards	GC12P053662.
H-InvDB	HIX0201902.
HGNC	HGNC:16856. ESPL1.
HPA	CAB012185.
MIM	604143. gene.
neXtProt	NX_Q14674.
PharmGKB	PA27884.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5155.
HOGENOM	HOG000290657.
HOVERGEN	HBG051510.
InParanoid	Q14674.
KO	K02365.
OMA	LALCLGH.
OrthoDB	EOG47H5P4.
PhylomeDB	Q14674.
Enzyme and pathway databases
BioCyc	MetaCyc:ENSG00000135476-MONOMER.
Reactome	REACT_115566. Cell Cycle. REACT_21300. Mitotic M-M/G1 phases.
Gene expression databases
ArrayExpress	Q14674.
Bgee	Q14674.
CleanEx	HS_ESPL1.
Genevestigator	Q14674.
GermOnline	ENSG00000135476. Homo sapiens.
Family and domain databases
InterPro	IPR005314. Peptidase_C50. [Graphical view]
PANTHER	PTHR12792. PTHR12792. 1 hit.
Pfam	PF03568. Peptidase_C50. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	ESPL1. human.
GenomeRNAi	9700.
NextBio	36451.
SOURCE	Search...

Entry information

Entry name

ESPL1_HUMAN

Accession

Primary (citable) accession number: Q14674

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 25, 2003
Last sequence update:	October 5, 2010
Last modified:	April 3, 2013
This is version 125 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.