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Protein

G2 and S phase-expressed protein 1

Gene

GTSE1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

May be involved in p53-induced cell cycle arrest in G2/M phase by interfering with microtubule rearrangements that are required to enter mitosis. Overexpression delays G2/M phase progression.

GO - Biological processi

  • DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Source: UniProtKB
  • microtubule-based process Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
G2 and S phase-expressed protein 1
Short name:
GTSE-1
Alternative name(s):
Protein B99 homolog
Gene namesi
Name:GTSE1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:13698. GTSE1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasmic microtubule Source: UniProtKB
  • membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29061.

Polymorphism and mutation databases

BioMutaiGTSE1.
DMDMi317373439.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 720720G2 and S phase-expressed protein 1PRO_0000083875Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei72 – 721PhosphoserineCombined sources
Modified residuei138 – 1381PhosphoserineCombined sources
Modified residuei140 – 1401PhosphothreonineCombined sources
Modified residuei152 – 1521PhosphoserineCombined sources
Modified residuei168 – 1681PhosphoserineCombined sources
Modified residuei189 – 1891PhosphoserineCombined sources
Modified residuei461 – 4611PhosphoserineBy similarity
Modified residuei466 – 4661PhosphothreonineBy similarity
Modified residuei477 – 4771PhosphoserineCombined sources
Modified residuei480 – 4801PhosphoserineCombined sources
Modified residuei495 – 4951PhosphoserineCombined sources
Modified residuei501 – 5011PhosphoserineCombined sources
Modified residuei504 – 5041PhosphoserineCombined sources
Modified residuei509 – 5091PhosphoserineCombined sources
Modified residuei513 – 5131PhosphothreonineCombined sources
Modified residuei516 – 5161PhosphoserineCombined sources
Modified residuei536 – 5361PhosphoserineCombined sources
Modified residuei575 – 5751PhosphoserineCombined sources
Modified residuei592 – 5921PhosphoserineCombined sources
Modified residuei677 – 6771PhosphothreonineCombined sources
Modified residuei688 – 6881PhosphoserineCombined sources
Modified residuei698 – 6981PhosphoserineCombined sources
Modified residuei699 – 6991PhosphoserineCombined sources
Modified residuei705 – 7051PhosphoserineCombined sources
Modified residuei715 – 7151PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated in mitosis.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9NYZ3.
MaxQBiQ9NYZ3.
PaxDbiQ9NYZ3.
PRIDEiQ9NYZ3.

PTM databases

iPTMnetiQ9NYZ3.
PhosphoSiteiQ9NYZ3.

Expressioni

Developmental stagei

Expressed in G2/M phase. Not detected in quiescent cells.

Gene expression databases

BgeeiQ9NYZ3.
GenevisibleiQ9NYZ3. HS.

Organism-specific databases

HPAiHPA049873.
HPA060544.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
PLK1P533506EBI-2511327,EBI-476768

Protein-protein interaction databases

BioGridi119580. 138 interactions.
IntActiQ9NYZ3. 130 interactions.
MINTiMINT-7988145.
STRINGi9606.ENSP00000415430.

Structurei

3D structure databases

ProteinModelPortaliQ9NYZ3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi22 – 276Poly-Ser

Phylogenomic databases

eggNOGiENOG410IHTJ. Eukaryota.
ENOG410ZUTK. LUCA.
HOVERGENiHBG103867.
InParanoidiQ9NYZ3.
KOiK10129.
OrthoDBiEOG7288RK.
PhylomeDBiQ9NYZ3.
TreeFamiTF332555.

