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Protein

Treslin

Gene

TICRR

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

Functioni

Regulator of DNA replication and S/M and G2/M checkpoints. Regulates the triggering of DNA replication initiation via its interaction with TOPBP1 by participating in CDK2-mediated loading of CDC45L onto replication origins. Required for the transition from pre-replication complex (pre-RC) to pre-initiation complex (pre-IC). Required to prevent mitotic entry after treatment with ionizing radiation.1 Publication

GO - Molecular functioni

  • chromatin binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, DNA damage, DNA repair

Names & Taxonomyi

Protein namesi
Recommended name:
Treslin
Alternative name(s):
TopBP1-interacting checkpoint and replication regulator
TopBP1-interacting, replication-stimulating protein
Gene namesi
Name:TICRR
Synonyms:C15orf42
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:28704. TICRR.

Subcellular locationi

GO - Cellular componenti

  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142672278.

Polymorphism and mutation databases

BioMutaiTICRR.
DMDMi156631024.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 19101910TreslinPRO_0000296623Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei292 – 2921PhosphoserineCombined sources
Modified residuei441 – 4411PhosphoserineCombined sources
Modified residuei599 – 5991PhosphoserineCombined sources
Modified residuei820 – 8201PhosphoserineCombined sources
Modified residuei838 – 8381PhosphoserineCombined sources
Modified residuei865 – 8651PhosphoserineCombined sources
Modified residuei923 – 9231PhosphoserineCombined sources
Modified residuei938 – 9381PhosphoserineCombined sources
Modified residuei1001 – 10011PhosphoserineCombined sources
Modified residuei1026 – 10261PhosphoserineCombined sources
Modified residuei1057 – 10571PhosphoserineCombined sources
Modified residuei1078 – 10781PhosphoserineCombined sources
Modified residuei1125 – 11251PhosphoserineCombined sources
Modified residuei1134 – 11341PhosphothreonineCombined sources
Modified residuei1141 – 11411PhosphoserineBy similarity
Modified residuei1307 – 13071PhosphothreonineCombined sources
Modified residuei1413 – 14131PhosphoserineCombined sources
Modified residuei1484 – 14841PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ7Z2Z1.
MaxQBiQ7Z2Z1.
PaxDbiQ7Z2Z1.
PeptideAtlasiQ7Z2Z1.
PRIDEiQ7Z2Z1.

PTM databases

iPTMnetiQ7Z2Z1.
PhosphoSiteiQ7Z2Z1.

Expressioni

Gene expression databases

BgeeiQ7Z2Z1.
CleanExiHS_C15orf42.
ExpressionAtlasiQ7Z2Z1. baseline and differential.
GenevisibleiQ7Z2Z1. HS.

Interactioni

Subunit structurei

Interacts with TOPBP1 (via BRCT domains); interaction takes place in a CDK2-dependent manner.1 Publication

Protein-protein interaction databases

BioGridi124706. 4 interactions.
IntActiQ7Z2Z1. 1 interaction.
STRINGi9606.ENSP00000268138.

Structurei

3D structure databases

ProteinModelPortaliQ7Z2Z1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1193 – 1378186Pro-richAdd
BLAST

Sequence similaritiesi

Belongs to the treslin family.Curated

Phylogenomic databases

eggNOGiENOG410IFG8. Eukaryota.
ENOG410Y8R6. LUCA.
GeneTreeiENSGT00390000005222.
HOVERGENiHBG101933.
InParanoidiQ7Z2Z1.
OMAiHSASFYS.
OrthoDBiEOG78WKVH.
PhylomeDBiQ7Z2Z1.
TreeFamiTF332114.

Family and domain databases

InterProiIPR026153. Treslin.
IPR032746. Treslin_N.
[Graphical view]
PANTHERiPTHR21556. PTHR21556. 1 hit.
PfamiPF15292. Treslin_N. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q7Z2Z1-1) [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
MACCHKVMLL LDTAGGAARH SRVRRAALRL LTYLSCRFGL ARVHWAFKFF
60 70 80 90 100
DSQGARSRPS RVSDFRELGS RSWEDFEEEL EARLEDRAHL PGPAPRATHT
110 120 130 140 150
HGALMETLLD YQWDRPEITS PTKPILRSSG RRLLDVESEA KEAEAALGGL
160 170 180 190 200
VNAVFLLAPC PHSQRELLQF VSGCEAQAQR LPPTPKQVME KLLPKRVREV
210 220 230 240 250
MVARKITFYW VDTTEWSKLW ESPDHLGYWT VCELLHHGGG TVLPSESFSW
260 270 280 290 300
DFAQAGEMLL RSGIKLSSEP HLSPWISMLP TDATLNRLLY NSPEYEASFP
310 320 330 340 350
RMEGMLFLPV EAGKEIQETW TVTLEPLAMH QRHFQKPVRI FLKGSVAQWS
360 370 380 390 400
LPTSSTLGTD SWMLGSPEES TATQRLLFQQ LVSRLTAEEL HLVADVDPGE
410 420 430 440 450
GRPPITGVIS PLSASAMILT VCRTKEAEFQ RHVLQTAVAD SPRDTASLFS
460 470 480 490 500
DVVDSILNQT HDSLADTASA ASPVPEWAQQ ELGHTTPWSP AVVEKWFPFC
510 520 530 540 550
NISGASSDLM ESFGLLQAAS ANKEESSKTE GELIHCLAEL YQRKSREEST
560 570 580 590 600
IAHQEDSKKK RGVPRTPVRQ KMNTMCRSLK MLNVARLNVK AQKLHPDGSP
610 620 630 640 650
DVAGEKGIQK IPSGRTVDKL EDRGRTLRSS KPKDFKTEEE LLSYIRENYQ
660 670 680 690 700
KTVATGEIML YACARNMIST VKMFLKSKGT KELEVNCLNQ VKSSLLKTSK
710 720 730 740 750
SLRQNLGKKL DKEDKVRECQ LQVFLRLEMC LQCPSINEST DDMEQVVEEV
760 770 780 790 800
TDLLRMVCLT EDSAYLAEFL EEILRLYIDS IPKTLGNLYN SLGFVIPQKL
810 820 830 840 850
AGVLPTDFFS DDSMTQENKS PLLSVPFLSS ARRSVSGSPE SDELQELRTR
860 870 880 890 900
SAKKRRKNAL IRHKSIAEVS QNLRQIEIPK VSKRATKKEN SHPAPQQPSQ
910 920 930 940 950
PVKDTVQEVT KVRRNLFNQE LLSPSKRSLK RGLPRSHSVS AVDGLEDKLD
960 970 980 990 1000
NFKKNKGYHK LLTKSVAETP VHKQISKRLL HRQIKGRSSD PGPDIGVVEE
1010 1020 1030 1040 1050
SPEKGDEISL RRSPRIKQLS FSRTHSASFY SVSQPKSRSV QRVHSFQQDK
1060 1070 1080 1090 1100
SDQRENSPVQ SIRSPKSLLF GAMSEMISPS EKGSARMKKR SRNTLDSEVP
1110 1120 1130 1140 1150
AAYQTPKKSH QKSLSFSKTT PRRISHTPQT PLYTPERLQK SPAKMTPTKQ
1160 1170 1180 1190 1200
AAFKESLKDS SSPGHDSPLD SKITPQKRHT QAGEGTSLET KTPRTPKRQG
1210 1220 1230 1240 1250
TQPPGFLPNC TWPHSVNSSP ESPSCPAPPT SSTAQPRREC LTPIRDPLRT
1260 1270 1280 1290 1300
PPRAAAFMGT PQNQTHQQPH VLRAARAEEP AQKLKDKAIK TPKRPGNSTV
1310 1320 1330 1340 1350
TSSPPVTPKK LFTSPLCDVS KKSPFRKSKI ECPSPGELDQ KEPQMSPSVA
1360 1370 1380 1390 1400
ASLSCPVPST PPELSQRATL DTVPPPPPSK VGKRCRKTSD PRRSIVECQP
1410 1420 1430 1440 1450
DASATPGVGT ADSPAAPTDS RDDQKGLSLS PQSPPERRGY PGPGLRSDWH
1460 1470 1480 1490 1500
ASSPLLITSD TEHVTLLSEA EHHGIGDLKS NVLSVEEGEG LRTADAEKSS
1510 1520 1530 1540 1550
LSHPGIPPSP PSCGPGSPLM PSRDVHCTTD GRQCQASAQL DNLPASAWHS
1560 1570 1580 1590 1600
TDSASPQTYE VELEMQASGL PKLRIKKIDP SSSLEAEPLS KEESSLGEES
1610 1620 1630 1640 1650
FLPALSMPRA SRSLSKPEPT YVSPPCPRLS HSTPGKSRGQ TYICQACTPT
1660 1670 1680 1690 1700
HGPSSTPSPF QTDGVPWTPS PKHSGKTTPD IIKDWPRRKR AVGCGAGSSS
1710 1720 1730 1740 1750
GRGEVGADLP GSLSLLESEG KDHGLELSIH RTPILEDFEL EGVCQLPDQS
1760 1770 1780 1790 1800
PPRNSMPKAE EASSWGQFGL SSRKRVLLAK EEADRGAKRI CDLREDSEVS
1810 1820 1830 1840 1850
KSKEGSPSWS AWQLPSTGDE EVFVSGSTPP PSCAVRSCLS ASALQALTQS
1860 1870 1880 1890 1900
PLLFQGKTPS SQSKDPRDED VDVLPSTVED SPFSRAFSRR RPISRTYTRK
1910
KLMGTWLEDL
Length:1,910
Mass (Da):210,857
Last modified:July 24, 2007 - v2
Checksum:i3E726E5091B9FA5B
GO
Isoform 2 (identifier: Q7Z2Z1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     312-312: Missing.

Show »
Length:1,909
Mass (Da):210,786
Checksum:i01A60617B75CDB54
GO

Sequence cautioni

The sequence BAC11165.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAG38104.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAG53921.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti152 – 1521N → Y in DR731357 (Ref. 3) Curated
Sequence conflicti336 – 3361K → T in DR731357 (Ref. 3) Curated
Sequence conflicti1009 – 10091S → G in ADC30133 (PubMed:20116089).Curated
Sequence conflicti1009 – 10091S → G in BAG53921 (PubMed:14702039).Curated
Sequence conflicti1344 – 13441Q → L in BAG38104 (PubMed:14702039).Curated
Sequence conflicti1373 – 13731V → I in BAG53921 (PubMed:14702039).Curated
Sequence conflicti1427 – 14271L → P in BAC11165 (PubMed:14702039).Curated
Sequence conflicti1667 – 16671W → R in BAC11165 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti287 – 2871R → C.1 Publication
Corresponds to variant rs10775247 [ dbSNP | Ensembl ].
VAR_050886
Natural varianti402 – 4021R → W.
Corresponds to variant rs11629584 [ dbSNP | Ensembl ].
VAR_050887
Natural varianti628 – 6281R → C.
Corresponds to variant rs3743372 [ dbSNP | Ensembl ].
VAR_034631
Natural varianti747 – 7471V → A.
Corresponds to variant rs12905387 [ dbSNP | Ensembl ].
VAR_050888
Natural varianti923 – 9231S → C.
Corresponds to variant rs16943377 [ dbSNP | Ensembl ].
VAR_050889
Natural varianti1523 – 15231R → C.2 Publications
Corresponds to variant rs894157 [ dbSNP | Ensembl ].
VAR_050890
Natural varianti1718 – 17181S → T.1 Publication
Corresponds to variant rs1866928 [ dbSNP | Ensembl ].
VAR_050891
Natural varianti1885 – 18851R → C.1 Publication
Corresponds to variant rs3743372 [ dbSNP | Ensembl ].
VAR_050892

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei312 – 3121Missing in isoform 2. 1 PublicationVSP_039218

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
GQ227787 mRNA. Translation: ADC30133.1.
AC013391 Genomic DNA. No translation available.
AC013787 Genomic DNA. No translation available.
DR731357 mRNA. No translation available.
AK074727 mRNA. Translation: BAC11165.1. Different initiation.
AK123612 mRNA. Translation: BAG53921.1. Different initiation.
AK315750 mRNA. Translation: BAG38104.1. Different initiation.
BX538335 mRNA. Translation: CAD98102.1.
BC002881 mRNA. Translation: AAH02881.2.
BC033209 mRNA. Translation: AAH33209.2.
CCDSiCCDS10352.2. [Q7Z2Z1-1]
CCDS76791.1. [Q7Z2Z1-2]
RefSeqiNP_001294954.1. NM_001308025.1. [Q7Z2Z1-2]
NP_689472.3. NM_152259.3. [Q7Z2Z1-1]
UniGeneiHs.441708.

Genome annotation databases

EnsembliENST00000268138; ENSP00000268138; ENSG00000140534. [Q7Z2Z1-1]
ENST00000560985; ENSP00000453306; ENSG00000140534. [Q7Z2Z1-2]
GeneIDi90381.
KEGGihsa:90381.
UCSCiuc002boe.4. human. [Q7Z2Z1-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
GQ227787 mRNA. Translation: ADC30133.1.
AC013391 Genomic DNA. No translation available.
AC013787 Genomic DNA. No translation available.
DR731357 mRNA. No translation available.
AK074727 mRNA. Translation: BAC11165.1. Different initiation.
AK123612 mRNA. Translation: BAG53921.1. Different initiation.
AK315750 mRNA. Translation: BAG38104.1. Different initiation.
BX538335 mRNA. Translation: CAD98102.1.
BC002881 mRNA. Translation: AAH02881.2.
BC033209 mRNA. Translation: AAH33209.2.
CCDSiCCDS10352.2. [Q7Z2Z1-1]
CCDS76791.1. [Q7Z2Z1-2]
RefSeqiNP_001294954.1. NM_001308025.1. [Q7Z2Z1-2]
NP_689472.3. NM_152259.3. [Q7Z2Z1-1]
UniGeneiHs.441708.

