CD2B2_HUMAN - dbPTM
CD2B2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CD2B2_HUMAN
UniProt AC O95400
Protein Name CD2 antigen cytoplasmic tail-binding protein 2
Gene Name CD2BP2
Organism Homo sapiens (Human).
Sequence Length 341
Subcellular Localization Cytoplasm. Nucleus. Predominantly nuclear.
Protein Description Involved in pre-mRNA splicing as component of the U5 snRNP complex that is involved in spliceosome assembly..
Protein Sequence MPKRKVTFQGVGDEEDEDEIIVPKKKLVDPVAGSGGPGSRFKGKHSLDSDEEEDDDDGGSSKYDILASEDVEGQEAATLPSEGGVRITPFNLQEEMEEGHFDADGNYFLNRDAQIRDSWLDNIDWVKIRERPPGQRQASDSEEEDSLGQTSMSAQALLEGLLELLLPRETVAGALRRLGARGGGKGRKGPGQPSSPQRLDRLSGLADQMVARGNLGVYQETRERLAMRLKGLGCQTLGPHNPTPPPSLDMFAEELAEEELETPTPTQRGEAESRGDGLVDVMWEYKWENTGDAELYGPFTSAQMQTWVSEGYFPDGVYCRKLDPPGGQFYNSKRIDFDLYT
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
7Phosphorylation-MPKRKVTFQGVGDE
-CCCCEEEEECCCCC
17.1824719451
24UbiquitinationEDEIIVPKKKLVDPV
CCCEEEECHHCCCCC
52.20-
26AcetylationEIIVPKKKLVDPVAG
CEEEECHHCCCCCCC
60.9326051181
26SumoylationEIIVPKKKLVDPVAG
CEEEECHHCCCCCCC
60.9328112733
26SumoylationEIIVPKKKLVDPVAG
CEEEECHHCCCCCCC
60.93-
34PhosphorylationLVDPVAGSGGPGSRF
CCCCCCCCCCCCCCC
30.7325159151
39PhosphorylationAGSGGPGSRFKGKHS
CCCCCCCCCCCCCCC
37.3626074081
39O-linked_GlycosylationAGSGGPGSRFKGKHS
CCCCCCCCCCCCCCC
37.3629351928
44AcetylationPGSRFKGKHSLDSDE
CCCCCCCCCCCCCCC
30.52-
46PhosphorylationSRFKGKHSLDSDEEE
CCCCCCCCCCCCCCC
37.0422167270
49PhosphorylationKGKHSLDSDEEEDDD
CCCCCCCCCCCCCCC
52.8222167270
60PhosphorylationEDDDDGGSSKYDILA
CCCCCCCCCHHEEEE
29.2322167270
61PhosphorylationDDDDGGSSKYDILAS
CCCCCCCCHHEEEEE
38.2122167270
63PhosphorylationDDGGSSKYDILASED
CCCCCCHHEEEEECC
15.3430576142
68PhosphorylationSKYDILASEDVEGQE
CHHEEEEECCCCCCC
30.7728464451
78PhosphorylationVEGQEAATLPSEGGV
CCCCCCCCCCCCCCE
46.3723927012
81PhosphorylationQEAATLPSEGGVRIT
CCCCCCCCCCCEEEC
52.5723927012
88PhosphorylationSEGGVRITPFNLQEE
CCCCEEECCCCCCHH
15.9726074081
107PhosphorylationHFDADGNYFLNRDAQ
CCCCCCCEECCCCCC
18.25-
118PhosphorylationRDAQIRDSWLDNIDW
CCCCCCCHHHHCCCE
21.4925159151
127UbiquitinationLDNIDWVKIRERPPG
HHCCCEEEEECCCCC
31.62-
139PhosphorylationPPGQRQASDSEEEDS
CCCCCCCCCCCCCCC
33.0720363803
141PhosphorylationGQRQASDSEEEDSLG
CCCCCCCCCCCCCCC
44.4020363803
146PhosphorylationSDSEEEDSLGQTSMS
CCCCCCCCCCCCCHH
37.3621406692
150PhosphorylationEEDSLGQTSMSAQAL
CCCCCCCCCHHHHHH
25.3029116813
151PhosphorylationEDSLGQTSMSAQALL
CCCCCCCCHHHHHHH
11.6729116813
153PhosphorylationSLGQTSMSAQALLEG
CCCCCCHHHHHHHHH
19.5928464451
176MethylationETVAGALRRLGARGG
HHHHHHHHHHHHCCC
31.10-
181MethylationALRRLGARGGGKGRK
HHHHHHHCCCCCCCC
42.35-
