MSPD2_HUMAN - dbPTM
MSPD2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MSPD2_HUMAN
UniProt AC Q8NHP6
Protein Name Motile sperm domain-containing protein 2
Gene Name MOSPD2
Organism Homo sapiens (Human).
Sequence Length 518
Subcellular Localization Cell membrane
Single-pass membrane protein .
Protein Description Promotes migration of primary monocytes and neutrophils, in response to various chemokines..
Protein Sequence MAENHAQNKAKLISETRRRFEAEYVTDKSDKYDARDVERLQQDDNWVESYLSWRHNIVDETLKMLDESFQWRKEISVNDLNESSIPRWLLEIGVIYLHGYDKEGNKLFWIRVKYHVKDQKTILDKKKLIAFWLERYAKRENGKPVTVMFDLSETGINSIDMDFVRFIINCFKVYYPKYLSKIVIFDMPWLMNAAFKIVKTWLGPEAVSLLKFTSKNEVQDYVSVEYLPPHMGGTDPFKYSYPPLVDDDFQTPLCENGPITSEDETSSKEDIESDGKETLETISNEEQTPLLKKINPTESTSKAEENEKVDSKVKAFKKPLSVFKGPLLHISPAEELYFGSTESGEKKTLIVLTNVTKNIVAFKVRTTAPEKYRVKPSNSSCDPGASVDIVVSPHGGLTVSAQDRFLIMAAEMEQSSGTGPAELTQFWKEVPRNKVMEHRLRCHTVESSKPNTLTLKDNAFNMSDKTSEDICLQLSRLLESNRKLEDQVQRCIWFQQLLLSLTMLLLAFVTSFFYLLYS
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
11UbiquitinationNHAQNKAKLISETRR
HHHHHHHHHHHHHHH		48.22-
11AcetylationNHAQNKAKLISETRR
HHHHHHHHHHHHHHH		48.2225953088
14PhosphorylationQNKAKLISETRRRFE
HHHHHHHHHHHHHHH		43.2729083192
16PhosphorylationKAKLISETRRRFEAE
HHHHHHHHHHHHHHE		23.7629083192
24PhosphorylationRRRFEAEYVTDKSDK
HHHHHHEECCCCCCC		18.72-
52PhosphorylationNWVESYLSWRHNIVD
CHHHHHHHHHHHHHH		17.5224719451
62 (in isoform 2)Ubiquitination-2.6321890473
64 (in isoform 2)Ubiquitination-6.8421890473
83PhosphorylationSVNDLNESSIPRWLL
CHHHCCCCCCCHHHH		32.28-
84PhosphorylationVNDLNESSIPRWLLE
HHHCCCCCCCHHHHH		30.36-
125 (in isoform 1)Ubiquitination-48.6521890473
125AcetylationDQKTILDKKKLIAFW
CCCCCCCHHHHHHHH		48.657432035
126AcetylationQKTILDKKKLIAFWL
CCCCCCHHHHHHHHH		53.107432045
127 (in isoform 1)Ubiquitination-51.3621890473
127UbiquitinationKTILDKKKLIAFWLE
CCCCCHHHHHHHHHH		51.3621890473
143AcetylationYAKRENGKPVTVMFD
HHHHHCCCCEEEEEE		48.1526051181
148 (in isoform 2)Ubiquitination-1.2621890473
199UbiquitinationNAAFKIVKTWLGPEA
HHHHHHHHHHHCHHH		37.14-
208PhosphorylationWLGPEAVSLLKFTSK
HHCHHHHHHHCCCCC		34.7224719451
211UbiquitinationPEAVSLLKFTSKNEV
HHHHHHHCCCCCCCC		52.4621890473
211 (in isoform 1)Ubiquitination-52.4621890473
251PhosphorylationLVDDDFQTPLCENGP
CCCCCCCCCCCCCCC		20.4428102081
260PhosphorylationLCENGPITSEDETSS
CCCCCCCCCCCCCCC		29.2422817900
261PhosphorylationCENGPITSEDETSSK
CCCCCCCCCCCCCCH		43.7122817900
265PhosphorylationPITSEDETSSKEDIE
CCCCCCCCCCHHHHH		51.0922817900
266PhosphorylationITSEDETSSKEDIES
CCCCCCCCCHHHHHC		37.0522817900
267PhosphorylationTSEDETSSKEDIESD
CCCCCCCCHHHHHCC		47.7022817900
273PhosphorylationSSKEDIESDGKETLE
CCHHHHHCCCHHHHH		52.5821815630
278PhosphorylationIESDGKETLETISNE
HHCCCHHHHHHHCCH		33.1229396449
281PhosphorylationDGKETLETISNEEQT
CCHHHHHHHCCHHCC		32.5825849741
283PhosphorylationKETLETISNEEQTPL
HHHHHHHCCHHCCHH		45.6829255136
288PhosphorylationTISNEEQTPLLKKIN
HHCCHHCCHHHHHCC		21.1329255136
292UbiquitinationEEQTPLLKKINPTES
HHCCHHHHHCCCCCC		60.33-
293UbiquitinationEQTPLLKKINPTEST
HCCHHHHHCCCCCCC		47.92-
297PhosphorylationLLKKINPTESTSKAE
HHHHCCCCCCCCHHH		37.7723312004
299PhosphorylationKKINPTESTSKAEEN
HHCCCCCCCCHHHHH		40.2226657352
300PhosphorylationKINPTESTSKAEENE
HCCCCCCCCHHHHHH		28.1923312004
301PhosphorylationINPTESTSKAEENEK
CCCCCCCCHHHHHHH		38.8623312004
317MalonylationDSKVKAFKKPLSVFK
HHHHHHHCCCHHHCC		59.3432601280
363MalonylationTKNIVAFKVRTTAPE
CCCEEEEEEECCCCC		22.5226320211
444PhosphorylationEHRLRCHTVESSKPN
HHHHEEEECCCCCCC		29.6022817900
447PhosphorylationLRCHTVESSKPNTLT
HEEEECCCCCCCCEE		39.0529449344
448PhosphorylationRCHTVESSKPNTLTL
EEEECCCCCCCCEEE		38.3323898821
449UbiquitinationCHTVESSKPNTLTLK
EEECCCCCCCCEEEC		52.12-
452PhosphorylationVESSKPNTLTLKDNA
CCCCCCCCEEECCCC		29.6422817900
454PhosphorylationSSKPNTLTLKDNAFN
CCCCCCEEECCCCCC		29.7128555341
483UbiquitinationRLLESNRKLEDQVQR
HHHHHCCCHHHHHHH		61.55-
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 MSPD2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MSPD2_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 MSPD2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of MSPD2_HUMAN !!
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 MSPD2_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-283, 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-261; THR-265; SER-266;SER-267; THR-444 AND THR-452, AND MASS SPECTROMETRY.

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