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Q9HAW4 (CLSPN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Claspin

Short name=hClaspin
Gene names
Name:CLSPN
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1339 AA.
Sequence statusComplete.
Protein existenceEvidence 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.21

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.

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13391339Claspin
PRO_0000089875

Regions

Repeat910 – 91910CKB motif 1
Repeat939 – 94810CKB motif 2
Repeat976 – 98510CKB motif 3
Coiled coil162 – 19635 Potential
Coiled coil592 – 68190 Potential

Amino acid modifications

Modified residue651Phosphoserine Ref.15 Ref.19 Ref.22
Modified residue671Phosphoserine Ref.15 Ref.19 Ref.22
Modified residue831Phosphoserine Ref.22
Modified residue2251Phosphoserine Ref.15 Ref.19 Ref.22
Modified residue7181Phosphoserine Ref.19
Modified residue7201Phosphoserine Ref.15
Modified residue7231Phosphoserine Ref.19
Modified residue8081Phosphoserine Ref.15 Ref.19
Modified residue8101Phosphoserine Ref.15 Ref.19
Modified residue8331Phosphoserine Ref.13
Modified residue8391Phosphoserine Ref.17
Modified residue8461Phosphoserine Ref.15 Ref.17
Modified residue8911N6-acetyllysine Ref.18
Modified residue9161Phosphothreonine; by CHEK1 Ref.11
Modified residue10121Phosphoserine Ref.15
Modified residue10181Phosphoserine Ref.15
Modified residue10201Phosphoserine Ref.15
Modified residue11561Phosphoserine Ref.15 Ref.17
Modified residue12891Phosphoserine Ref.15 Ref.17 Ref.19

Natural variations

Alternative sequence527 – 59064Missing in isoform 2.
VSP_036033
Alternative sequence1304 – 133936VKKRG…KYLES → KIPEKDSDWLTWSGAPIPGF FRLSFDPHG in isoform 3.
VSP_036034
Natural variant4391H → R in a breast cancer sample; somatic mutation. Ref.23
VAR_035674
Natural variant5251N → S.
Corresponds to variant rs7537203 [ dbSNP | Ensembl ].
VAR_023439
Natural variant8921P → T.
Corresponds to variant rs34390044 [ dbSNP | Ensembl ].
VAR_050867
Natural variant12801S → L.
Corresponds to variant rs35490896 [ dbSNP | Ensembl ].
VAR_050868

Experimental info

Mutagenesis9161T → A: Impairs interaction with CHEK1. Ref.8
Mutagenesis9451S → A: Impairs interaction with CHEK1. Ref.8
Mutagenesis9821S → A: No effect on interaction with CHEK1. Ref.8
Sequence conflict341S → G in AAI15026. Ref.3
Sequence conflict4461G → E in AAI15026. Ref.3
Sequence conflict6281F → S in AAG24515. Ref.1
Sequence conflict6641E → G in AAG24515. Ref.1
Sequence conflict7381F → S in AAG24515. Ref.1
Sequence conflict931 – 9333SDK → GDE in AAI15026. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 16, 2008. Version 3.
Checksum: 3F3E392D5915955F

FASTA1,339151,094
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 5F02FE258D856D5C
Show »

FASTA1,275144,167
Isoform 3 [UniParc].

Checksum: 6FF64D7891BB7484
Show »

FASTA1,332150,368

References

« Hide '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. expand/collapse author list , 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"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].
[17]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[18]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"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].
[21]"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.
[22]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"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. expand/collapse author list , 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.
RefSeqNP_001177410.1. NM_001190481.1.
NP_071394.2. NM_022111.3.
UniGeneHs.175613.

3D structure databases

ProteinModelPortalQ9HAW4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122015. 23 interactions.
IntActQ9HAW4. 5 interactions.
MINTMINT-7897460.
STRING9606.ENSP00000312995.

PTM databases

PhosphoSiteQ9HAW4.

Polymorphism databases

DMDM218512100.

Proteomic databases

PaxDbQ9HAW4.
PRIDEQ9HAW4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000251195; ENSP00000251195; ENSG00000092853. [Q9HAW4-3]
ENST00000318121; ENSP00000312995; ENSG00000092853. [Q9HAW4-1]
ENST00000373220; ENSP00000362317; ENSG00000092853. [Q9HAW4-2]
GeneID63967.
KEGGhsa:63967.
UCSCuc001bzi.3. human. [Q9HAW4-1]
uc009vux.3. human. [Q9HAW4-2]

Organism-specific databases

CTD63967.
GeneCardsGC01M036185.
HGNCHGNC:19715. CLSPN.
MIM605434. gene.
neXtProtNX_Q9HAW4.
PharmGKBPA134920757.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG314362.
HOVERGENHBG080104.
OMAEEGNQET.
OrthoDBEOG77T13Q.
PhylomeDBQ9HAW4.
TreeFamTF328925.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_578. Apoptosis.

Gene expression databases

ArrayExpressQ9HAW4.
BgeeQ9HAW4.
CleanExHS_CLSPN.
GenevestigatorQ9HAW4.

Family and domain databases

InterProIPR024147. Claspin.
IPR024146. Claspin/Claspin-like.
[Graphical view]
PANTHERPTHR14396. PTHR14396. 1 hit.
PTHR14396:SF4. PTHR14396:SF4. 1 hit.
ProtoNetSearch...

Other

GeneWikiCLSPN.
GenomeRNAi63967.
NextBio65748.
PMAP-CutDBQ2KHM3.
PROQ9HAW4.
SOURCESearch...

Entry information

Entry nameCLSPN_HUMAN
AccessionPrimary (citable) accession number: Q9HAW4
Secondary accession number(s): A6NFL4 expand/collapse secondary AC list , Q1RMC6, Q2KHM3, Q5VYG0, Q6P6H5, Q8IWI1
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: December 16, 2008
Last modified: April 16, 2014
This is version 102 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM