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Protein

TIMELESS-interacting protein

Gene

TIPIN

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

Functioni

Plays an important role in the control of DNA replication and the maintenance of replication fork stability. Important for cell survival after DNA damage or replication stress. May be specifically required for the ATR-CHEK1 pathway in the replication checkpoint induced by hydroxyurea or ultraviolet light. Forms a complex with TIMELESS and this complex regulates DNA replication processes under both normal and stress conditions, stabilizes replication forks and influences both CHEK1 phosphorylation and the intra-S phase checkpoint in response to genotoxic stress.3 Publications

GO - Biological processi

  • cell cycle phase transition Source: BHF-UCL
  • cell division Source: UniProtKB-KW
  • DNA replication Source: Reactome
  • DNA replication checkpoint Source: HGNC
  • intra-S DNA damage checkpoint Source: HGNC
  • mitotic nuclear division Source: UniProtKB-KW
  • positive regulation of cell proliferation Source: HGNC
  • regulation of nuclear cell cycle DNA replication Source: HGNC
  • replication fork protection Source: InterPro
  • response to UV Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, DNA damage, Mitosis

Enzyme and pathway databases

ReactomeiR-HSA-5693607. Processing of DNA double-strand break ends.

Names & Taxonomyi

Protein namesi
Recommended name:
TIMELESS-interacting protein
Gene namesi
Name:TIPIN
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:30750. TIPIN.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA147357269.

Polymorphism and mutation databases

BioMutaiTIPIN.
DMDMi296452932.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 301301TIMELESS-interacting proteinPRO_0000305253Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei194 – 1941PhosphoserineCombined sources
Modified residuei222 – 2221PhosphoserineCombined sources
Modified residuei233 – 2331PhosphothreonineCombined sources
Modified residuei244 – 2441PhosphothreonineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9BVW5.
MaxQBiQ9BVW5.
PaxDbiQ9BVW5.
PeptideAtlasiQ9BVW5.
PRIDEiQ9BVW5.

PTM databases

iPTMnetiQ9BVW5.
PhosphoSiteiQ9BVW5.

Expressioni

Gene expression databases

BgeeiQ9BVW5.
CleanExiHS_TIPIN.
ExpressionAtlasiQ9BVW5. baseline and differential.
GenevisibleiQ9BVW5. HS.

Organism-specific databases

HPAiHPA039704.
HPA058799.

Interactioni

Subunit structurei

Interacts with TIMELESS, which impairs TIMELESS self-association. Interacts with RPA2, PRDX2, MCM6 and MCM7.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
RPA2P159274EBI-2515360,EBI-621404
TEX11Q8IYF33EBI-2515360,EBI-742397

Protein-protein interaction databases

BioGridi120300. 16 interactions.
DIPiDIP-53658N.
IntActiQ9BVW5. 10 interactions.
MINTiMINT-4650579.
STRINGi9606.ENSP00000261881.

Structurei

3D structure databases

ProteinModelPortaliQ9BVW5.
SMRiQ9BVW5. Positions 195-220.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni67 – 14377Interaction with TIMELESSAdd
BLAST

Sequence similaritiesi

Belongs to the CSM3 family.Curated

Phylogenomic databases

eggNOGiKOG3004. Eukaryota.
ENOG4111VXN. LUCA.
GeneTreeiENSGT00390000005764.
HOGENOMiHOG000154594.
HOVERGENiHBG061130.
InParanoidiQ9BVW5.
KOiK10904.
OMAiDILDNPC.
OrthoDBiEOG7MSMPZ.
PhylomeDBiQ9BVW5.
TreeFamiTF313290.

Family and domain databases

InterProiIPR012923. Csm3.
[Graphical view]
PfamiPF07962. Swi3. 1 hit.
[Graphical view]
ProDomiPD089639. Swi3. 1 hit.
[Graphical view] [Entries sharing at least one domain]

Sequencei

Sequence statusi: Complete.