Family and domain databases

InterProiIPR026657. DDA3/GTSE-1.
IPR026659. GTSE1.
IPR032768. GTSE1_N.
[Graphical view]
PANTHERiPTHR21584. PTHR21584. 1 hit.
PTHR21584:SF10. PTHR21584:SF10. 1 hit.
PfamiPF15259. GTSE1_N. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9NYZ3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDDPKKEDIL LLADEKFDFD LSLSSSSANE DDEVFFGPFG HKERCIAASL
60 70 80 90 100
ELNNPVPEQP PLPTSESPFA WSPLAGEKFV EVYKEAHLLA LHIESSSRNQ
110 120 130 140 150
AAQAAKPEDP RSQGVERFIQ ESKLKINLFE KEKEMKKSPT SLKRETYYLS
160 170 180 190 200
DSPLLGPPVG EPRLLASSPA LPSSGAQARL TRAPGPPHSA HALPRESCTA
210 220 230 240 250
HAASQAATQR KPGTKLLLPR AASVRGRSIP GAAEKPKKEI PASPSRTKIP
260 270 280 290 300
AEKESHRDVL PDKPAPGAVN VPAAGSHLGQ GKRAIPVPNK LGLKKTLLKA
310 320 330 340 350
PGSTSNLARK SSSGPVWSGA SSACTSPAVG KAKSSEFASI PANSSRPLSN
360 370 380 390 400
ISKSGRMGPA MLRPALPAGP VGASSWQAKR VDVSELAAEQ LTAPPSASPT
410 420 430 440 450
QPQTPEGGGQ WLNSSCAWSE SSQLNKTRSI RRRDSCLNSK TKVMPTPTNQ
460 470 480 490 500
FKIPKFSIGD SPDSSTPKLS RAQRPQSCTS VGRVTVHSTP VRRSSGPAPQ
510 520 530 540 550
SLLSAWRVSA LPTPASRRCS GLPPMTPKTM PRAVGSPLCV PARRRSSEPR
560 570 580 590 600
KNSAMRTEPT RESNRKTDSR LVDVSPDRGS PPSRVPQALN FSPEESDSTF
610 620 630 640 650
SKSTATEVAR EEAKPGGDAA PSEALLVDIK LEPLAVTPDA ASQPLIDLPL
660 670 680 690 700
IDFCDTPEAH VAVGSESRPL IDLMTNTPDM NKNVAKPSPV VGQLIDLSSP
710 720
LIQLSPEADK ENVDSPLLKF
Length:720
Mass (Da):76,645
Last modified:January 11, 2011 - v3
Checksum:iDBAC3C9ED528FB29
GO

Sequence cautioni

The sequence CAQ09324.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAQ10552.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 41P → S in AAH75828 (PubMed:15489334).Curated
Sequence conflicti135 – 1351M → V in BAD96526 (PubMed:14702039).Curated
Sequence conflicti259 – 2591V → I in AAF31459 (PubMed:10974554).Curated
Sequence conflicti306 – 3061N → D in BAD96526 (PubMed:14702039).Curated
Sequence conflicti455 – 4551K → R in BAD96526 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti181 – 1811T → A.
Corresponds to variant rs6008600 [ dbSNP | Ensembl ].
VAR_032816
Natural varianti200 – 2001A → V.
Corresponds to variant rs34404175 [ dbSNP | Ensembl ].
VAR_032817
Natural varianti274 – 2741A → T.
Corresponds to variant rs35503220 [ dbSNP | Ensembl ].
VAR_032818
Natural varianti303 – 3031S → N.
Corresponds to variant rs6008622 [ dbSNP | Ensembl ].
VAR_056905
Natural varianti322 – 3221S → N.
Corresponds to variant rs6008622 [ dbSNP | Ensembl ].
VAR_032819
Natural varianti463 – 4631D → E.
Corresponds to variant rs6008684 [ dbSNP | Ensembl ].
VAR_032820
Natural varianti470 – 4701S → L.
Corresponds to variant rs2281192 [ dbSNP | Ensembl ].
VAR_021973
Natural varianti506 – 5061W → R.Combined sources4 Publications
Corresponds to variant rs140054 [ dbSNP | Ensembl ].
VAR_024154
Natural varianti635 – 6351A → T.
Corresponds to variant rs16995138 [ dbSNP | Ensembl ].
VAR_032821

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF223408 mRNA. Translation: AAF31459.1.
CT841519 mRNA. Translation: CAJ86449.1.
AK222806 mRNA. Translation: BAD96526.1.
AK315550 mRNA. Translation: BAG37928.1.
AL031588, Z93024 Genomic DNA. Translation: CAQ09324.2. Different initiation.
Z93024, AL031588 Genomic DNA. Translation: CAQ10552.2. Different initiation.
BC006325 mRNA. Translation: AAH06325.1.
BC075828 mRNA. Translation: AAH75828.1.
RefSeqiNP_057510.4. NM_016426.6.
UniGeneiHs.386189.
Hs.439524.

