CSPP1_HUMAN - dbPTM
CSPP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CSPP1_HUMAN
UniProt AC Q1MSJ5
Protein Name Centrosome and spindle pole-associated protein 1
Gene Name CSPP1
Organism Homo sapiens (Human).
Sequence Length 1256
Subcellular Localization Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytoskeleton, spindle pole. Associated with mitotic spindles.
Protein Description May play a role in cell-cycle-dependent microtubule organization..
Protein Sequence MLFPLQVAAVTSSVRDDPLEHCVSPRTRARSPEICKMADNLDEFIEEQKARLAEDKAELESDPPYMEMKGKLSAKLSENSKILISMAKENIPPNSQQTRGSLGIDYGLSLPLGEDYERKKHKLKEELRQDYRRYLTQGITQGKRKKNFLSTSETDPSTLGVSLPIGERLSAKERLKLERNKEYNQFLRGKEESSEKFRQVEKSTEPKSQRNKKPIGQVKPDLTSQIQTSCENSEGPRKDVLTPSEAYEELLNQRRLEEDRYRQLDDEIELRNRRIIKKANEEVGISNLKHQRFASKAGIPDRRFHRFNEDRVFDRRYHRPDQDPEVSEEMDERFRYESDFDRRLSRVYTNDRMHRNKRGNMPPMEHDGDVIEQSNIRISSAENKSAPDNETSKSANQDTCSPFAGMLFGGEDRELIQRRKEKYRLELLEQMAEQQRNKRREKDLELRVAASGAQDPEKSPDRLKQFSVAPRHFEEMIPPERPRIAFQTPLPPLSAPSVPPIPSVHPVPSQNEDLRSGLSSALGEMVSPRIAPLPPPPLLPPLATNYRTPYDDAYYFYGSRNTFDPSLAYYGSGMMGVQPAAYVSAPVTHQLAQPVVNTVGQNELKITSDQVINSGLIFEDKPKPSKQSLQSYQEALQQQIREREERRKKEREEKEEYEAKLEAEMRTYNPWGKGGGGAPLRDAKGNLITDLNRMHRQNIDAYHNPDARTYEDKRAVVSLDPNLATSNAENLEDAANKSSGHMQTQSSPFARGNVFGEPPTELQIKQQELYKNFLRFQIEEKKQREEAERERLRIAEEKEERRLAEQRARIQQEYEEEQEKKREKEEEQRLKNEEHIRLAEERQKEAERKKKEEEEKYNLQLQHYCERDNLIGEETKHMRQPSPIVPALQNKIASKLQRPPSVDSIIRSFIHESSMSRAQSPPVPARKNQLRAEEEKKNVIMELSEMRKQLRSEERRLQERLLHMDSDDEIPIRKKERNPMDIFDMARHRLQAPVRRQSPKGLDAATFQNVHDFNELKDRDSETRVDLKFMYLDPPRDHHTLEIQQQALLREQQKRLNRIKMQEGAKVDLDAIPSAKVREQRMPRDDTSDFLKNSLLESDSAFIGAYGETYPAIEDDVLPPPSQLPSARERRRNKWKGLDIDSSRPNVAPDGLSLKSISSVNVDELRVRNEERMRRLNEFHNKPINTDDESSLVDPDDIMKHIGDDGSNSVATEPWLRPGTSETLKRFMAEQLNQEQQQIPGKPGTFTWQGLSTAHG
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
24PhosphorylationDPLEHCVSPRTRARS
CCCHHCCCHHHCCCC		17.6628122231
31PhosphorylationSPRTRARSPEICKMA
CHHHCCCCHHHHHHH		26.3730576142
61PhosphorylationEDKAELESDPPYMEM
HHHHHHHCCCCCHHH		68.95-
65PhosphorylationELESDPPYMEMKGKL
HHHCCCCCHHHHCHH		15.8721945579
69MethylationDPPYMEMKGKLSAKL
CCCCHHHHCHHHHHH		39.32-
77PhosphorylationGKLSAKLSENSKILI
CHHHHHHCCCCHHHH		33.7425159151
80PhosphorylationSAKLSENSKILISMA
HHHHCCCCHHHHHHH		19.6130622161
85PhosphorylationENSKILISMAKENIP
CCCHHHHHHHHHCCC		14.8330622161
101PhosphorylationNSQQTRGSLGIDYGL
CCCCCCCCCCCCCCC		21.8228348404
136 (in isoform 1)Phosphorylation-18.80-
170PhosphorylationLPIGERLSAKERLKL
CCCCCCCCHHHHHHH		43.4427966365
183PhosphorylationKLERNKEYNQFLRGK
HHHHHHHHHHHHCCC		18.84-
203PhosphorylationKFRQVEKSTEPKSQR
HHHHHHHCCCCCCCC		25.2119664995
242PhosphorylationGPRKDVLTPSEAYEE
CCCCCCCCHHHHHHH		25.3122199227
244PhosphorylationRKDVLTPSEAYEELL
CCCCCCHHHHHHHHH		29.6226074081
247PhosphorylationVLTPSEAYEELLNQR
CCCHHHHHHHHHHHH		13.0928796482
278MethylationRNRRIIKKANEEVGI
HHHHHHHHHHHHCCC		46.14-
286PhosphorylationANEEVGISNLKHQRF
HHHHCCCCHHHHHHH		30.1325599653
289MethylationEVGISNLKHQRFASK
HCCCCHHHHHHHHHH		41.77-
336PhosphorylationEMDERFRYESDFDRR
HHHHHHCHHCHHHHH		19.64-
344 (in isoform 2)Ubiquitination-3.9021906983
367 (in isoform 2)Phosphorylation-41.5025159151
385PhosphorylationISSAENKSAPDNETS
ECCCCCCCCCCCCCC		57.5228985074
401PhosphorylationSANQDTCSPFAGMLF
CCCCCCCCCCHHHHH		25.7425159151
451PhosphorylationLELRVAASGAQDPEK
HHHHHHHCCCCCCCC		25.5630266825
459PhosphorylationGAQDPEKSPDRLKQF
CCCCCCCCHHHHHHH		30.3023401153
467PhosphorylationPDRLKQFSVAPRHFE
HHHHHHHCCCHHHHH		18.1826074081
516PhosphorylationSQNEDLRSGLSSALG
CCCHHHHHHHHHHHH		51.9223403867
527PhosphorylationSALGEMVSPRIAPLP
HHHHHHCCCCCCCCC		13.7221712546
554PhosphorylationRTPYDDAYYFYGSRN
CCCCCCCCCCCCCCC		10.9127642862
555PhosphorylationTPYDDAYYFYGSRNT
CCCCCCCCCCCCCCC		7.6427642862
557PhosphorylationYDDAYYFYGSRNTFD
CCCCCCCCCCCCCCC		9.70-
638 (in isoform 1)Ubiquitination-41.3321906983
641MethylationEALQQQIREREERRK
HHHHHHHHHHHHHHH		32.36-
643MethylationLQQQIREREERRKKE
HHHHHHHHHHHHHHH		41.02-
648AcetylationREREERRKKEREEKE
HHHHHHHHHHHHHHH		66.2712437841
649AcetylationEREERRKKEREEKEE
HHHHHHHHHHHHHHH		61.2612437851
668PhosphorylationLEAEMRTYNPWGKGG
HHHHHHHCCCCCCCC		14.63-
673UbiquitinationRTYNPWGKGGGGAPL
HHCCCCCCCCCCCCC		50.98-
686 (in isoform 2)Ubiquitination-27.8021906983
696 (in isoform 2)Ubiquitination-23.1521906983
702PhosphorylationHRQNIDAYHNPDART
HHCCCHHHCCCCCCC		9.8128796482
718PhosphorylationEDKRAVVSLDPNLAT
CCHHEEEECCCCCCC		22.0628555341
739PhosphorylationEDAANKSSGHMQTQS
HHHHHHCCCCCCCCC		34.0425627689
744PhosphorylationKSSGHMQTQSSPFAR
HCCCCCCCCCCCCCC		23.8928348404
746PhosphorylationSGHMQTQSSPFARGN
CCCCCCCCCCCCCCC		43.2828348404
747PhosphorylationGHMQTQSSPFARGNV
CCCCCCCCCCCCCCC		17.7725159151
882PhosphorylationTKHMRQPSPIVPALQ
CCCCCCCCCCHHHHH		20.9430266825
895AcetylationLQNKIASKLQRPPSV
HHHHHHHHCCCCCCH		39.3525953088
901PhosphorylationSKLQRPPSVDSIIRS
HHCCCCCCHHHHHHH		41.0430266825
904PhosphorylationQRPPSVDSIIRSFIH
CCCCCHHHHHHHHHH		20.1230266825
908PhosphorylationSVDSIIRSFIHESSM
CHHHHHHHHHHHHHC		20.3929449344
920PhosphorylationSSMSRAQSPPVPARK
HHCCCCCCCCCCHHH		30.1323401153
931PhosphorylationPARKNQLRAEEEKKN
CHHHHHHHHHHHHHH		30.1318669648
944PhosphorylationKNVIMELSEMRKQLR
HHHHHHHHHHHHHHH		18.9521815630
952PhosphorylationEMRKQLRSEERRLQE
HHHHHHHHHHHHHHH		53.0229449344
966PhosphorylationERLLHMDSDDEIPIR
HHHHCCCCCCCCCCC		39.1123927012
998PhosphorylationQAPVRRQSPKGLDAA
CCCHHHCCCCCCCHH		27.1127067055
1017UbiquitinationVHDFNELKDRDSETR
CCCHHHHCCCCCCCC		44.53-
1031 (in isoform 1)Ubiquitination-15.8721906983
1041 (in isoform 1)Ubiquitination-4.7921906983
1066UbiquitinationIKMQEGAKVDLDAIP
HHCCCCCCCCHHHCC		47.33-
1074PhosphorylationVDLDAIPSAKVREQR
CCHHHCCCHHHHHHC		34.3124719451
1076UbiquitinationLDAIPSAKVREQRMP
HHHCCCHHHHHHCCC		46.27-