Q9BVW5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLEPQENGVI DLPDYEHVED ETFPPFPPPA SPERQDGEGT EPDEESGNGA
60 70 80 90 100
PVRVPPKRTV KRNIPKLDAQ RLISERGLPA LRHVFDKAKF KGKGHEAEDL
110 120 130 140 150
KMLIRHMEHW AHRLFPKLQF EDFIDRVEYL GSKKEVQTCL KRIRLDLPIL
160 170 180 190 200
HEDFVSNNDE VAENNEHDVT STELDPFLTN LSESEMFASE LSRSLTEEQQ
210 220 230 240 250
QRIERNKQLA LERRQAKLLS NSQTLGNDML MNTPRAHTVE EVNTDEDQKE
260 270 280 290 300
ESNGLNEDIL DNPCNDAIAN TLNEEETLLD QSFKNVQQQL DATSRNITEA

R
Length:301
Mass (Da):34,555
Last modified:May 18, 2010 - v2
Checksum:iB0C69117A636CE3A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti201 – 2011Q → R in BAA91229 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti53 – 531R → P.4 Publications
Corresponds to variant rs9806123 [ dbSNP | Ensembl ].
VAR_035194
Natural varianti111 – 1111A → G.1 Publication
Corresponds to variant rs2063690 [ dbSNP | Ensembl ].
VAR_035195
Natural varianti260 – 2601L → P.
Corresponds to variant rs3759787 [ dbSNP | Ensembl ].
VAR_053952
Natural varianti267 – 2671A → S.1 Publication
Corresponds to variant rs3759786 [ dbSNP | Ensembl ].
VAR_035196
Natural varianti270 – 2701N → D.
Corresponds to variant rs34848112 [ dbSNP | Ensembl ].
VAR_062207
Natural varianti270 – 2701N → S.1 Publication
Corresponds to variant rs780014564 [ dbSNP | Ensembl ].
VAR_054483

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK000523 mRNA. Translation: BAA91229.1.
EU551725 Genomic DNA. Translation: ACB21044.1.
AC055855 Genomic DNA. No translation available.
CH471082 Genomic DNA. Translation: EAW77762.1.
BC000870 mRNA. Translation: AAH00870.1.
BK001386 mRNA. Translation: DAA01365.1.
CCDSiCCDS10215.1.
RefSeqiNP_001276915.1. NM_001289986.1.
NP_060328.2. NM_017858.2.
XP_005254578.1. XM_005254521.2.
XP_005254579.1. XM_005254522.3.
XP_006720657.1. XM_006720594.2.
XP_011520045.1. XM_011521743.1.
UniGeneiHs.744308.

Genome annotation databases

EnsembliENST00000261881; ENSP00000261881; ENSG00000075131.
GeneIDi54962.
KEGGihsa:54962.
UCSCiuc002apr.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK000523 mRNA. Translation: BAA91229.1.
EU551725 Genomic DNA. Translation: ACB21044.1.
AC055855 Genomic DNA. No translation available.
CH471082 Genomic DNA. Translation: EAW77762.1.
BC000870 mRNA. Translation: AAH00870.1.
BK001386 mRNA. Translation: DAA01365.1.
CCDSiCCDS10215.1.
RefSeqiNP_001276915.1. NM_001289986.1.
NP_060328.2. NM_017858.2.
XP_005254578.1. XM_005254521.2.
XP_005254579.1. XM_005254522.3.
XP_006720657.1. XM_006720594.2.
XP_011520045.1. XM_011521743.1.
UniGeneiHs.744308.

3D structure databases

ProteinModelPortaliQ9BVW5.
SMRiQ9BVW5. Positions 195-220.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120300. 16 interactions.
DIPiDIP-53658N.
IntActiQ9BVW5. 10 interactions.
MINTiMINT-4650579.
STRINGi9606.ENSP00000261881.

PTM databases

iPTMnetiQ9BVW5.
PhosphoSiteiQ9BVW5.

Polymorphism and mutation databases

BioMutaiTIPIN.
DMDMi296452932.

