SPI2B_HUMAN - dbPTM
SPI2B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SPI2B_HUMAN
UniProt AC Q9BPZ2
Protein Name Spindlin-2B
Gene Name SPIN2B
Organism Homo sapiens (Human).
Sequence Length 258
Subcellular Localization Nucleus .
Protein Description Involved in the regulation of cell cycle progression, this activity is related to the inhibition of apoptosis following the removal of essential growth factors. [PubMed: 12145692 Exhibits H3K4me3-binding activity]
Protein Sequence MKTPNAQEAEGQQTRAAAGRATGSANMTKKKVSQKKQRGRPSSQPRRNIVGCRISHGWKEGDEPITQWKGTVLDQVPINPSLYLVKYDGIDCVYGLELHRDERVLSLKILSDRVASSHISDANLANTIIGKAVEHMFEGEHGSKDEWRGMVLAQAPIMKAWFYITYEKDPVLYMYQLLDDYKEGDLRIMPESSESPPTEREPGGVVDGLIGKHVEYTKEDGSKRIGMVIHQVEAKPSVYFIKFDDDFHIYVYDLVKKS
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
2Methylation------MKTPNAQEA
------CCCCCHHHH
73.09-
3Phosphorylation-----MKTPNAQEAE
-----CCCCCHHHHC
22.0721815630
3O-linked_Glycosylation-----MKTPNAQEAE
-----CCCCCHHHHC
22.0730620550
14PhosphorylationQEAEGQQTRAAAGRA
HHHCCHHHHHHHHHC
17.8724043423
35AcetylationTKKKVSQKKQRGRPS
CHHHHHHHHHCCCCC
43.2811565435
36AcetylationKKKVSQKKQRGRPSS
HHHHHHHHHCCCCCC
37.2811565443
87PhosphorylationPSLYLVKYDGIDCVY
CCEEEEEECCCCEEE
16.36-
94PhosphorylationYDGIDCVYGLELHRD
ECCCCEEEEEEECCC
23.48-
106PhosphorylationHRDERVLSLKILSDR
CCCCCEEEEEECHHH
25.4324719451
108UbiquitinationDERVLSLKILSDRVA
CCCEEEEEECHHHHH
37.9221890473
116PhosphorylationILSDRVASSHISDAN
ECHHHHHHCCCCHHH
21.4220068231
117PhosphorylationLSDRVASSHISDANL
CHHHHHHCCCCHHHH
18.3320068231
120PhosphorylationRVASSHISDANLANT
HHHHCCCCHHHHHHH
25.8320068231
127PhosphorylationSDANLANTIIGKAVE
CHHHHHHHHHHHHHH
14.3620068231
143PhosphorylationMFEGEHGSKDEWRGM
HHCCCCCCCCHHHCE
38.55-
144UbiquitinationFEGEHGSKDEWRGMV
HCCCCCCCCHHHCEE
65.35-
182UbiquitinationYQLLDDYKEGDLRIM
EEECHHHHCCCEEEC
63.31-
192PhosphorylationDLRIMPESSESPPTE
CEEECCCCCCCCCCC
33.2727732954
193PhosphorylationLRIMPESSESPPTER
EEECCCCCCCCCCCC
40.1924719451
195PhosphorylationIMPESSESPPTEREP
ECCCCCCCCCCCCCC
37.8221815630
198PhosphorylationESSESPPTEREPGGV
CCCCCCCCCCCCCCC
51.5727732954
212UbiquitinationVVDGLIGKHVEYTKE
CCCCCCEEEEEEECC
37.17-

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 SPI2B_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SPI2B_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 SPI2B_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SPIN1_HUMANSPIN1physical
26186194
XPC_HUMANXPCphysical
26186194
WDHD1_HUMANWDHD1physical
26186194
SP16H_HUMANSUPT16Hphysical
26186194
CGBP1_HUMANCGGBP1physical
26186194
PARP2_HUMANPARP2physical
26186194
WDR76_HUMANWDR76physical
26186194
MCM2_HUMANMCM2physical
26186194
XPP1_HUMANXPNPEP1physical
26186194
H2B1J_HUMANHIST1H2BJphysical
26186194
MCM6_HUMANMCM6physical
26186194
SSRP1_HUMANSSRP1physical
26186194
H2A2B_HUMANHIST2H2ABphysical
26186194
YRDC_HUMANYRDCphysical
26186194
MCM4_HUMANMCM4physical
26186194
CK084_HUMANC11orf84physical
26186194
UBR7_HUMANUBR7physical
26186194
DAXX_HUMANDAXXphysical
26186194
RHG39_HUMANARHGAP39physical
26186194
F122B_HUMANFAM122Bphysical
26186194
TOPRS_HUMANTOPORSphysical
26186194
SPIN1_HUMANSPIN1physical
28514442
CK084_HUMANC11orf84physical
28514442
CGBP1_HUMANCGGBP1physical
28514442
RHG39_HUMANARHGAP39physical
28514442
XPP1_HUMANXPNPEP1physical
28514442
UBR7_HUMANUBR7physical
28514442
YRDC_HUMANYRDCphysical
28514442
F122B_HUMANFAM122Bphysical
28514442
PARP2_HUMANPARP2physical
28514442
SP16H_HUMANSUPT16Hphysical
28514442
WDHD1_HUMANWDHD1physical
28514442
DAXX_HUMANDAXXphysical
28514442
TOPRS_HUMANTOPORSphysical
28514442
XPC_HUMANXPCphysical
28514442
MCM2_HUMANMCM2physical
28514442
SSRP1_HUMANSSRP1physical
28514442
MCM6_HUMANMCM6physical
28514442

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 SPI2B_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP