PDLI7_MOUSE - dbPTM
PDLI7_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PDLI7_MOUSE
UniProt AC Q3TJD7
Protein Name PDZ and LIM domain protein 7
Gene Name Pdlim7
Organism Mus musculus (Mouse).
Sequence Length 457
Subcellular Localization Cytoplasm. Cytoplasm, cytoskeleton. Colocalizes with RET to the cell periphery and in some cytoskeletal components. Colocalizes with TPM2 near the Z line in muscle. Colocalizes with TBX4 and TBX5 to actin filaments (By similarity)..
Protein Description May function as a scaffold on which the coordinated assembly of proteins can occur. May play a role as an adapter that, via its PDZ domain, localizes LIM-binding proteins to actin filaments of both skeletal muscle and nonmuscle tissues. Involved in both of the two fundamental mechanisms of bone formation, direct bone formation (e.g. embryonic flat bones mandible and cranium), and endochondral bone formation (e.g. embryonic long bone development). Plays a role during fracture repair. Involved in BMP6 signaling pathway (By similarity)..
Protein Sequence MDSFKVVLEGPAPWGFRLQGGKDFNVPLSISRLTPGGKAAQAGVAVGDWVLNIDGENAGSLTHIEAQNKIRACGERLSLGLSRAQPVQSKPQKALTPPADPPRYTFAPSASLNKTARPFGAPPPTDSTLRQNGQLLRQPVPDASKQRLMEDTEDWRPRPGTGQSRSFRILAHLTGTEFMQDPDEEFMKKSSQVPRTEAPAPASTIPQESWPGPTTPSPTSRPPWAVDPAFAERYAPDKTSTVLTRHSQPATPTPLQNRTSIVQAAAGGGTGGGSNNGKTPVCHQCHKIIRGRYLVALGHAYHPEEFVCSQCGKVLEEGGFFEEKGAIFCPSCYDVRYAPNCAKCKKKITGEIMHALKMTWHVHCFTCAACKTPIRNRAFYMEEGAPYCERDYEKMFGTKCRGCDFKIDAGDRFLEALGFSWHDTCFVCAICQINLEGKTFYSKKDKPLCKSHAFSHV
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
22UbiquitinationGFRLQGGKDFNVPLS
CEEECCCCCCCCCEE
67.00-
78PhosphorylationRACGERLSLGLSRAQ
HHHHHHHHHCCCCCC
26.9826824392
96PhosphorylationSKPQKALTPPADPPR
CCCCCCCCCCCCCCC
31.8926824392
99 (in isoform 2)Ubiquitination-43.05-
103MethylationTPPADPPRYTFAPSA
CCCCCCCCCCCCCCC
48.8180702637
103Asymmetric dimethylarginineTPPADPPRYTFAPSA
CCCCCCCCCCCCCCC
48.81-
104PhosphorylationPPADPPRYTFAPSAS
CCCCCCCCCCCCCCC
16.3923984901
105PhosphorylationPADPPRYTFAPSASL
CCCCCCCCCCCCCCC
18.0129514104
109PhosphorylationPRYTFAPSASLNKTA
CCCCCCCCCCCCCCC
27.3626824392
111PhosphorylationYTFAPSASLNKTARP
CCCCCCCCCCCCCCC
36.4926824392
161PhosphorylationDWRPRPGTGQSRSFR
CCCCCCCCCCCCEEE
34.4326824392
166 (in isoform 2)Phosphorylation-24.9128542873
180 (in isoform 2)Phosphorylation-65.4922210690
188 (in isoform 2)Phosphorylation-55.6222210690
209PhosphorylationASTIPQESWPGPTTP
CCCCCCCCCCCCCCC
33.0726643407
214PhosphorylationQESWPGPTTPSPTSR
CCCCCCCCCCCCCCC
58.2021659605
215PhosphorylationESWPGPTTPSPTSRP
CCCCCCCCCCCCCCC
25.5426824392
217PhosphorylationWPGPTTPSPTSRPPW
CCCCCCCCCCCCCCC
38.4226824392
219PhosphorylationGPTTPSPTSRPPWAV
CCCCCCCCCCCCCCC
41.5326643407
220PhosphorylationPTTPSPTSRPPWAVD
CCCCCCCCCCCCCCC
46.2926643407
234PhosphorylationDPAFAERYAPDKTST
CHHHHHHHCCCCCCC
17.6226160508
238AcetylationAERYAPDKTSTVLTR
HHHHCCCCCCCEEEE
43.2323806337
239PhosphorylationERYAPDKTSTVLTRH
HHHCCCCCCCEEEEC
36.6926160508
240PhosphorylationRYAPDKTSTVLTRHS
HHCCCCCCCEEEECC
23.4324719451
241PhosphorylationYAPDKTSTVLTRHSQ
HCCCCCCCEEEECCC
25.4326160508
244PhosphorylationDKTSTVLTRHSQPAT
CCCCCEEEECCCCCC
23.2326160508
247PhosphorylationSTVLTRHSQPATPTP
CCEEEECCCCCCCCC
34.2726824392
251PhosphorylationTRHSQPATPTPLQNR
EECCCCCCCCCCCCC
34.0927087446
253PhosphorylationHSQPATPTPLQNRTS
CCCCCCCCCCCCCCC
32.0725619855
259PhosphorylationPTPLQNRTSIVQAAA
CCCCCCCCCEEEECC
30.2928285833
260PhosphorylationTPLQNRTSIVQAAAG
CCCCCCCCEEEECCC
19.9522817900
270PhosphorylationQAAAGGGTGGGSNNG
EECCCCCCCCCCCCC
35.6128973931
372PhosphorylationFTCAACKTPIRNRAF
HHHHHCCCCCCCCEE
24.67-
451PhosphorylationKDKPLCKSHAFSHV-
CCCCCCHHCCCCCC-
21.0323375375
455PhosphorylationLCKSHAFSHV-----
CCHHCCCCCC-----
24.9123375375

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 PDLI7_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PDLI7_MOUSE !!

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 PDLI7_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SH2B2_MOUSESh2b2physical
15946664

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PDLI7_MOUSE

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Related Literatures of Post-Translational Modification

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