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Q14674

- ESPL1_HUMAN

UniProt

Q14674 - ESPL1_HUMAN

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Protein

Separin

Gene

ESPL1

Organism
Homo sapiens (Human)
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.2 Publications

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-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.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei1506 – 15072Cleavage; by autolysis
Sitei1535 – 15362Cleavage; by autolysis
Active sitei2029 – 20291

GO - Molecular functioni

  1. catalytic activity Source: UniProtKB
  2. cysteine-type peptidase activity Source: UniProtKB

GO - Biological processi

  1. apoptotic process Source: UniProtKB
  2. cytokinesis Source: UniProtKB
  3. establishment of mitotic spindle localization Source: UniProtKB
  4. homologous chromosome segregation Source: Ensembl
  5. meiotic spindle organization Source: Ensembl
  6. mitotic cell cycle Source: Reactome
  7. mitotic sister chromatid segregation Source: UniProtKB
  8. negative regulation of sister chromatid cohesion Source: UniProtKB
  9. positive regulation of mitotic metaphase/anaphase transition Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Chromosome partition

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000135476-MONOMER.
ReactomeiREACT_150471. 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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:16856. ESPL1.

Subcellular locationi

GO - Cellular componenti

  1. centrosome Source: UniProtKB
  2. cytosol Source: Reactome
  3. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1126 – 11261S → A: Abolishes phosphorylation at this site, as well as the negative regulation due to phosphorylation.
Mutagenesisi1483 – 14864EIMR → RIME: Abolishes autocleavage; when associated with R-1178; E-1181; R-1207 and E-1210. Does not affect the protease function. 1 Publication
Mutagenesisi1486 – 14861R → A: Abolishes autocleavage; when associated with A-1181 and A-1210. 1 Publication
Mutagenesisi1503 – 15064EILR → RILE: Does not affect autocleavage. Does not affect the protease function. 1 Publication
Mutagenesisi1506 – 15061R → A: Abolishes autocleavage; when associated with A-1161 and A-1210. 1 Publication
Mutagenesisi1532 – 15354ELLR → RLLE: Strongly reduces autocleavage at this site, but enhances autocleavage at site 1. Does not affect the protease function. 1 Publication
Mutagenesisi1535 – 15351R → A: Abolishes autocleavage; when associated with A-1161 and A-1281. 1 Publication
Mutagenesisi2029 – 20291C → A: Abolishes protease activity. 1 Publication

Organism-specific databases

PharmGKBiPA27884.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 21202120SeparinPRO_0000205900Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1126 – 11261Phosphoserine1 Publication
Modified residuei1396 – 13961Phosphoserine2 Publications
Modified residuei1399 – 13991Phosphoserine2 Publications
Modified residuei1508 – 15081Phosphoserine2 Publications

Post-translational modificationi

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.4 Publications

Keywords - PTMi

Autocatalytic cleavage, Phosphoprotein

Proteomic databases

MaxQBiQ14674.
PaxDbiQ14674.
PRIDEiQ14674.

PTM databases

PhosphoSiteiQ14674.

Expressioni

Gene expression databases

BgeeiQ14674.
CleanExiHS_ESPL1.
ExpressionAtlasiQ14674. baseline and differential.
GenevestigatoriQ14674.

Organism-specific databases

HPAiCAB012185.

Interactioni

Subunit structurei

Interacts with PTTG1. Interacts with RAD21.2 Publications

Protein-protein interaction databases

BioGridi115052. 15 interactions.
DIPiDIP-46079N.
IntActiQ14674. 3 interactions.
STRINGi9606.ENSP00000257934.

Structurei

3D structure databases

ProteinModelPortaliQ14674.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1945 – 204096Peptidase C50Add
BLAST

Sequence similaritiesi

Contains 1 peptidase C50 domain.Curated

Phylogenomic databases

eggNOGiCOG5155.
GeneTreeiENSGT00390000004990.
HOGENOMiHOG000290657.
HOVERGENiHBG051510.
InParanoidiQ14674.
KOiK02365.
OMAiELAQVLC.
OrthoDBiEOG7PCJGQ.
PhylomeDBiQ14674.
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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q14674-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MRSFKRVNFG TLLSSQKEAE ELLPALKEFL SNPPAGFPSS RSDAERRQAC
60 70 80 90 100
DAILRACNQQ LTAKLACPRH LGSLLELAEL ACDGYLVSTP QRPPLYLERI
110 120 130 140 150
LFVLLRNAAA QGSPEATLRL AQPLHACLVQ CSREAAPQDY EAVARGSFSL
160 170 180 190 200
LWKGAEALLE RRAAFAARLK ALSFLVLLED ESTPCEVPHF ASPTACRAVA
210 220 230 240 250
AHQLFDASGH GLNEADADFL DDLLSRHVIR ALVGERGSSS GLLSPQRALC
260 270 280 290 300
LLELTLEHCR RFCWSRHHDK AISAVEKAHS YLRNTNLAPS LQLCQLGVKL
310 320 330 340 350
LQVGEEGPQA VAKLLIKASA VLSKSMEAPS PPLRALYESC QFFLSGLERG
360 370 380 390 400
TKRRYRLDAI LSLFAFLGGY CSLLQQLRDD GVYGGSSKQQ QSFLQMYFQG
410 420 430 440 450
LHLYTVVVYD FAQGCQIVDL ADLTQLVDSC KSTVVWMLEA LEGLSGQELT
460 470 480 490 500
DHMGMTASYT SNLAYSFYSH KLYAEACAIS EPLCQHLGLV KPGTYPEVPP
510 520 530 540 550
EKLHRCFRLQ VESLKKLGKQ AQGCKMVILW LAALQPCSPE HMAEPVTFWV
560 570 580 590 600
RVKMDAARAG DKELQLKTLR DSLSGWDPET LALLLREELQ AYKAVRADTG
610 620 630 640 650
QERFNIICDL LELSPEETPA GAWARATHLV ELAQVLCYHD FTQQTNCSAL
660 670 680 690 700
DAIREALQLL DSVRPEAQAR DQLLDDKAQA LLWLYICTLE AKMQEGIERD
710 720 730 740 750
RRAQAPGNLE EFEVNDLNYE DKLQEDRFLY SNIAFNLAAD AAQSKCLDQA
760 770 780 790 800
LALWKELLTK GQAPAVRCLQ QTAASLQILA ALYQLVAKPM QALEVLLLLR
810 820 830 840 850
IVSERLKDHS KAAGSSCHIT QLLLTLGCPS YAQLHLEEAA SSLKHLDQTT
860 870 880 890 900
DTYLLLSLTC DLLRSQLYWT HQKVTKGVSL LLSVLRDPAL QKSSKAWYLL
910 920 930 940 950
RVQVLQLVAA YLSLPSNNLS HSLWEQLCAQ GWQTPEIALI DSHKLLRSII
960 970 980 990 1000
LLLMGSDILS TQKAAVETSF LDYGENLVQK WQVLSEVLSC SEKLVCHLGR
1010 1020 1030 1040 1050
LGSVSEAKAF CLEALKLTTK LQIPRQCALF LVLKGELELA RNDIDLCQSD
1060 1070 1080 1090 1100
LQQVLFLLES CTEFGGVTQH LDSVKKVHLQ KGKQQAQVPC PPQLPEEELF
1110 1120 1130 1140 1150
LRGPALELVA TVAKEPGPIA PSTNSSPVLK TKPQPIPNFL SHSPTCDCSL
1160 1170 1180 1190 1200
CASPVLTAVC LRWVLVTAGV RLAMGHQAQG LDLLQVVLKG CPEAAERLTQ
1210 1220 1230 1240 1250
ALQASLNHKT PPSLVPSLLD EILAQAYTLL ALEGLNQPSN ESLQKVLQSG
1260 1270 1280 1290 1300
LKFVAARIPH LEPWRASLLL IWALTKLGGL SCCTTQLFAS SWGWQPPLIK
1310 1320 1330 1340 1350
SVPGSEPSKT QGQKRSGRGR QKLASAPLRL NNTSQKGLEG RGLPCTPKPP
1360 1370 1380 1390 1400
DRIRQAGPHV PFTVFEEVCP TESKPEVPQA PRVQQRVQTR LKVNFSDDSD
1410 1420 1430 1440 1450
LEDPVSAEAW LAEEPKRRGT ASRGRGRARK GLSLKTDAVV APGSAPGNPG
1460 1470 1480 1490 1500
LNGRSRRAKK VASRHCEERR PQRASDQARP GPEIMRTIPE EELTDNWRKM
1510 1520 1530 1540 1550
SFEILRGSDG EDSASGGKTP APGPEAASGE WELLRLDSSK KKLPSPCPDK
1560 1570 1580 1590 1600
ESDKDLGPRL RLPSAPVATG LSTLDSICDS LSVAFRGISH CPPSGLYAHL
1610 1620 1630 1640 1650
CRFLALCLGH RDPYATAFLV TESVSITCRH QLLTHLHRQL SKAQKHRGSL
1660 1670 1680 1690 1700
EIADQLQGLS LQEMPGDVPL ARIQRLFSFR ALESGHFPQP EKESFQERLA
1710 1720 1730 1740 1750
LIPSGVTVCV LALATLQPGT VGNTLLLTRL EKDSPPVSVQ IPTGQNKLHL
1760 1770 1780 1790 1800
RSVLNEFDAI QKAQKENSSC TDKREWWTGR LALDHRMEVL IASLEKSVLG
1810 1820 1830 1840 1850
CWKGLLLPSS EEPGPAQEAS RLQELLQDCG WKYPDRTLLK IMLSGAGALT
1860 1870 1880 1890 1900
PQDIQALAYG LCPTQPERAQ ELLNEAVGRL QGLTVPSNSH LVLVLDKDLQ
1910 1920 1930 1940 1950
KLPWESMPSL QALPVTRLPS FRFLLSYSII KEYGASPVLS QGVDPRSTFY
1960 1970 1980 1990 2000
VLNPHNNLSS TEEQFRANFS SEAGWRGVVG EVPRPEQVQE ALTKHDLYIY
2010 2020 2030 2040 2050
AGHGAGARFL DGQAVLRLSC RAVALLFGCS SAALAVRGNL EGAGIVLKYI
2060 2070 2080 2090 2100
MAGCPLFLGN LWDVTDRDID RYTEALLQGW LGAGPGAPLL YYVNQARQAP
2110 2120
RLKYLIGAAP IAYGLPVSLR
Length:2,120
Mass (Da):233,175
Last modified:October 5, 2010 - v3
Checksum:i0257A69093B4954C
GO
Isoform 2 (identifier: Q14674-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-325: Missing.

Note: No experimental confirmation available.

Show »
Length:1,795
Mass (Da):197,745
Checksum:i47FC0C2740C5A400
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti25 – 251A → D in AAR18247. (PubMed:12194817)Curated
Sequence conflicti116 – 1161A → V in AAR18247. (PubMed:12194817)Curated
Sequence conflicti693 – 6931M → I in AAR18247. (PubMed:12194817)Curated
Sequence conflicti693 – 6931M → I in BAA11482. (PubMed:8724849)Curated
Sequence conflicti1329 – 13291R → S in AAR18247. (PubMed:12194817)Curated
Sequence conflicti1329 – 13291R → S in BAA11482. (PubMed:8724849)Curated
Sequence conflicti1561 – 15611R → Q in AAR18247. (PubMed:12194817)Curated
Sequence conflicti1561 – 15611R → Q in BAA11482. (PubMed:8724849)Curated
Sequence conflicti2037 – 20371R → H in AAR18247. (PubMed:12194817)Curated
Sequence conflicti2037 – 20371R → H in BAA11482. (PubMed:8724849)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti614 – 6141S → R.
Corresponds to variant rs1318648 [ dbSNP | Ensembl ].
VAR_057703
Natural varianti699 – 6991R → Q.
Corresponds to variant rs34424268 [ dbSNP | Ensembl ].
VAR_057704
Natural varianti1136 – 11361I → V.
Corresponds to variant rs34130634 [ dbSNP | Ensembl ].
VAR_057705
Natural varianti1157 – 11571T → A.
Corresponds to variant rs35428211 [ dbSNP | Ensembl ].
VAR_057706
Natural varianti1237 – 12371Q → H.
Corresponds to variant rs34396464 [ dbSNP | Ensembl ].
VAR_057707
Natural varianti1435 – 14351K → M.
Corresponds to variant rs1110719 [ dbSNP | Ensembl ].
VAR_057708