194PhosphorylationRKGPGQPSSPQRLDR
CCCCCCCCCHHHHHH
46.9229255136
195PhosphorylationKGPGQPSSPQRLDRL
CCCCCCCCHHHHHHH
31.5629255136
203PhosphorylationPQRLDRLSGLADQMV
HHHHHHHHHHHHHHH
32.4323090842
209SulfoxidationLSGLADQMVARGNLG
HHHHHHHHHHHCCCC
2.3421406390
236PhosphorylationLKGLGCQTLGPHNPT
HCCCCCCCCCCCCCC
37.4529496963
243PhosphorylationTLGPHNPTPPPSLDM
CCCCCCCCCCCCHHH
54.4625159151
247PhosphorylationHNPTPPPSLDMFAEE
CCCCCCCCHHHHHHH
42.6525159151
262PhosphorylationLAEEELETPTPTQRG
HHHHHHCCCCCCCCC
45.1227174698
264PhosphorylationEEELETPTPTQRGEA
HHHHCCCCCCCCCCH
46.5225159151
266PhosphorylationELETPTPTQRGEAES
HHCCCCCCCCCCHHH
33.1227174698
273PhosphorylationTQRGEAESRGDGLVD
CCCCCHHHCCCCCEE
48.9227174698
321SumoylationPDGVYCRKLDPPGGQ
CCCCEEEECCCCCCC
54.39-
321UbiquitinationPDGVYCRKLDPPGGQ
CCCCEEEECCCCCCC
54.39-
330PhosphorylationDPPGGQFYNSKRIDF
CCCCCCCCCCCCCCE
15.61-
332PhosphorylationPGGQFYNSKRIDFDL
CCCCCCCCCCCCEEC
16.36-
333AcetylationGGQFYNSKRIDFDLY
CCCCCCCCCCCEECC
50.1325953088
333UbiquitinationGGQFYNSKRIDFDLY
CCCCCCCCCCCEECC
50.13-
341PhosphorylationRIDFDLYT-------
CCCEECCC-------
39.1621712546

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 CD2B2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CD2B2_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 CD2B2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
U520_HUMANSNRNP200physical
17353931
PRP8_HUMANPRPF8physical
17353931
U5S1_HUMANEFTUD2physical
17353931
DDX23_HUMANDDX23physical
17353931
PRP6_HUMANPRPF6physical
17353931
SNUT2_HUMANUSP39physical
17353931
SNR40_HUMANSNRNP40physical
17353931
PUF60_HUMANPUF60physical
17353931
PDIA1_HUMANP4HBphysical
17353931
FSBP_HUMANRAD54Bphysical
17353931
RA54B_HUMANRAD54Bphysical
17353931
KPRA_HUMANPRPSAP1physical
17353931
KHK_HUMANKHKphysical
17353931
RUXG_HUMANSNRPGphysical
17353931
CPSF5_HUMANNUDT21physical
17353931
RUXF_HUMANSNRPFphysical
17353931
DCD_HUMANDCDphysical
17353931
CRERF_HUMANCREBRFphysical
17353931
EWS_HUMANEWSR1physical
17353931
CMBL_HUMANCMBLphysical
17353931
CD2_HUMANCD2physical
9843987
AKNA_HUMANAKNAphysical
16000308
CD2_HUMANCD2physical
16000308
PSMF1_HUMANPSMF1physical
16000308
WBP11_HUMANWBP11physical
16000308
RSMB_HUMANSNRPBphysical
16000308
PRP6_HUMANPRPF6physical
22939629
PRP8_HUMANPRPF8physical
22939629
U520_HUMANSNRNP200physical
22939629
RUXF_HUMANSNRPFphysical
22939629
SNR40_HUMANSNRNP40physical
22939629
RSMB_HUMANSNRPBphysical
22939629
SGTA_HUMANSGTAphysical
22939629
PSMD9_HUMANPSMD9physical
22939629
PSF3_HUMANGINS3physical
22939629
S10A9_HUMANS100A9physical
22939629
S10A6_HUMANS100A6physical
22939629
SAHH2_HUMANAHCYL1physical
22939629
SLD5_HUMANGINS4physical
22939629
TBL1R_HUMANTBL1XR1physical
22939629
PLP2_HUMANPLP2physical
22939629
RAB5B_HUMANRAB5Bphysical
22939629
UB2V2_HUMANUBE2V2physical
22939629
EP400_HUMANEP400physical
22939629
COTL1_HUMANCOTL1physical
22939629
SH3L1_HUMANSH3BGRLphysical
22939629
POMP_HUMANPOMPphysical
22939629
MGAP_HUMANMGAphysical
22939629
UBQL4_HUMANUBQLN4physical
22939629
PRP6_HUMANPRPF6physical
22365833
SMU1_HUMANSMU1physical
22365833
PP1A_HUMANPPP1CAphysical
22365833
RSMB_HUMANSNRPBphysical
15105431
DDX23_HUMANDDX23physical
26344197
RPC3_HUMANPOLR3Cphysical
26344197
PRP8_HUMANPRPF8physical
26344197
SNUT1_HUMANSART1physical
26344197
ACD11_HUMANACAD11physical
28514442
SNR40_HUMANSNRNP40physical
28514442
U520_HUMANSNRNP200physical
28514442
PRP8_HUMANPRPF8physical
28514442
PRP6_HUMANPRPF6physical
28514442
TXN4A_HUMANTXNL4Aphysical
28514442
U5S1_HUMANEFTUD2physical
28514442
TRAF7_HUMANTRAF7physical
28514442
KLH36_HUMANKLHL36physical
28514442
SMD1_HUMANSNRPD1physical
28514442
NAA30_HUMANNAA30physical
28514442
PRP16_HUMANDHX38physical
28514442
SMD2_HUMANSNRPD2physical
28514442
RSMB_HUMANSNRPBphysical
28514442
OBSL1_HUMANOBSL1physical
28514442
ZNHI2_HUMANZNHIT2physical
28514442
U520_HUMANSNRNP200physical
27173435
SMU1_HUMANSMU1physical
27173435
AAR2_HUMANAAR2physical
28561026
ACD11_HUMANACAD11physical
28561026
AQR_HUMANAQRphysical
28561026
CD2B2_HUMANCD2BP2physical
28561026
CDC5L_HUMANCDC5Lphysical
28561026
CWC22_HUMANCWC22physical
28561026
DDX20_HUMANDDX20physical
28561026
DDX23_HUMANDDX23physical
28561026
DDX46_HUMANDDX46physical
28561026
DDX5_HUMANDDX5physical
28561026
DHX15_HUMANDHX15physical
28561026
PRP16_HUMANDHX38physical
28561026
DHX8_HUMANDHX8physical
28561026
ECD_HUMANECDphysical
28561026
U5S1_HUMANEFTUD2physical
28561026
TCAF1_HUMANFAM115Aphysical
28561026
GEMI4_HUMANGEMIN4physical
28561026
GPTC8_HUMANGPATCH8physical
28561026
HNRL1_HUMANHNRNPUL1physical
28561026
HTSF1_HUMANHTATSF1physical
28561026
ISY1_HUMANISY1physical
28561026
KLH36_HUMANKLHL36physical
28561026
IMA5_HUMANKPNA1physical
28561026
IMA7_HUMANKPNA6physical
28561026
MFAP1_HUMANMFAP1physical
28561026
NAA30_HUMANNAA30physical
28561026
NAA35_HUMANNAA35physical
28561026
NEDD1_HUMANNEDD1physical
28561026
NONO_HUMANNONOphysical
28561026
PHF5A_HUMANPHF5Aphysical
28561026
PLRG1_HUMANPLRG1physical
28561026
PNISR_HUMANPNISRphysical
28561026
PP1A_HUMANPPP1CAphysical
28561026
PP1B_HUMANPPP1CBphysical
28561026
PP1G_HUMANPPP1CCphysical
28561026
PRP19_HUMANPRPF19physical
28561026
PRPF3_HUMANPRPF3physical
28561026
PRP31_HUMANPRPF31physical
28561026
PR38B_HUMANPRPF38Bphysical
28561026
PRP4_HUMANPRPF4physical
28561026
PRP4B_HUMANPRPF4Bphysical
28561026
