Q9HAW4 (CLSPN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Claspin
Short name=hClaspin

Gene names

Name:

CLSPN

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1339 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Required for checkpoint mediated cell cycle arrest in response to inhibition of DNA replication or to DNA damage induced by both ionizing and UV irradiation. Adapter protein which binds to BRCA1 and the checkpoint kinase CHEK1 and facilitates the ATR-dependent phosphorylation of both proteins. Can also bind specifically to branched DNA structures and may associate with S-phase chromatin following formation of the pre-replication complex (pre-RC). This may indicate a role for this protein as a sensor which monitors the integrity of DNA replication forks. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8
Subunit structure	Interacts (phosphorylation-dependent) with CHEK1; regulates CLSPN function in checkpoint for DNA damage and replication. Interacts with ATR and RAD9A and these interactions are slightly reduced during checkpoint activation. Interacts with BRCA1 and this interaction increases during checkpoint activation. Interacts with TIMELESS. Ref.4 Ref.7 Ref.8 Ref.11 Ref.12 Ref.14
Subcellular location	Nucleus Ref.4.
Induction	Expression peaks at S/G2 phases of the cell cycle. Ref.4
Domain	The C-terminus of the protein contains 3 potential CHEK1-binding motifs (CKB motifs). Potential phosphorylation sites within CKB motif 1 and CKB motif 2 are required for interaction with CHEK1.
Post-translational modification	Phosphorylated. Undergoes ATR-dependent phosphorylation by CHEK1 during activation of DNA replication or damage checkpoints. Phosphorylation by CSNK1G1/CK1 promotes CHEK1 binding. Ref.4 Ref.7 Ref.11 Ref.20 Ubiquitinated by the anaphase promoting complex/cyclosome (APC/C) during G1 phase, leading to its degradation by the proteasome. Ubiquitination is mediated via its interaction with FZR1/CDH1. Following DNA damage, it is deubiquitinated by USP28 in G2 phase, preventing its degradation. Ref.9 Ref.14
Sequence similarities	Belongs to the claspin family.
Sequence caution	The sequence AAH38991.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence. The sequence AAH62215.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

Ontologies

Keywords
Biological process	Cell cycle DNA damage DNA repair
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil Repeat
Ligand	DNA-binding
PTM	Acetylation Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA repair Inferred from electronic annotation. Source: UniProtKB-KW DNA replication Traceable author statement. Source: Reactome G2 DNA damage checkpoint Inferred from direct assay Ref.14. Source: UniProtKB activation of protein kinase activity Inferred from direct assay PubMed 16885022. Source: UniProtKB cellular component disassembly involved in execution phase of apoptosis Traceable author statement. Source: Reactome mitotic DNA replication checkpoint Inferred from mutant phenotype PubMed 16885022. Source: UniProtKB peptidyl-serine phosphorylation Inferred from direct assay PubMed 16885022. Source: UniProtKB
Cellular_component	nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CHEK1	O14757	5	EBI-1369377,EBI-974488
FZR1	Q9UM11	4	EBI-1369377,EBI-724997

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9HAW4-1)

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.

Isoform 2 (identifier: Q9HAW4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     527-590: Missing.

Isoform 3 (identifier: Q9HAW4-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1304-1339: VKKRGPSFMTSPSPKHLKTDDSTSGLTRSIFKYLES → KIPEKDSDWLTWSGAPIPGFFRLSFDPHG

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1339	1339	Claspin		PRO_0000089875
Regions
	Repeat	910 – 919	10	CKB motif 1
	Repeat	939 – 948	10	CKB motif 2
	Repeat	976 – 985	10	CKB motif 3
	Coiled coil	162 – 196	35	Potential
	Coiled coil	592 – 681	90	Potential
Amino acid modifications
	Modified residue	65	1	Phosphoserine Ref.15 Ref.18 Ref.21
	Modified residue	67	1	Phosphoserine Ref.15 Ref.18 Ref.21
	Modified residue	83	1	Phosphoserine Ref.21
	Modified residue	225	1	Phosphoserine Ref.15 Ref.18 Ref.21
	Modified residue	718	1	Phosphoserine Ref.18
	Modified residue	720	1	Phosphoserine Ref.15
	Modified residue	723	1	Phosphoserine Ref.18
	Modified residue	808	1	Phosphoserine Ref.15 Ref.18
	Modified residue	810	1	Phosphoserine Ref.15 Ref.18
	Modified residue	833	1	Phosphoserine Ref.13
	Modified residue	839	1	Phosphoserine Ref.16
	Modified residue	846	1	Phosphoserine Ref.15 Ref.16
	Modified residue	891	1	N6-acetyllysine Ref.17
	Modified residue	916	1	Phosphothreonine; by CHEK1 Ref.11
	Modified residue	1012	1	Phosphoserine Ref.15
	Modified residue	1018	1	Phosphoserine Ref.15
	Modified residue	1020	1	Phosphoserine Ref.15
	Modified residue	1156	1	Phosphoserine Ref.15 Ref.16
	Modified residue	1289	1	Phosphoserine Ref.15 Ref.16 Ref.18
Natural variations
	Alternative sequence	527 – 590	64	Missing in isoform 2.		VSP_036033
	Alternative sequence	1304 – 1339	36	VKKRG…KYLES → KIPEKDSDWLTWSGAPIPGF FRLSFDPHG in isoform 3.		VSP_036034
	Natural variant	439	1	H → R in a breast cancer sample; somatic mutation. Ref.22		VAR_035674
	Natural variant	525	1	N → S. Corresponds to variant rs7537203 [ dbSNP | Ensembl ].		VAR_023439
	Natural variant	892	1	P → T. Corresponds to variant rs34390044 [ dbSNP | Ensembl ].		VAR_050867
	Natural variant	1280	1	S → L. Corresponds to variant rs35490896 [ dbSNP | Ensembl ].		VAR_050868
Experimental info
	Mutagenesis	916	1	T → A: Impairs interaction with CHEK1. Ref.8
	Mutagenesis	945	1	S → A: Impairs interaction with CHEK1. Ref.8
	Mutagenesis	982	1	S → A: No effect on interaction with CHEK1. Ref.8
	Sequence conflict	34	1	S → G in AAI15026. Ref.3
	Sequence conflict	446	1	G → E in AAI15026. Ref.3
	Sequence conflict	628	1	F → S in AAG24515. Ref.1
	Sequence conflict	664	1	E → G in AAG24515. Ref.1
	Sequence conflict	738	1	F → S in AAG24515. Ref.1
	Sequence conflict	931 – 933	3	SDK → GDE in AAI15026. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 16, 2008. Version 3. Checksum: 3F3E392D5915955F	FASTA	1,339	151,094
	10 20 30 40 50 60 MTGEVGSEVH LEINDPNVIS QEEADSPSDS GQGSYETIGP LSEGDSDEEI FVSKKLKNRK 70 80 90 100 110 120 VLQDSDSETE DTNASPEKTT YDSAEEENKE NLYAGKNTKI KRIYKTVADS DESYMEKSLY 130 140 150 160 170 180 QENLEAQVKP CLELSLQSGN STDFTTDRKS SKKHIHDKEG TAGKAKVKSK RRLEKEERKM 190 200 210 220 230 240 EKIRQLKKKE TKNQEDDVEQ PFNDSGCLLV DKDLFETGLE DENNSPLEDE ESLESIRAAV 250 260 270 280 290 300 KNKVKKHKKK EPSLESGVHS FEEGSELSKG TTRKERKAAR LSKEALKQLH SETQRLIRES 310 320 330 340 350 360 ALNLPYHMPE NKTIHDFFKR KPRPTCHGNA MALLKSSKYQ SSHHKEIIDT ANTTEMNSDH 370 380 390 400 410 420 HSKGSEQTTG AENEVETNAL PVVSKETQII TGSDESCRKD LVKNEELEIQ EKQKQSDIRP 430 440 450 460 470 480 SPGDSSVLQQ ESNFLGNNHS EECQVGGLVA FEPHALEGEG PQNPEETDEK VEEPEQQNKS 490 500 510 520 530 540 SAVGPPEKVR RFTLDRLKQL GVDVSIKPRL GADEDSFVIL EPETNRELEA LKQRFWKHAN 550 560 570 580 590 600 PAAKPRAGQT VNVNVIVKDM GTDGKEELKA DVVPVTLAPK KLDGASHTKP GEKLQVLKAK 610 620 630 640 650 660 LQEAMKLRRF EERQKRQALF KLDNEDGFEE EEEEEEEMTD ESEEDGEEKV EKEEKEEELE 670 680 690 700 710 720 EEEEKEEEEE EEGNQETAEF LLSSEEIETK DEKEMDKENN DGSSEIGKAV GFLSVPKSLS 730 740 750 760 770 780 SDSTLLLFKD SSSKMGYFPT EEKSETDENS GKQPSKLDED DSCSLLTKES SHNSSFELIG 790 800 810 820 830 840 STIPSYQPCN RQTGRGTSFF PTAGGFRSPS PGLFRASLVS SASKSSGKLS EPSLPIEDSQ 850 860 870 880 890 900 DLYNASPEPK TLFLGAGDFQ FCLEDDTQSQ LLDADGFLNV RNHRNQYQAL KPRLPLASMD 910 920 930 940 950 960 ENAMDANMDE LLDLCTGKFT SQAEKHLPRK SDKKENMEEL LNLCSGKFTS QDASTPASSE 970 980 990 1000 1010 1020 LNKQEKESSM GDPMEEALAL CSGSFPTDKE EEDEEEEFGD FRLVSNDNEF DSDEDEHSDS 1030 1040 1050 1060 1070 1080 GNDLALEDHE DDDEEELLKR SEKLKRQMRL RKYLEDEAEV SGSDVGSEDE YDGEEIDEYE 1090 1100 1110 1120 1130 1140 EDVIDEVLPS DEELQSQIKK IHMKTMLDDD KRQLRLYQER YLADGDLHSD GPGRMRKFRW 1150 1160 1170 1180 1190 1200 KNIDDASQMD LFHRDSDDDQ TEEQLDESEA RWRKERIERE QWLRDMAQQG KITAEEEEEI 1210 1220 1230 1240 1250 1260 GEDSQFMILA KKVTAKALQK NASRPMVIQE SKSLLRNPFE AIRPGSAQQV KTGSLLNQPK 1270 1280 1290 1300 1310 1320 AVLQKLAALS DHNPSAPRNS RNFVFHTLSP VKAEAAKESS KSQVKKRGPS FMTSPSPKHL 1330 KTDDSTSGLT RSIFKYLES
	Isoform 2 [UniParc]. Checksum: 5F02FE258D856D5C	FASTA	1,275	144,167
	10 20 30 40 50 60 MTGEVGSEVH LEINDPNVIS QEEADSPSDS GQGSYETIGP LSEGDSDEEI FVSKKLKNRK 70 80 90 100 110 120 VLQDSDSETE DTNASPEKTT YDSAEEENKE NLYAGKNTKI KRIYKTVADS DESYMEKSLY 130 140 150 160 170 180 QENLEAQVKP CLELSLQSGN STDFTTDRKS SKKHIHDKEG TAGKAKVKSK RRLEKEERKM 190 200 210 220 230 240 EKIRQLKKKE TKNQEDDVEQ PFNDSGCLLV DKDLFETGLE DENNSPLEDE ESLESIRAAV 250 260 270 280 290 300 KNKVKKHKKK EPSLESGVHS FEEGSELSKG TTRKERKAAR LSKEALKQLH SETQRLIRES 310 320 330 340 350 360 ALNLPYHMPE NKTIHDFFKR KPRPTCHGNA MALLKSSKYQ SSHHKEIIDT ANTTEMNSDH 370 380 390 400 410 420 HSKGSEQTTG AENEVETNAL PVVSKETQII TGSDESCRKD LVKNEELEIQ EKQKQSDIRP 430 440 450 460 470 480 SPGDSSVLQQ ESNFLGNNHS EECQVGGLVA FEPHALEGEG PQNPEETDEK VEEPEQQNKS 490 500 510 520 530 540 SAVGPPEKVR RFTLDRLKQL GVDVSIKPRL GADEDSFVIL EPETNRGEKL QVLKAKLQEA 550 560 570 580 590 600 MKLRRFEERQ KRQALFKLDN EDGFEEEEEE EEEMTDESEE DGEEKVEKEE KEEELEEEEE 610 620 630 640 650 660 KEEEEEEEGN QETAEFLLSS EEIETKDEKE MDKENNDGSS EIGKAVGFLS VPKSLSSDST 670 680 690 700 710 720 LLLFKDSSSK MGYFPTEEKS ETDENSGKQP SKLDEDDSCS LLTKESSHNS SFELIGSTIP 730 740 750 760 770 780 SYQPCNRQTG RGTSFFPTAG GFRSPSPGLF RASLVSSASK SSGKLSEPSL PIEDSQDLYN 790 800 810 820 830 840 ASPEPKTLFL GAGDFQFCLE DDTQSQLLDA DGFLNVRNHR NQYQALKPRL PLASMDENAM 850 860 870 880 890 900 DANMDELLDL CTGKFTSQAE KHLPRKSDKK ENMEELLNLC SGKFTSQDAS TPASSELNKQ 910 920 930 940 950 960 EKESSMGDPM EEALALCSGS FPTDKEEEDE EEEFGDFRLV SNDNEFDSDE DEHSDSGNDL 970 980 990 1000 1010 1020 ALEDHEDDDE EELLKRSEKL KRQMRLRKYL EDEAEVSGSD VGSEDEYDGE EIDEYEEDVI 1030 1040 1050 1060 1070 1080 DEVLPSDEEL QSQIKKIHMK TMLDDDKRQL RLYQERYLAD GDLHSDGPGR MRKFRWKNID 1090 1100 1110 1120 1130 1140 DASQMDLFHR DSDDDQTEEQ LDESEARWRK ERIEREQWLR DMAQQGKITA EEEEEIGEDS 1150 1160 1170 1180 1190 1200 QFMILAKKVT AKALQKNASR PMVIQESKSL LRNPFEAIRP GSAQQVKTGS LLNQPKAVLQ 1210 1220 1230 1240 1250 1260 KLAALSDHNP SAPRNSRNFV FHTLSPVKAE AAKESSKSQV KKRGPSFMTS PSPKHLKTDD 1270 STSGLTRSIF KYLES
	Isoform 3 [UniParc]. Checksum: 6FF64D7891BB7484	FASTA	1,332	150,368
	10 20 30 40 50 60 MTGEVGSEVH LEINDPNVIS QEEADSPSDS GQGSYETIGP LSEGDSDEEI FVSKKLKNRK 70 80 90 100 110 120 VLQDSDSETE DTNASPEKTT YDSAEEENKE NLYAGKNTKI KRIYKTVADS DESYMEKSLY 130 140 150 160 170 180 QENLEAQVKP CLELSLQSGN STDFTTDRKS SKKHIHDKEG TAGKAKVKSK RRLEKEERKM 190 200 210 220 230 240 EKIRQLKKKE TKNQEDDVEQ PFNDSGCLLV DKDLFETGLE DENNSPLEDE ESLESIRAAV 250 260 270 280 290 300 KNKVKKHKKK EPSLESGVHS FEEGSELSKG TTRKERKAAR LSKEALKQLH SETQRLIRES 310 320 330 340 350 360 ALNLPYHMPE NKTIHDFFKR KPRPTCHGNA MALLKSSKYQ SSHHKEIIDT ANTTEMNSDH 370 380 390 400 410 420 HSKGSEQTTG AENEVETNAL PVVSKETQII TGSDESCRKD LVKNEELEIQ EKQKQSDIRP 430 440 450 460 470 480 SPGDSSVLQQ ESNFLGNNHS EECQVGGLVA FEPHALEGEG PQNPEETDEK VEEPEQQNKS 490 500 510 520 530 540 SAVGPPEKVR RFTLDRLKQL GVDVSIKPRL GADEDSFVIL EPETNRELEA LKQRFWKHAN 550 560 570 580 590 600 PAAKPRAGQT VNVNVIVKDM GTDGKEELKA DVVPVTLAPK KLDGASHTKP GEKLQVLKAK 610 620 630 640 650 660 LQEAMKLRRF EERQKRQALF KLDNEDGFEE EEEEEEEMTD ESEEDGEEKV EKEEKEEELE 670 680 690 700 710 720 EEEEKEEEEE EEGNQETAEF LLSSEEIETK DEKEMDKENN DGSSEIGKAV GFLSVPKSLS 730 740 750 760 770 780 SDSTLLLFKD SSSKMGYFPT EEKSETDENS GKQPSKLDED DSCSLLTKES SHNSSFELIG 790 800 810 820 830 840 STIPSYQPCN RQTGRGTSFF PTAGGFRSPS PGLFRASLVS SASKSSGKLS EPSLPIEDSQ 850 860 870 880 890 900 DLYNASPEPK TLFLGAGDFQ FCLEDDTQSQ LLDADGFLNV RNHRNQYQAL KPRLPLASMD 910 920 930 940 950 960 ENAMDANMDE LLDLCTGKFT SQAEKHLPRK SDKKENMEEL LNLCSGKFTS QDASTPASSE 970 980 990 1000 1010 1020 LNKQEKESSM GDPMEEALAL CSGSFPTDKE EEDEEEEFGD FRLVSNDNEF DSDEDEHSDS 1030 1040 1050 1060 1070 1080 GNDLALEDHE DDDEEELLKR SEKLKRQMRL RKYLEDEAEV SGSDVGSEDE YDGEEIDEYE 1090 1100 1110 1120 1130 1140 EDVIDEVLPS DEELQSQIKK IHMKTMLDDD KRQLRLYQER YLADGDLHSD GPGRMRKFRW 1150 1160 1170 1180 1190 1200 KNIDDASQMD LFHRDSDDDQ TEEQLDESEA RWRKERIERE QWLRDMAQQG KITAEEEEEI 1210 1220 1230 1240 1250 1260 GEDSQFMILA KKVTAKALQK NASRPMVIQE SKSLLRNPFE AIRPGSAQQV KTGSLLNQPK 1270 1280 1290 1300 1310 1320 AVLQKLAALS DHNPSAPRNS RNFVFHTLSP VKAEAAKESS KSQKIPEKDS DWLTWSGAPI 1330 PGFFRLSFDP HG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Claspin, a novel protein required for the activation of Chk1 during a DNA replication checkpoint response in Xenopus egg extracts." Kumagai A., Dunphy W.G. Mol. Cell 6:839-849(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[2]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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] (ISOFORMS 1 AND 2). Tissue: Skin.
[4]	"Human claspin is required for replication checkpoint control." Chini C.C.S., Chen J. J. Biol. Chem. 278:30057-30062(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH CHEK1; ATR AND RAD9A, SUBCELLULAR LOCATION, INDUCTION, PHOSPHORYLATION.
[5]	"ATR, claspin and the Rad9-Rad1-Hus1 complex regulate Chk1 and Cdc25A in the absence of DNA damage." Sorensen C.S., Syljuasen R.G., Lukas J., Bartek J. Cell Cycle 3:941-945(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[6]	"Human claspin is a ring-shaped DNA-binding protein with high affinity to branched DNA structures." Sar F., Lindsey-Boltz L.A., Subramanian D., Croteau D.L., Hutsell S.Q., Griffith J.D., Sancar A. J. Biol. Chem. 279:39289-39295(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[7]	"Human claspin works with BRCA1 to both positively and negatively regulate cell proliferation." Lin S.-Y., Li K., Stewart G.S., Elledge S.J. Proc. Natl. Acad. Sci. U.S.A. 101:6484-6489(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH BRCA1, PHOSPHORYLATION BY ATR.
[8]	"DNA-dependent phosphorylation of Chk1 and claspin in a human cell-free system." Clarke C.A.L., Clarke P.R. Biochem. J. 388:705-712(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH CHEK1, MUTAGENESIS OF THR-916; SER-945 AND SER-982.
[9]	"A role for the deubiquitinating enzyme USP28 in control of the DNA-damage response." Zhang D., Zaugg K., Mak T.W., Elledge S.J. Cell 126:529-542(2006) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION, DEUBIQUITINATION BY USP28.
[10]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[11]	"Repeated phosphopeptide motifs in human Claspin are phosphorylated by Chk1 and mediate Claspin function." Chini C.C., Chen J. J. Biol. Chem. 281:33276-33282(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT THR-916 BY CHEK1, INTERACTION WITH CHEK1.
[12]	"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 TIMELESS.
[13]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-833, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[14]	"The Cdc14B-Cdh1-Plk1 axis controls the G2 DNA-damage-response checkpoint." Bassermann F., Frescas D., Guardavaccaro D., Busino L., Peschiaroli A., Pagano M. Cell 134:256-267(2008) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION BY THE APC/C COMPLEX, DEUBIQUITINATION BY USP28, INTERACTION WITH FZR1.
[15]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-67; SER-225; SER-720; SER-808; SER-810; SER-846; SER-1012; SER-1018; SER-1020; SER-1156 AND SER-1289, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"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-839; SER-846; SER-1156 AND SER-1289, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[17]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-891, MASS SPECTROMETRY.
