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Q14674

- ESPL1_HUMAN

UniProt

Q14674 - ESPL1_HUMAN

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Protein

Separin

Gene
ESPL1, ESP1, KIAA0165
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
  3. protein binding 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-SubCell
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. 2 Publications
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. 2 Publications
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. 2 Publications
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.1 Publication

Keywords - PTMi

Autocatalytic cleavage, Phosphoprotein

Proteomic databases

MaxQBiQ14674.
PaxDbiQ14674.
PRIDEiQ14674.

PTM databases

PhosphoSiteiQ14674.

Expressioni

Gene expression databases

ArrayExpressiQ14674.
BgeeiQ14674.
CleanExiHS_ESPL1.
GenevestigatoriQ14674.

Organism-specific databases

HPAiCAB012185.

Interactioni

Subunit structurei

Interacts with PTTG1. Interacts with RAD21.2 Publications

Protein-protein interaction databases

BioGridi115052. 11 interactions.
DIPiDIP-46079N.
IntActiQ14674. 3 interactions.
STRINGi9606.ENSP00000257934.

Structurei

3D structure databases

ProteinModelPortaliQ14674.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG5155.
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

MRSFKRVNFG TLLSSQKEAE ELLPALKEFL SNPPAGFPSS RSDAERRQAC     50
DAILRACNQQ LTAKLACPRH LGSLLELAEL ACDGYLVSTP QRPPLYLERI 100
LFVLLRNAAA QGSPEATLRL AQPLHACLVQ CSREAAPQDY EAVARGSFSL 150
LWKGAEALLE RRAAFAARLK ALSFLVLLED ESTPCEVPHF ASPTACRAVA 200
AHQLFDASGH GLNEADADFL DDLLSRHVIR ALVGERGSSS GLLSPQRALC 250
LLELTLEHCR RFCWSRHHDK AISAVEKAHS YLRNTNLAPS LQLCQLGVKL 300
LQVGEEGPQA VAKLLIKASA VLSKSMEAPS PPLRALYESC QFFLSGLERG 350
TKRRYRLDAI LSLFAFLGGY CSLLQQLRDD GVYGGSSKQQ QSFLQMYFQG 400
LHLYTVVVYD FAQGCQIVDL ADLTQLVDSC KSTVVWMLEA LEGLSGQELT 450
DHMGMTASYT SNLAYSFYSH KLYAEACAIS EPLCQHLGLV KPGTYPEVPP 500
EKLHRCFRLQ VESLKKLGKQ AQGCKMVILW LAALQPCSPE HMAEPVTFWV 550
RVKMDAARAG DKELQLKTLR DSLSGWDPET LALLLREELQ AYKAVRADTG 600
QERFNIICDL LELSPEETPA GAWARATHLV ELAQVLCYHD FTQQTNCSAL 650
DAIREALQLL DSVRPEAQAR DQLLDDKAQA LLWLYICTLE AKMQEGIERD 700
RRAQAPGNLE EFEVNDLNYE DKLQEDRFLY SNIAFNLAAD AAQSKCLDQA 750
LALWKELLTK GQAPAVRCLQ QTAASLQILA ALYQLVAKPM QALEVLLLLR 800
IVSERLKDHS KAAGSSCHIT QLLLTLGCPS YAQLHLEEAA SSLKHLDQTT 850
DTYLLLSLTC DLLRSQLYWT HQKVTKGVSL LLSVLRDPAL QKSSKAWYLL 900
RVQVLQLVAA YLSLPSNNLS HSLWEQLCAQ GWQTPEIALI DSHKLLRSII 950
LLLMGSDILS TQKAAVETSF LDYGENLVQK WQVLSEVLSC SEKLVCHLGR 1000
LGSVSEAKAF CLEALKLTTK LQIPRQCALF LVLKGELELA RNDIDLCQSD 1050
LQQVLFLLES CTEFGGVTQH LDSVKKVHLQ KGKQQAQVPC PPQLPEEELF 1100
LRGPALELVA TVAKEPGPIA PSTNSSPVLK TKPQPIPNFL SHSPTCDCSL 1150
CASPVLTAVC LRWVLVTAGV RLAMGHQAQG LDLLQVVLKG CPEAAERLTQ 1200
ALQASLNHKT PPSLVPSLLD EILAQAYTLL ALEGLNQPSN ESLQKVLQSG 1250
LKFVAARIPH LEPWRASLLL IWALTKLGGL SCCTTQLFAS SWGWQPPLIK 1300
SVPGSEPSKT QGQKRSGRGR QKLASAPLRL NNTSQKGLEG RGLPCTPKPP 1350
DRIRQAGPHV PFTVFEEVCP TESKPEVPQA PRVQQRVQTR LKVNFSDDSD 1400
LEDPVSAEAW LAEEPKRRGT ASRGRGRARK GLSLKTDAVV APGSAPGNPG 1450
LNGRSRRAKK VASRHCEERR PQRASDQARP GPEIMRTIPE EELTDNWRKM 1500
SFEILRGSDG EDSASGGKTP APGPEAASGE WELLRLDSSK KKLPSPCPDK 1550
ESDKDLGPRL RLPSAPVATG LSTLDSICDS LSVAFRGISH CPPSGLYAHL 1600
CRFLALCLGH RDPYATAFLV TESVSITCRH QLLTHLHRQL SKAQKHRGSL 1650
EIADQLQGLS LQEMPGDVPL ARIQRLFSFR ALESGHFPQP EKESFQERLA 1700
LIPSGVTVCV LALATLQPGT VGNTLLLTRL EKDSPPVSVQ IPTGQNKLHL 1750
RSVLNEFDAI QKAQKENSSC TDKREWWTGR LALDHRMEVL IASLEKSVLG 1800
CWKGLLLPSS EEPGPAQEAS RLQELLQDCG WKYPDRTLLK IMLSGAGALT 1850
PQDIQALAYG LCPTQPERAQ ELLNEAVGRL QGLTVPSNSH LVLVLDKDLQ 1900
KLPWESMPSL QALPVTRLPS FRFLLSYSII KEYGASPVLS QGVDPRSTFY 1950
VLNPHNNLSS TEEQFRANFS SEAGWRGVVG EVPRPEQVQE ALTKHDLYIY 2000
AGHGAGARFL DGQAVLRLSC RAVALLFGCS SAALAVRGNL EGAGIVLKYI 2050
MAGCPLFLGN LWDVTDRDID RYTEALLQGW LGAGPGAPLL YYVNQARQAP 2100
RLKYLIGAAP IAYGLPVSLR 2120
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

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. VSP_009361Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti25 – 251A → D in AAR18247. 1 Publication
Sequence conflicti116 – 1161A → V in AAR18247. 1 Publication
Sequence conflicti693 – 6931M → I in AAR18247. 1 Publication
Sequence conflicti693 – 6931M → I in BAA11482. 1 Publication
Sequence conflicti1329 – 13291R → S in AAR18247. 1 Publication
Sequence conflicti1329 – 13291R → S in BAA11482. 1 Publication
Sequence conflicti1561 – 15611R → Q in AAR18247. 1 Publication
Sequence conflicti1561 – 15611R → Q in BAA11482. 1 Publication
Sequence conflicti2037 – 20371R → H in AAR18247. 1 Publication
Sequence conflicti2037 – 20371R → H in BAA11482. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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. 11 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.
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

ArrayExpressi Q14674.
Bgeei Q14674.
CleanExi HS_ESPL1.
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: September 3, 2014
This is version 137 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

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