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Protein

Securin

Gene

Pttg1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Regulatory protein, which plays a central role in chromosome stability, in the p53/TP53 pathway, and DNA repair. Probably acts by blocking the action of key proteins. During the mitosis, it blocks Separase/ESPL1 function, preventing the proteolysis of the cohesin complex and the subsequent segregation of the chromosomes. At the onset of anaphase, it is ubiquitinated, conducting to its destruction and to the liberation of ESPL1. Its function is however not limited to a blocking activity, since it is required to activate ESPL1. Negatively regulates the transcriptional activity and related apoptosis activity of p53/TP53. The negative regulation of p53/TP53 may explain the strong transforming capability of the protein when it is overexpressed. May also play a role in DNA repair via its interaction with Ku, possibly by connecting DNA damage-response pathways with sister chromatid separation (By similarity).By similarity

GO - Molecular functioni

  • cysteine-type endopeptidase inhibitor activity Source: MGI
  • ribosome binding Source: Ensembl

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • cellular process Source: MGI
  • chromosome organization Source: InterPro
  • chromosome segregation Source: MGI
  • DNA repair Source: UniProtKB-KW
  • homologous chromosome segregation Source: MGI
  • mitotic nuclear division Source: UniProtKB-KW
  • negative regulation of cell proliferation Source: Ensembl
  • negative regulation of endopeptidase activity Source: GOC
  • regulation of cell growth Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Chromosome partition, DNA damage, DNA repair, Mitosis

Enzyme and pathway databases

ReactomeiR-MMU-174154. APC/C:Cdc20 mediated degradation of Securin.
R-MMU-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-MMU-2467813. Separation of Sister Chromatids.

Names & Taxonomyi

Protein namesi
Recommended name:
Securin
Alternative name(s):
Pituitary tumor-transforming gene 1 protein
Gene namesi
Name:Pttg1
Synonyms:Pttg
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1353578. Pttg1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi142 – 1421P → A or L: Strongly reduces transactivation and transforming capability. 1 Publication

Keywords - Diseasei

Proto-oncogene

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 199198SecurinPRO_0000206362Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei162 – 1621PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated at Ser-162 by CDC2 during mitosis.By similarity
Phosphorylated in vitro by ds-DNA kinase.By similarity
Ubiquitinated through 'Lys-11' linkage of ubiquitin moieties by the anaphase promoting complex (APC) at the onset of anaphase, conducting to its degradation. 'Lys-11'-linked ubiquitination is mediated by the E2 ligase UBE2C/UBCH10 (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9CQJ7.
MaxQBiQ9CQJ7.
PaxDbiQ9CQJ7.
PRIDEiQ9CQJ7.

PTM databases

iPTMnetiQ9CQJ7.
PhosphoSiteiQ9CQJ7.

Expressioni

Developmental stagei

During the stages E11.5-E13.5 it is expressed in most tissues of the embryo. Within the telencephalon, it is exclusively expressed inside of the ventricular zone (VZ). The expression reaches its peak by E15.5 and starts to decrease by E18.5, and is not detectable in the adult brains. Most of the cells expressing it were found in the lower part of the ventricular zone.1 Publication

Gene expression databases

BgeeiQ9CQJ7.
CleanExiMM_PTTG1.
ExpressionAtlasiQ9CQJ7. baseline and differential.
GenevisibleiQ9CQJ7. MM.

Interactioni

Subunit structurei

Interacts with RPS10 and DNAJA1. Interacts with the caspase-like ESPL1, and prevents its protease activity probably by covering its active site. Interacts with p53/TP53 and blocks its activity probably by blocking its binding to DNA. Interacts with the Ku 70 kDa subunit of ds-DNA kinase. Interacts with PTTG1IP (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
CLTCQ006101EBI-2551713,EBI-354967From a different organism.

Protein-protein interaction databases

BioGridi206016. 1 interaction.
IntActiQ9CQJ7. 1 interaction.
STRINGi10090.ENSMUSP00000020687.

Structurei

3D structure databases

ProteinModelPortaliQ9CQJ7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi58 – 614D-box
Motifi68 – 703TEK-box 1
Motifi91 – 933TEK-box 2
Motifi179 – 19214SH3-bindingAdd
BLAST

Domaini

The N-terminal destruction box (D-box) acts as a recognition signal for degradation via the ubiquitin-proteasome pathway.By similarity
The TEK-boxes are required for 'Lys-11'-linked ubiquitination and facilitate the transfer of the first ubiquitin and ubiquitin chain nucleation. TEK-boxes may direct a catalytically competent orientation of the UBE2C/UBCH10-ubiquitin thioester with the acceptor lysine residue (By similarity).By similarity

Sequence similaritiesi

Belongs to the securin family.Curated

Keywords - Domaini

Repeat, SH3-binding

Phylogenomic databases

eggNOGiENOG410IVQH. Eukaryota.
ENOG410Z8MR. LUCA.
GeneTreeiENSGT00390000009693.
HOGENOMiHOG000035097.
HOVERGENiHBG053264.
InParanoidiQ9CQJ7.
KOiK06635.
OMAiFSAKKVT.
OrthoDBiEOG7MPRH0.
PhylomeDBiQ9CQJ7.
TreeFamiTF330797.

Family and domain databases

InterProiIPR018008. Securin_separation-inh_met.
IPR006940. Securin_separation_inhibitor.
[Graphical view]
PANTHERiPTHR10418. PTHR10418. 1 hit.
PfamiPF04856. Securin. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9CQJ7-1) [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
MATLIFVDKD NEEPGRRLAS KDGLKLGTGV KALDGKLQVS TPRVGKVFNA
60 70 80 90 100
PAVPKASRKA LGTVNRVAEK PMKTGKPLQP KQPTLTGKKI TEKSTKTQSS
110 120 130 140 150
VPAPDDAYPE IEKFFPFNPL DFESFDLPEE HQISLLPLNG VPLMTLNEER
160 170 180 190
GLEKLLHLGP PSPLKTPFLS WESDPLYSPP SALSTLDVEL PPVCYDADI
Length:199
Mass (Da):21,725
Last modified:June 1, 2001 - v1
Checksum:i82E6A39B8B96F853
GO
Isoform 2 (identifier: Q9CQJ7-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     174-188: DPLYSPPSALSTLDV → GKGVRSNSGCKQLVT
     189-199: Missing.

Show »
Length:188
Mass (Da):20,468
Checksum:i5AB9A0169BEB2963
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti16 – 161R → S in AAH23324 (PubMed:15489334).Curated
Sequence conflicti28 – 281T → S in AAH23324 (PubMed:15489334).Curated
Sequence conflicti29 – 291G → S in AAC83236 (PubMed:10713046).Curated
Sequence conflicti53 – 531V → L in AAH23324 (PubMed:15489334).Curated
Sequence conflicti122 – 1243Missing in AAC62954 (PubMed:10713046).Curated
Sequence conflicti129 – 1291E → G in AAC83236 (PubMed:10713046).Curated
Sequence conflicti144 – 1441M → I in AAC62954 (PubMed:10713046).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei174 – 18815DPLYS…STLDV → GKGVRSNSGCKQLVT in isoform 2. 1 PublicationVSP_006998Add
BLAST
Alternative sequencei189 – 19911Missing in isoform 2. 1 PublicationVSP_006999Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF069051 mRNA. Translation: AAC62954.1.
AF071209 mRNA. Translation: AAC83236.1.
AK002473 mRNA. Translation: BAB22127.1.
AK008704 mRNA. Translation: BAB25844.1.
AK088387 mRNA. Translation: BAC40321.1.
BC023324 mRNA. Translation: AAH23324.1.
CCDSiCCDS24556.1. [Q9CQJ7-2]
CCDS48771.1. [Q9CQJ7-1]
RefSeqiNP_001124526.1. NM_001131054.1. [Q9CQJ7-1]
NP_038945.2. NM_013917.2. [Q9CQJ7-2]
XP_006533578.1. XM_006533515.2. [Q9CQJ7-1]
XP_006533579.1. XM_006533516.2. [Q9CQJ7-1]
UniGeneiMm.6856.