[18]	"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-65; SER-67; SER-225; SER-718; SER-723; SER-808; SER-810 AND SER-1289, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[19]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]	"Role for casein kinase 1 in the phosphorylation of Claspin on critical residues necessary for the activation of Chk1." Meng Z., Capalbo L., Glover D.M., Dunphy W.G. Mol. Biol. Cell 22:2834-2847(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION BY CSNK1G1/CK1.
[21]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-67; SER-83 AND SER-225, MASS SPECTROMETRY.
[22]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] ARG-439.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF297866 mRNA. Translation: AAG24515.1. AL354864 Genomic DNA. Translation: CAH73807.2. BC038991 mRNA. Translation: AAH38991.1. Sequence problems. BC062215 mRNA. Translation: AAH62215.1. Sequence problems. BC113116 mRNA. Translation: AAI13117.1. BC115025 mRNA. Translation: AAI15026.1. BC137279 mRNA. Translation: AAI37280.1. BC140789 mRNA. Translation: AAI40790.1.
IPI	IPI00186968. IPI00748041. IPI00879588.
RefSeq	NP_001177410.1. NM_001190481.1. NP_071394.2. NM_022111.3.
UniGene	Hs.175613.
3D structure databases
ProteinModelPortal	Q9HAW4.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9HAW4. 2 interactions.
STRING	9606.ENSP00000312995.
PTM databases
PhosphoSite	Q9HAW4.
Polymorphism databases
DMDM	218512100.
Proteomic databases
PaxDb	Q9HAW4.
PRIDE	Q9HAW4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000251195; ENSP00000251195; ENSG00000092853. ENST00000318121; ENSP00000312995; ENSG00000092853. ENST00000373220; ENSP00000362317; ENSG00000092853.
GeneID	63967.
KEGG	hsa:63967.
UCSC	uc001bzi.3. human. uc009vux.3. human.
Organism-specific databases
CTD	63967.
GeneCards	GC01M036185.
HGNC	HGNC:19715. CLSPN.
MIM	605434. gene.
neXtProt	NX_Q9HAW4.
PharmGKB	PA134920757.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG314362.
HOVERGEN	HBG080104.
OMA	KKLHSET.
PhylomeDB	Q9HAW4.
Enzyme and pathway databases
Reactome	REACT_115566. Cell Cycle. REACT_578. Apoptosis.
Gene expression databases
ArrayExpress	Q9HAW4.
Bgee	Q9HAW4.
CleanEx	HS_CLSPN.
Genevestigator	Q9HAW4.
GermOnline	ENSG00000092853. Homo sapiens.
Family and domain databases
InterPro	IPR024147. Claspin. IPR024146. Claspin/Claspin-like. [Graphical view]
PANTHER	PTHR14396. PTHR14396. 1 hit. PTHR14396:SF4. PTHR14396:SF4. 1 hit.
ProtoNet	Search...
Other
GenomeRNAi	63967.
NextBio	65748.
PMAP-CutDB	Q2KHM3.
SOURCE	Search...

Entry information

Entry name

CLSPN_HUMAN

Accession

Primary (citable) accession number: Q9HAW4
Secondary accession number(s): A6NFL4 , Q1RMC6, Q2KHM3, Q5VYG0, Q6P6H5, Q8IWI1

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2005
Last sequence update:	December 16, 2008
Last modified:	May 1, 2013
This is version 93 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.