PRP6_HUMANPRPF6physical
28561026
PRP8_HUMANPRPF8physical
28561026
PSPC1_HUMANPSPC1physical
28561026
RBM42_HUMANRBM42physical
28561026
SNUT1_HUMANSART1physical
28561026
SF3A1_HUMANSF3A1physical
28561026
SF3A3_HUMANSF3A3physical
28561026
SF3B1_HUMANSF3B1physical
28561026
SF3B2_HUMANSF3B2physical
28561026
SF3B3_HUMANSF3B3physical
28561026
SFPQ_HUMANSFPQphysical
28561026
SLU7_HUMANSLU7physical
28561026
U520_HUMANSNRNP200physical
28561026
SNR27_HUMANSNRNP27physical
28561026
SNR40_HUMANSNRNP40physical
28561026
RU17_HUMANSNRNP70physical
28561026
RU2A_HUMANSNRPA1physical
28561026
RSMB_HUMANSNRPBphysical
28561026
RU2B_HUMANSNRPB2physical
28561026
SMD1_HUMANSNRPD1physical
28561026
SMD3_HUMANSNRPD3physical
28561026
RUXE_HUMANSNRPEphysical
28561026
RSMN_HUMANSNRPNphysical
28561026
SNW1_HUMANSNW1physical
28561026
SRRM1_HUMANSRRM1physical
28561026
SRRM2_HUMANSRRM2physical
28561026
SRSF1_HUMANSRSF1physical
28561026
SRS11_HUMANSRSF11physical
28561026
SRSF4_HUMANSRSF4physical
28561026
SRSF6_HUMANSRSF6physical
28561026
TOE1_HUMANTOE1physical
28561026
TSSC4_HUMANTSSC4physical
28561026
TBG1_HUMANTUBG1physical
28561026
GCP2_HUMANTUBGCP2physical
28561026
GCP3_HUMANTUBGCP3physical
28561026
GCP4_HUMANTUBGCP4physical
28561026
GCP5_HUMANTUBGCP5physical
28561026
GCP6_HUMANTUBGCP6physical
28561026
SR140_HUMANU2SURPphysical
28561026
SNUT2_HUMANUSP39physical
28561026
WBP11_HUMANWBP11physical
28561026
ZNHI2_HUMANZNHIT2physical
28561026

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 CD2B2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194, AND MASSSPECTROMETRY.
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, 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-118, AND MASSSPECTROMETRY.
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment.";
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
J. Proteome Res. 7:5167-5176(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, 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-46, AND MASSSPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, AND MASSSPECTROMETRY.
"Quantitative phosphoproteome profiling of Wnt3a-mediated signalingnetwork: indicating the involvement of ribonucleoside-diphosphatereductase M2 subunit phosphorylation at residue serine 20 in canonicalWnt signal transduction.";
Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
Mol. Cell. Proteomics 6:1952-1967(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, AND MASSSPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-195, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49 AND SER-195, AND MASSSPECTROMETRY.

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