Genome annotation databases

EnsembliENSMUST00000020685; ENSMUSP00000020685; ENSMUSG00000020415. [Q9CQJ7-2]
ENSMUST00000020687; ENSMUSP00000020687; ENSMUSG00000020415. [Q9CQJ7-1]
ENSMUST00000101340; ENSMUSP00000098894; ENSMUSG00000020415. [Q9CQJ7-1]
ENSMUST00000117446; ENSMUSP00000112841; ENSMUSG00000020415. [Q9CQJ7-2]
ENSMUST00000118368; ENSMUSP00000112834; ENSMUSG00000020415. [Q9CQJ7-1]
ENSMUST00000121638; ENSMUSP00000112815; ENSMUSG00000020415. [Q9CQJ7-1]
GeneIDi30939.
KEGGimmu:30939.
UCSCiuc007imn.2. mouse. [Q9CQJ7-2]
uc011xth.1. mouse. [Q9CQJ7-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF069051 mRNA. Translation: AAC62954.1.
AF071209 mRNA. Translation: AAC83236.1.
AK002473 mRNA. Translation: BAB22127.1.
AK008704 mRNA. Translation: BAB25844.1.
AK088387 mRNA. Translation: BAC40321.1.
BC023324 mRNA. Translation: AAH23324.1.
CCDSiCCDS24556.1. [Q9CQJ7-2]
CCDS48771.1. [Q9CQJ7-1]
RefSeqiNP_001124526.1. NM_001131054.1. [Q9CQJ7-1]
NP_038945.2. NM_013917.2. [Q9CQJ7-2]
XP_006533578.1. XM_006533515.2. [Q9CQJ7-1]
XP_006533579.1. XM_006533516.2. [Q9CQJ7-1]
UniGeneiMm.6856.

3D structure databases

ProteinModelPortaliQ9CQJ7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi206016. 1 interaction.
IntActiQ9CQJ7. 1 interaction.
STRINGi10090.ENSMUSP00000020687.

PTM databases

iPTMnetiQ9CQJ7.
PhosphoSiteiQ9CQJ7.

Proteomic databases

EPDiQ9CQJ7.
MaxQBiQ9CQJ7.
PaxDbiQ9CQJ7.
PRIDEiQ9CQJ7.

Protocols and materials databases

DNASUi30939.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000020685; ENSMUSP00000020685; ENSMUSG00000020415. [Q9CQJ7-2]
ENSMUST00000020687; ENSMUSP00000020687; ENSMUSG00000020415. [Q9CQJ7-1]
ENSMUST00000101340; ENSMUSP00000098894; ENSMUSG00000020415. [Q9CQJ7-1]
ENSMUST00000117446; ENSMUSP00000112841; ENSMUSG00000020415. [Q9CQJ7-2]
ENSMUST00000118368; ENSMUSP00000112834; ENSMUSG00000020415. [Q9CQJ7-1]
ENSMUST00000121638; ENSMUSP00000112815; ENSMUSG00000020415. [Q9CQJ7-1]
GeneIDi30939.
KEGGimmu:30939.
UCSCiuc007imn.2. mouse. [Q9CQJ7-2]
uc011xth.1. mouse. [Q9CQJ7-1]

Organism-specific databases

CTDi9232.
MGIiMGI:1353578. Pttg1.

Phylogenomic databases

eggNOGiENOG410IVQH. Eukaryota.
ENOG410Z8MR. LUCA.
GeneTreeiENSGT00390000009693.
HOGENOMiHOG000035097.
HOVERGENiHBG053264.
InParanoidiQ9CQJ7.
KOiK06635.
OMAiFSAKKVT.
OrthoDBiEOG7MPRH0.
PhylomeDBiQ9CQJ7.
TreeFamiTF330797.

Enzyme and pathway databases

ReactomeiR-MMU-174154. APC/C:Cdc20 mediated degradation of Securin.
R-MMU-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-MMU-2467813. Separation of Sister Chromatids.

Miscellaneous databases

PROiQ9CQJ7.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CQJ7.
CleanExiMM_PTTG1.
ExpressionAtlasiQ9CQJ7. baseline and differential.
GenevisibleiQ9CQJ7. MM.

Family and domain databases

InterProiIPR018008. Securin_separation-inh_met.
IPR006940. Securin_separation_inhibitor.
[Graphical view]
PANTHERiPTHR10418. PTHR10418. 1 hit.
PfamiPF04856. Securin. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Pituitary tumor transforming gene (PTTG) transforming and transactivation activity."
    Wang Z., Melmed S.
    J. Biol. Chem. 275:7459-7461(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), MUTAGENESIS OF PRO-142.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J and NOD.
    Tissue: Kidney, Stomach and Thymus.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: FVB/N.
  4. "Expression of PTTG and prc1 genes during telencephalic neurogenesis."
    Tarabykin V., Britanova O., Fradkov A., Voss A., Katz L.S., Lukyanov S., Gruss P.
    Mech. Dev. 92:301-304(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  5. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Spleen and Testis.

Entry informationi

Entry nameiPTTG1_MOUSE
AccessioniPrimary (citable) accession number: Q9CQJ7
Secondary accession number(s): O88887, Q9Z2E6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: June 1, 2001
Last modified: June 8, 2016
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.