3D structure databases

ProteinModelPortaliQ7Z2Z1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124706. 4 interactions.
IntActiQ7Z2Z1. 1 interaction.
STRINGi9606.ENSP00000268138.

PTM databases

iPTMnetiQ7Z2Z1.
PhosphoSiteiQ7Z2Z1.

Polymorphism and mutation databases

BioMutaiTICRR.
DMDMi156631024.

Proteomic databases

EPDiQ7Z2Z1.
MaxQBiQ7Z2Z1.
PaxDbiQ7Z2Z1.
PeptideAtlasiQ7Z2Z1.
PRIDEiQ7Z2Z1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000268138; ENSP00000268138; ENSG00000140534. [Q7Z2Z1-1]
ENST00000560985; ENSP00000453306; ENSG00000140534. [Q7Z2Z1-2]
GeneIDi90381.
KEGGihsa:90381.
UCSCiuc002boe.4. human. [Q7Z2Z1-1]

Organism-specific databases

CTDi90381.
GeneCardsiTICRR.
H-InvDBHIX0012567.
HGNCiHGNC:28704. TICRR.
MIMi613298. gene.
neXtProtiNX_Q7Z2Z1.
PharmGKBiPA142672278.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IFG8. Eukaryota.
ENOG410Y8R6. LUCA.
GeneTreeiENSGT00390000005222.
HOVERGENiHBG101933.
InParanoidiQ7Z2Z1.
OMAiHSASFYS.
OrthoDBiEOG78WKVH.
PhylomeDBiQ7Z2Z1.
TreeFamiTF332114.

Miscellaneous databases

GenomeRNAii90381.
PROiQ7Z2Z1.
SOURCEiSearch...

Gene expression databases

BgeeiQ7Z2Z1.
CleanExiHS_C15orf42.
ExpressionAtlasiQ7Z2Z1. baseline and differential.
GenevisibleiQ7Z2Z1. HS.

Family and domain databases

InterProiIPR026153. Treslin.
IPR032746. Treslin_N.
[Graphical view]
PANTHERiPTHR21556. PTHR21556. 1 hit.
PfamiPF15292. Treslin_N. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Treslin collaborates with TopBP1 in triggering the initiation of DNA replication."
    Kumagai A., Shevchenko A., Shevchenko A., Dunphy W.G.
    Cell 140:349-359(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION.
  2. "Analysis of the DNA sequence and duplication history of human chromosome 15."
    Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
    , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
    Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "Exhaustive RT-PCR and sequencing of all novel TWINSCAN predictions in human."
    Stevens M., Wei C., Gross S.S., McPherson J., Brent M.R.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 134-367 (ISOFORM 1), VARIANT CYS-287.
  4. "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] OF 635-1910, VARIANTS CYS-1523; THR-1718 AND CYS-1885.
    Tissue: Teratocarcinoma, Tongue and Uterus.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 901-1910.
    Tissue: Rectum tumor.
  6. "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] OF 1321-1910, VARIANT CYS-1523.
    Tissue: Lung and Muscle.
  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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-441, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1307 AND SER-1413, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "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-1026; THR-1307 AND SER-1484, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  10. "A vertebrate gene, ticrr, is an essential checkpoint and replication regulator."
    Sansam C.L., Cruz N.M., Danielian P.S., Amsterdam A., Lau M.L., Hopkins N., Lees J.A.
    Genes Dev. 24:183-194(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH TOPBP1.
  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-441; SER-599; SER-820; SER-838; SER-923; SER-1001 AND SER-1078, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-292; SER-441; SER-599; SER-838; SER-865; SER-923; SER-938; SER-1001; SER-1026; SER-1057; SER-1078; SER-1125; THR-1134 AND SER-1484, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.

Entry informationi

Entry nameiTICRR_HUMAN
AccessioniPrimary (citable) accession number: Q7Z2Z1
Secondary accession number(s): B2RE07
, B3KVV9, D3IUT4, Q8N4X8, Q8NCH6, Q9BU55
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 24, 2007
Last sequence update: July 24, 2007
Last modified: July 6, 2016
This is version 97 of the entry and version 2 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 15
    Human chromosome 15: 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. 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.