Proteomic databases

EPDiQ9BVW5.
MaxQBiQ9BVW5.
PaxDbiQ9BVW5.
PeptideAtlasiQ9BVW5.
PRIDEiQ9BVW5.

Protocols and materials databases

DNASUi54962.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000261881; ENSP00000261881; ENSG00000075131.
GeneIDi54962.
KEGGihsa:54962.
UCSCiuc002apr.3. human.

Organism-specific databases

CTDi54962.
GeneCardsiTIPIN.
HGNCiHGNC:30750. TIPIN.
HPAiHPA039704.
HPA058799.
MIMi610716. gene.
neXtProtiNX_Q9BVW5.
PharmGKBiPA147357269.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3004. Eukaryota.
ENOG4111VXN. LUCA.
GeneTreeiENSGT00390000005764.
HOGENOMiHOG000154594.
HOVERGENiHBG061130.
InParanoidiQ9BVW5.
KOiK10904.
OMAiDILDNPC.
OrthoDBiEOG7MSMPZ.
PhylomeDBiQ9BVW5.
TreeFamiTF313290.

Enzyme and pathway databases

ReactomeiR-HSA-5693607. Processing of DNA double-strand break ends.

Miscellaneous databases

ChiTaRSiTIPIN. human.
GeneWikiiTIPIN.
GenomeRNAii54962.
PROiQ9BVW5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BVW5.
CleanExiHS_TIPIN.
ExpressionAtlasiQ9BVW5. baseline and differential.
GenevisibleiQ9BVW5. HS.

Family and domain databases

InterProiIPR012923. Csm3.
[Graphical view]
PfamiPF07962. Swi3. 1 hit.
[Graphical view]
ProDomiPD089639. Swi3. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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 PRO-53.
  2. NIEHS SNPs program
    Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLY-111; SER-267 AND SER-270.
  3. "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].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT PRO-53.
  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 PRO-53.
    Tissue: Cervix.
  6. "Tipin, a novel timeless-interacting protein, is developmentally co-expressed with timeless and disrupts its self-association."
    Gotter A.L.
    J. Mol. Biol. 331:167-176(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION, VARIANT PRO-53.
  7. "Tipin and Timeless form a mutually protective complex required for genotoxic stress resistance and checkpoint function."
    Chou D.M., Elledge S.J.
    Proc. Natl. Acad. Sci. U.S.A. 103:18143-18147(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH TIMELESS; MCM6 AND MCM7, FUNCTION.
  8. "Human Tim/Timeless-interacting protein, Tipin, is required for efficient progression of S phase and DNA replication checkpoint."
    Yoshizawa-Sugata N., Masai H.
    J. Biol. Chem. 282:2729-2740(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH TIMELESS, FUNCTION.
  9. "Mammalian TIMELESS and Tipin are evolutionarily conserved replication fork-associated factors."
    Gotter A.L., Suppa C., Emanuel B.S.
    J. Mol. Biol. 366:36-52(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RPA2 AND PRDX2, SUBCELLULAR LOCATION.
  10. "The human Tim/Tipin complex coordinates an Intra-S checkpoint response to UV that slows replication fork displacement."
    Uensal-Kacmaz K., Chastain P.D., Qu P.-P., Minoo P., Cordeiro-Stone M., Sancar A., Kaufmann W.K.
    Mol. Cell. Biol. 27:3131-3142(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TIMELESS AND RPA2, FUNCTION.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "The many facets of the Tim-Tipin protein families' roles in chromosome biology."
    McFarlane R.J., Mian S., Dalgaard J.Z.
    Cell Cycle 9:700-705(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  14. "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 THR-244, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "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-222 AND THR-233, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.

Entry informationi

Entry nameiTIPIN_HUMAN
AccessioniPrimary (citable) accession number: Q9BVW5
Secondary accession number(s): B2CW64, Q9NWZ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: May 18, 2010
Last modified: July 6, 2016
This is version 114 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.