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 325325Missing in isoform 2. 1 PublicationVSP_009361Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY455930 mRNA. Translation: AAR18247.1.
D79987 mRNA. Translation: BAA11482.2.
AC021072 Genomic DNA. No translation available.
AC073611 Genomic DNA. No translation available.
CCDSiCCDS8852.1. [Q14674-1]
RefSeqiNP_036423.4. NM_012291.4. [Q14674-1]
XP_006719768.1. XM_006719705.1. [Q14674-1]
UniGeneiHs.153479.

Genome annotation databases

EnsembliENST00000257934; ENSP00000257934; ENSG00000135476. [Q14674-1]
ENST00000552462; ENSP00000449831; ENSG00000135476. [Q14674-1]
GeneIDi9700.
KEGGihsa:9700.
UCSCiuc001scj.2. human. [Q14674-1]

Polymorphism databases

DMDMi308153600.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY455930 mRNA. Translation: AAR18247.1 .
D79987 mRNA. Translation: BAA11482.2 .
AC021072 Genomic DNA. No translation available.
AC073611 Genomic DNA. No translation available.
CCDSi CCDS8852.1. [Q14674-1 ]
RefSeqi NP_036423.4. NM_012291.4. [Q14674-1 ]
XP_006719768.1. XM_006719705.1. [Q14674-1 ]
UniGenei Hs.153479.

3D structure databases

ProteinModelPortali Q14674.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115052. 15 interactions.
DIPi DIP-46079N.
IntActi Q14674. 3 interactions.
STRINGi 9606.ENSP00000257934.

Protein family/group databases

MEROPSi C50.002.

PTM databases

PhosphoSitei Q14674.

Polymorphism databases

DMDMi 308153600.

Proteomic databases

MaxQBi Q14674.
PaxDbi Q14674.
PRIDEi Q14674.

Protocols and materials databases

DNASUi 9700.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000257934 ; ENSP00000257934 ; ENSG00000135476 . [Q14674-1 ]
ENST00000552462 ; ENSP00000449831 ; ENSG00000135476 . [Q14674-1 ]
GeneIDi 9700.
KEGGi hsa:9700.
UCSCi uc001scj.2. human. [Q14674-1 ]

Organism-specific databases

CTDi 9700.
GeneCardsi GC12P053662.
H-InvDB HIX0201902.
HGNCi HGNC:16856. ESPL1.
HPAi CAB012185.
MIMi 604143. gene.
neXtProti NX_Q14674.
PharmGKBi PA27884.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5155.
GeneTreei ENSGT00390000004990.
HOGENOMi HOG000290657.
HOVERGENi HBG051510.
InParanoidi Q14674.
KOi K02365.
OMAi ELAQVLC.
OrthoDBi EOG7PCJGQ.
PhylomeDBi Q14674.
TreeFami TF101169.

Enzyme and pathway databases

BioCyci MetaCyc:ENSG00000135476-MONOMER.
Reactomei REACT_150471. Separation of Sister Chromatids.

Miscellaneous databases

ChiTaRSi ESPL1. human.
GeneWikii Separase.
GenomeRNAii 9700.
NextBioi 36451.
PROi Q14674.
SOURCEi Search...

Gene expression databases

Bgeei Q14674.
CleanExi HS_ESPL1.
ExpressionAtlasi Q14674. baseline and differential.
Genevestigatori Q14674.

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. "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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiESPL1_HUMAN
AccessioniPrimary (citable) accession number: Q14674
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: October 5, 2010
Last modified: October 29, 2014
This is version 139 of the entry and version 3 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: 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. Peptidase families
    Classification of peptidase families and list of entries
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3