Genome annotation databases

EnsembliENST00000454366; ENSP00000415430; ENSG00000075218.
GeneIDi51512.
KEGGihsa:51512.
UCSCiuc011aqy.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF223408 mRNA. Translation: AAF31459.1.
CT841519 mRNA. Translation: CAJ86449.1.
AK222806 mRNA. Translation: BAD96526.1.
AK315550 mRNA. Translation: BAG37928.1.
AL031588, Z93024 Genomic DNA. Translation: CAQ09324.2. Different initiation.
Z93024, AL031588 Genomic DNA. Translation: CAQ10552.2. Different initiation.
BC006325 mRNA. Translation: AAH06325.1.
BC075828 mRNA. Translation: AAH75828.1.
RefSeqiNP_057510.4. NM_016426.6.
UniGeneiHs.386189.
Hs.439524.

3D structure databases

ProteinModelPortaliQ9NYZ3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119580. 138 interactions.
IntActiQ9NYZ3. 130 interactions.
MINTiMINT-7988145.
STRINGi9606.ENSP00000415430.

PTM databases

iPTMnetiQ9NYZ3.
PhosphoSiteiQ9NYZ3.

Polymorphism and mutation databases

BioMutaiGTSE1.
DMDMi317373439.

Proteomic databases

EPDiQ9NYZ3.
MaxQBiQ9NYZ3.
PaxDbiQ9NYZ3.
PRIDEiQ9NYZ3.

Protocols and materials databases

DNASUi51512.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000454366; ENSP00000415430; ENSG00000075218.
GeneIDi51512.
KEGGihsa:51512.
UCSCiuc011aqy.2. human.

Organism-specific databases

CTDi51512.
GeneCardsiGTSE1.
HGNCiHGNC:13698. GTSE1.
HPAiHPA049873.
HPA060544.
MIMi607477. gene.
neXtProtiNX_Q9NYZ3.
PharmGKBiPA29061.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IHTJ. Eukaryota.
ENOG410ZUTK. LUCA.
HOVERGENiHBG103867.
InParanoidiQ9NYZ3.
KOiK10129.
OrthoDBiEOG7288RK.
PhylomeDBiQ9NYZ3.
TreeFamiTF332555.

Miscellaneous databases

ChiTaRSiGTSE1. human.
GeneWikiiGTSE1.
GenomeRNAii51512.
NextBioi55202.
PROiQ9NYZ3.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NYZ3.
GenevisibleiQ9NYZ3. HS.

Family and domain databases

InterProiIPR026657. DDA3/GTSE-1.
IPR026659. GTSE1.
IPR032768. GTSE1_N.
[Graphical view]
PANTHERiPTHR21584. PTHR21584. 1 hit.
PTHR21584:SF10. PTHR21584:SF10. 1 hit.
PfamiPF15259. GTSE1_N. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, chromosome mapping and functional characterization of a human homologue of murine Gtse-1 (B99) gene."
    Monte M., Collavin L., Lazarevic D., Utrera R., Dragani T.A., Schneider C.
    Gene 254:229-236(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ARG-506.
    Tissue: Placenta.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ARG-506.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ARG-506.
    Tissue: Liver and Placenta.
  4. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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], VARIANT ARG-506.
    Tissue: Brain and Muscle.
  6. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168; SER-504 AND SER-592, VARIANT [LARGE SCALE ANALYSIS] ARG-506, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-592, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152; SER-168; SER-477; SER-480; SER-495; SER-501; SER-504; SER-575 AND SER-592, VARIANT [LARGE SCALE ANALYSIS] ARG-506, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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].
  11. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  12. "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-72; SER-138; THR-140; SER-152; SER-168; SER-189; SER-495; SER-504; SER-509; THR-513; SER-516; SER-536; SER-575; SER-592; THR-677; SER-688; SER-698; SER-699; SER-705 AND SER-715, VARIANT [LARGE SCALE ANALYSIS] ARG-506, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.

Entry informationi

Entry nameiGTSE1_HUMAN
AccessioniPrimary (citable) accession number: Q9NYZ3
Secondary accession number(s): B0QYM3
, Q20WK2, Q53GX5, Q5R3I6, Q6DHX4, Q9BRE0, Q9UGZ9, Q9Y557
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 26, 2002
Last sequence update: January 11, 2011
Last modified: May 11, 2016
This is version 131 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, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: 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

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.