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Q14674

- ESPL1_HUMAN

UniProt

Q14674 - ESPL1_HUMAN

Protein

Separin

Gene

ESPL1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 3 (05 Oct 2010)
      Previous versions | rss
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    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

    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

    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.
    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.
    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.
    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

    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.
    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.
    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

    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:
    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

    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 1, 2014
    This is version 138 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