CHERP_HUMAN - dbPTM
CHERP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CHERP_HUMAN
UniProt AC Q8IWX8
Protein Name Calcium homeostasis endoplasmic reticulum protein
Gene Name CHERP {ECO:0000312|HGNC:HGNC:16930}
Organism Homo sapiens (Human).
Sequence Length 916
Subcellular Localization Cytoplasm . Cytoplasm, perinuclear region . Endoplasmic reticulum . Distributed throughout the cytoplasm and also localizes to the perinuclear region of both human erythroleukemia (HEL) cells and Jurkat cells. Colocalizes with ITPR1.
Protein Description Involved in calcium homeostasis, growth and proliferation..
Protein Sequence MEMPLPPDDQELRNVIDKLAQFVARNGPEFEKMTMEKQKDNPKFSFLFGGEFYSYYKCKLALEQQQLICKQQTPELEPAATMPPLPQPPLAPAAPIPPAQGAPSMDELIQQSQWNLQQQEQHLLALRQEQVTAAVAHAVEQQMQKLLEETQLDMNEFDNLLQPIIDTCTKDAISAGKNWMFSNAKSPPHCELMAGHLRNRITADGAHFELRLHLIYLINDVLHHCQRKQARELLAALQKVVVPIYCTSFLAVEEDKQQKIARLLQLWEKNGYFDDSIIQQLQSPALGLGQYQATLINEYSSVVQPVQLAFQQQIQTLKTQHEEFVTSLAQQQQQQQQQQQQLQMPQMEAEVKATPPPPAPPPAPAPAPAIPPTTQPDDSKPPIQMPGSSEYEAPGGVQDPAAAGPRGPGPHDQIPPNKPPWFDQPHPVAPWGQQQPPEQPPYPHHQGGPPHCPPWNNSHEGMWGEQRGDPGWNGQRDAPWNNQPDAAWNSQFEGPWNSQHEQPPWGGGQREPPFRMQRPPHFRGPFPPHQQHPQFNQPPHPHNFNRFPPRFMQDDFPPRHPFERPPYPHRFDYPQGDFPAEMGPPHHHPGHRMPHPGINEHPPWAGPQHPDFGPPPHGFNGQPPHMRRQGPPHINHDDPSLVPNVPYFDLPAGLMAPLVKLEDHEYKPLDPKDIRLPPPMPPSERLLAAVEAFYSPPSHDRPRNSEGWEQNGLYEFFRAKMRARRRKGQEKRNSGPSRSRSRSKSRGRSSSRSNSRSSKSSGSYSRSRSRSCSRSYSRSRSRSRSRSRSSRSRSRSQSRSRSKSYSPGRRRRSRSRSPTPPSSAGLGSNSAPPIPDSRLGEENKGHQMLVKMGWSGSGGLGAKEQGIQDPIKGGDVRDKWDQYKGVGVALDDPYENYRRNKSYSFIARMKARDECK
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
1Acetylation-------MEMPLPPD
-------CCCCCCCC		10.0622814378
18UbiquitinationELRNVIDKLAQFVAR
HHHHHHHHHHHHHHH		34.3022817900
18AcetylationELRNVIDKLAQFVAR
HHHHHHHHHHHHHHH		34.3019608861
177 (in isoform 1)Ubiquitination-47.3421906983
177UbiquitinationKDAISAGKNWMFSNA
HHHHHCCCCCCCCCC		47.3423000965
177AcetylationKDAISAGKNWMFSNA
HHHHHCCCCCCCCCC		47.3426051181
186PhosphorylationWMFSNAKSPPHCELM
CCCCCCCCCCCCHHH		41.0523927012
239AcetylationELLAALQKVVVPIYC
HHHHHHHHHHHHHHH		37.5470933
256AcetylationFLAVEEDKQQKIARL
HHCCCHHHHHHHHHH		58.8925953088
259AcetylationVEEDKQQKIARLLQL
CCHHHHHHHHHHHHH		35.5225953088
354PhosphorylationMEAEVKATPPPPAPP
HHHHHHCCCCCCCCC		30.5226074081
510MethylationPPWGGGQREPPFRMQ
CCCCCCCCCCCCCCC		62.76-
546DimethylationPHPHNFNRFPPRFMQ
CCCCCCCCCCCCCCC		41.11-
546MethylationPHPHNFNRFPPRFMQ
CCCCCCCCCCCCCCC		41.11-
667AcetylationKLEDHEYKPLDPKDI
ECCCCCCCCCCHHHC		35.8025953088
675MethylationPLDPKDIRLPPPMPP
CCCHHHCCCCCCCCH		51.80-
683PhosphorylationLPPPMPPSERLLAAV
CCCCCCHHHHHHHHH		29.4920068231
694PhosphorylationLAAVEAFYSPPSHDR
HHHHHHHCCCCCCCC		27.5821712546
695PhosphorylationAAVEAFYSPPSHDRP
HHHHHHCCCCCCCCC		24.7122617229
698PhosphorylationEAFYSPPSHDRPRNS
HHHCCCCCCCCCCCC		41.2122617229
705PhosphorylationSHDRPRNSEGWEQNG
CCCCCCCCCHHHHCC		38.4723663014
714PhosphorylationGWEQNGLYEFFRAKM
HHHHCCHHHHHHHHH		16.4617360941
734PhosphorylationKGQEKRNSGPSRSRS
HCHHHHCCCCCCHHH		56.9922798277
749PhosphorylationRSKSRGRSSSRSNSR
HHHCCCCCCCCCCCC		35.1723322592
750PhosphorylationSKSRGRSSSRSNSRS
HHCCCCCCCCCCCCC		28.54-
755PhosphorylationRSSSRSNSRSSKSSG
CCCCCCCCCCCCCCC		34.4823322592
757PhosphorylationSSRSNSRSSKSSGSY
CCCCCCCCCCCCCCC		41.7723322592
763PhosphorylationRSSKSSGSYSRSRSR
CCCCCCCCCCHHHCC		23.1421406692
764PhosphorylationSSKSSGSYSRSRSRS
CCCCCCCCCHHHCCC		16.1921406692
765PhosphorylationSKSSGSYSRSRSRSC
CCCCCCCCHHHCCCC		26.0221406692
767PhosphorylationSSGSYSRSRSRSCSR
CCCCCCHHHCCCCCH		28.7721406692
769PhosphorylationGSYSRSRSRSCSRSY
CCCCHHHCCCCCHHH		29.7724719451
773PhosphorylationRSRSRSCSRSYSRSR
HHHCCCCCHHHHHHH		26.0520068231
775PhosphorylationRSRSCSRSYSRSRSR
HCCCCCHHHHHHHHH		15.9220068231
776PhosphorylationSRSCSRSYSRSRSRS
CCCCCHHHHHHHHHH		13.6417081983
777PhosphorylationRSCSRSYSRSRSRSR
CCCCHHHHHHHHHHH		25.6520068231
779PhosphorylationCSRSYSRSRSRSRSR
CCHHHHHHHHHHHHH		28.7721406692
785PhosphorylationRSRSRSRSRSRSSRS
HHHHHHHHHCHHHHH		35.54-
787PhosphorylationRSRSRSRSRSSRSRS
HHHHHHHCHHHHHHH		37.4526657352
789PhosphorylationRSRSRSRSSRSRSRS
HHHHHCHHHHHHHHH		31.2026657352
792PhosphorylationSRSRSSRSRSRSQSR
HHCHHHHHHHHHHHH		36.23-
794PhosphorylationSRSSRSRSRSQSRSR
CHHHHHHHHHHHHHH		37.2126657352
798PhosphorylationRSRSRSQSRSRSKSY
HHHHHHHHHHHCCCC		33.21-
800PhosphorylationRSRSQSRSRSKSYSP
HHHHHHHHHCCCCCC		46.2624719451
802PhosphorylationRSQSRSRSKSYSPGR
HHHHHHHCCCCCCCC		27.4825849741
804PhosphorylationQSRSRSKSYSPGRRR
HHHHHCCCCCCCCCC		31.9026055452
805PhosphorylationSRSRSKSYSPGRRRR
HHHHCCCCCCCCCCC		23.7121955146
806PhosphorylationRSRSKSYSPGRRRRS
HHHCCCCCCCCCCCC		28.1526055452
811DimethylationSYSPGRRRRSRSRSP
CCCCCCCCCCCCCCC		39.30-
813PhosphorylationSPGRRRRSRSRSPTP
CCCCCCCCCCCCCCC		32.5623927012
815PhosphorylationGRRRRSRSRSPTPPS
CCCCCCCCCCCCCCC		38.0529255136
817PhosphorylationRRRSRSRSPTPPSSA
CCCCCCCCCCCCCCC		34.0829255136
819PhosphorylationRSRSRSPTPPSSAGL
CCCCCCCCCCCCCCC		49.4229255136
822PhosphorylationSRSPTPPSSAGLGSN
CCCCCCCCCCCCCCC		33.7429255136
823PhosphorylationRSPTPPSSAGLGSNS
CCCCCCCCCCCCCCC		31.9329255136
828PhosphorylationPSSAGLGSNSAPPIP
CCCCCCCCCCCCCCC		32.4329255136
830PhosphorylationSAGLGSNSAPPIPDS
CCCCCCCCCCCCCCC		43.8029255136
837PhosphorylationSAPPIPDSRLGEENK
CCCCCCCCCCCCCCC		24.8523927012
838DimethylationAPPIPDSRLGEENKG
CCCCCCCCCCCCCCC		54.84-
844SumoylationSRLGEENKGHQMLVK
CCCCCCCCCCEEEEE		62.1328112733
844SumoylationSRLGEENKGHQMLVK
CCCCCCCCCCEEEEE		62.13-
848SulfoxidationEENKGHQMLVKMGWS
CCCCCCEEEEECCCC		3.7421406390
855PhosphorylationMLVKMGWSGSGGLGA
EEEECCCCCCCCCCC		19.8325159151
857PhosphorylationVKMGWSGSGGLGAKE
EECCCCCCCCCCCHH		24.9525159151
863UbiquitinationGSGGLGAKEQGIQDP
CCCCCCCHHHCCCCC		49.0932015554
863AcetylationGSGGLGAKEQGIQDP