1094PhosphorylationTSDFLKNSLLESDSA
CHHHHHHHHHHCCCE		32.5126074081
1098PhosphorylationLKNSLLESDSAFIGA
HHHHHHHCCCEEECC		36.5126074081
1136UbiquitinationERRRNKWKGLDIDSS
HHHHHCCCCCCCCCC		51.73-
1142PhosphorylationWKGLDIDSSRPNVAP
CCCCCCCCCCCCCCC		28.6925003641
1153PhosphorylationNVAPDGLSLKSISSV
CCCCCCCCCCCCCCC		39.0024719451
1156PhosphorylationPDGLSLKSISSVNVD
CCCCCCCCCCCCCHH		32.7522617229
1186PhosphorylationFHNKPINTDDESSLV
HCCCCCCCCCHHHCC		45.6130576142
1190PhosphorylationPINTDDESSLVDPDD
CCCCCCHHHCCCHHH		35.6527732954
1191PhosphorylationINTDDESSLVDPDDI
CCCCCHHHCCCHHHH		30.3030576142
1207PhosphorylationKHIGDDGSNSVATEP
HHHCCCCCCCCCCCC		32.6920068231
1212PhosphorylationDGSNSVATEPWLRPG
CCCCCCCCCCCCCCC		40.1920068231
1220PhosphorylationEPWLRPGTSETLKRF
CCCCCCCCHHHHHHH		26.5228348404
1221PhosphorylationPWLRPGTSETLKRFM
CCCCCCCHHHHHHHH		34.2024719451
1223PhosphorylationLRPGTSETLKRFMAE
CCCCCHHHHHHHHHH		37.0329759185
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of CSPP1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CSPP1_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of CSPP1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MR1L1_HUMANMRFAP1L1physical
25416956
ACTY_HUMANACTR1Bphysical
26186194
DCTN3_HUMANDCTN3physical
26186194
KLH13_HUMANKLHL13physical
26186194
CPNE8_HUMANCPNE8physical
26186194
DCTN4_HUMANDCTN4physical
26186194
CAZA2_HUMANCAPZA2physical
26186194
DCTN2_HUMANDCTN2physical
26186194
GAN_HUMANGANphysical
26186194
ARP10_HUMANACTR10physical
26186194
DCTN5_HUMANDCTN5physical
26186194
DCTN6_HUMANDCTN6physical
26186194
KLH26_HUMANKLHL26physical
26186194
PCM1_HUMANPCM1physical
26186194
ATP23_HUMANXRCC6BP1physical
26186194
HOME2_HUMANHOMER2physical
26186194
HOME1_HUMANHOMER1physical
26186194
NDK7_HUMANNME7physical
26186194
PXDNL_HUMANPXDNLphysical
26186194
GAN_HUMANGANphysical
28514442
DCTN6_HUMANDCTN6physical
28514442
DCTN5_HUMANDCTN5physical
28514442
ARP10_HUMANACTR10physical
28514442
DCTN4_HUMANDCTN4physical
28514442
DCTN3_HUMANDCTN3physical
28514442
HOME1_HUMANHOMER1physical
28514442
ACTY_HUMANACTR1Bphysical
28514442
ATP23_HUMANXRCC6BP1physical
28514442
NDK7_HUMANNME7physical
28514442
DCTN2_HUMANDCTN2physical
28514442
KLH26_HUMANKLHL26physical
28514442
PCM1_HUMANPCM1physical
28514442
CPNE8_HUMANCPNE8physical
28514442
SNPC1_HUMANSNAPC1physical
27173435
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615636Joubert syndrome 21 (JBTS21)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CSPP1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-527, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-920, AND MASSSPECTROMETRY.
"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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-966, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-920, AND MASSSPECTROMETRY.

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