CCCCCCCHHHCCCCC		49.0926051181
872UbiquitinationQGIQDPIKGGDVRDK
HCCCCCCCCCCHHHH		63.3333845483
872SumoylationQGIQDPIKGGDVRDK
HCCCCCCCCCCHHHH		63.3328112733
872AcetylationQGIQDPIKGGDVRDK
HCCCCCCCCCCHHHH		63.3326051181
879AcetylationKGGDVRDKWDQYKGV
CCCCHHHHHHHCCCE		41.9519608861
879UbiquitinationKGGDVRDKWDQYKGV
CCCCHHHHHHHCCCE		41.9522817900
883PhosphorylationVRDKWDQYKGVGVAL
HHHHHHHCCCEEEEC		13.7717360941
884UbiquitinationRDKWDQYKGVGVALD
HHHHHHCCCEEEECC		41.3032015554
894PhosphorylationGVALDDPYENYRRNK
EEECCCHHHHHHCCC		24.6528796482
897PhosphorylationLDDPYENYRRNKSYS
CCCHHHHHHCCCCCH		10.0628796482
901AcetylationYENYRRNKSYSFIAR
HHHHHCCCCCHHHHH		49.3019608861
901UbiquitinationYENYRRNKSYSFIAR
HHHHHCCCCCHHHHH		49.30-
901MethylationYENYRRNKSYSFIAR
HHHHHCCCCCHHHHH		49.30-
902PhosphorylationENYRRNKSYSFIARM
HHHHCCCCCHHHHHH		29.5623401153
903PhosphorylationNYRRNKSYSFIARMK
HHHCCCCCHHHHHHH		14.8128796482
904PhosphorylationYRRNKSYSFIARMKA
HHCCCCCHHHHHHHH		19.7823401153
908MethylationKSYSFIARMKARDEC
CCCHHHHHHHHHHHC		23.48-
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 CHERP_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CHERP_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 CHERP_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PDE6A_HUMANPDE6Aphysical
22939629
ZN827_HUMANZNF827physical
22939629
PUR4_HUMANPFASphysical
22939629
RU17_HUMANSNRNP70physical
22365833
PR40A_HUMANPRPF40Aphysical
22365833
SF3B4_HUMANSF3B4physical
22365833
U2AF2_HUMANU2AF2physical
22365833
U2AF1_HUMANU2AF1physical
22365833
CCAR1_HUMANCCAR1physical
22365833
RBM23_HUMANRBM23physical
22365833
RBM39_HUMANRBM39physical
22365833
SNUT1_HUMANSART1physical
22365833
PR38A_HUMANPRPF38Aphysical
22365833
SNIP1_HUMANSNIP1physical
22365833
DHX8_HUMANDHX8physical
22365833
RNPS1_HUMANRNPS1physical
22365833
F10C1_HUMANFRA10AC1physical
22365833
RBM7_HUMANRBM7physical
22365833
ARGL1_HUMANARGLU1physical
22365833
AGGF1_HUMANAGGF1physical
22365833
PPIL4_HUMANPPIL4physical
22365833
SNR27_HUMANSNRNP27physical
22365833
HNRH3_HUMANHNRNPH3physical
22365833
TTC14_HUMANTTC14physical
22365833
RACK1_HUMANGNB2L1physical
22365833
LUC7L_HUMANLUC7Lphysical
22365833
EWS_HUMANEWSR1physical
21988832
SR140_HUMANU2SURPphysical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CHERP_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-815; SER-817; THR-819 AND SER-822, AND MASSSPECTROMETRY.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-18; LYS-879 AND LYS-901, ANDMASS SPECTROMETRY.
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-815 AND SER-817, ANDMASS SPECTROMETRY.
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-815; SER-817; THR-819 AND SER-822, 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-813; SER-815; SER-817;THR-819; SER-822; SER-823; SER-828; SER-830 AND SER-904, AND MASSSPECTROMETRY.

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