SEM7A_HUMAN - dbPTM
SEM7A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SEM7A_HUMAN
UniProt AC O75326
Protein Name Semaphorin-7A
Gene Name SEMA7A
Organism Homo sapiens (Human).
Sequence Length 666
Subcellular Localization Cell membrane
Lipid-anchor, GPI-anchor
Extracellular side . Detected in a punctate pattern on the cell membrane of basal and supra-basal skin keratinocytes.
Protein Description Plays an important role in integrin-mediated signaling and functions both in regulating cell migration and immune responses. Promotes formation of focal adhesion complexes, activation of the protein kinase PTK2/FAK1 and subsequent phosphorylation of MAPK1 and MAPK3. Promotes production of proinflammatory cytokines by monocytes and macrophages. Plays an important role in modulating inflammation and T-cell-mediated immune responses. Promotes axon growth in the embryonic olfactory bulb. Promotes attachment, spreading and dendrite outgrowth in melanocytes..
Protein Sequence MTPPPPGRAAPSAPRARVPGPPARLGLPLRLRLLLLLWAAAASAQGHLRSGPRIFAVWKGHVGQDRVDFGQTEPHTVLFHEPGSSSVWVGGRGKVYLFDFPEGKNASVRTVNIGSTKGSCLDKRDCENYITLLERRSEGLLACGTNARHPSCWNLVNGTVVPLGEMRGYAPFSPDENSLVLFEGDEVYSTIRKQEYNGKIPRFRRIRGESELYTSDTVMQNPQFIKATIVHQDQAYDDKIYYFFREDNPDKNPEAPLNVSRVAQLCRGDQGGESSLSVSKWNTFLKAMLVCSDAATNKNFNRLQDVFLLPDPSGQWRDTRVYGVFSNPWNYSAVCVYSLGDIDKVFRTSSLKGYHSSLPNPRPGKCLPDQQPIPTETFQVADRHPEVAQRVEPMGPLKTPLFHSKYHYQKVAVHRMQASHGETFHVLYLTTDRGTIHKVVEPGEQEHSFAFNIMEIQPFRRAAAIQTMSLDAERRKLYVSSQWEVSQVPLDLCEVYGGGCHGCLMSRDPYCGWDQGRCISIYSSERSVLQSINPAEPHKECPNPKPDKAPLQKVSLAPNSRYYLSCPMESRHATYSWRHKENVEQSCEPGHQSPNCILFIENLTAQQYGHYFCEAQEGSYFREAQHWQLLPEDGIMAEHLLGHACALAASLWLGVLPTLTLGLLVH
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
105N-linked_GlycosylationFDFPEGKNASVRTVN
EECCCCCCCEEEEEE
48.5920727575
135Asymmetric dimethylarginineNYITLLERRSEGLLA
HHHHHHHHHCCCCEE
47.60-
135MethylationNYITLLERRSEGLLA
HHHHHHHHHCCCCEE
47.60-
157N-linked_GlycosylationPSCWNLVNGTVVPLG
CHHHHCCCCEEEECC
43.5120727575
258N-linked_GlycosylationKNPEAPLNVSRVAQL
CCCCCCCCHHHHHHH
28.7620727575
258N-linked_GlycosylationKNPEAPLNVSRVAQL
CCCCCCCCHHHHHHH
28.7620727575
275PhosphorylationGDQGGESSLSVSKWN
CCCCCCCCCCHHHHH
21.99-
277PhosphorylationQGGESSLSVSKWNTF
CCCCCCCCHHHHHHH
26.7124719451
292PhosphorylationLKAMLVCSDAATNKN
HHHHHHCCHHHCCCC
23.86-
296PhosphorylationLVCSDAATNKNFNRL
HHCCHHHCCCCCCCC
48.74-
313PhosphorylationVFLLPDPSGQWRDTR
EEEEECCCCCCCCEE
51.50-
330N-linked_GlycosylationGVFSNPWNYSAVCVY
EEECCCCCEEEEEEE
23.3420727575
375O-linked_GlycosylationPDQQPIPTETFQVAD
CCCCCCCCCCEEHHH
48.67OGP
602N-linked_GlycosylationNCILFIENLTAQQYG
CEEEEEECCCHHHHC
37.5610201933
648GPI-anchorLGHACALAASLWLGV
HHHHHHHHHHHHHCH
4.05-

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 SEM7A_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SEM7A_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 SEM7A_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SOAT1_HUMANSOAT1physical
28514442
D19L1_HUMANDPY19L1physical
28514442
UN93B_HUMANUNC93B1physical
28514442
TAPT1_HUMANTAPT1physical
28514442
TM214_HUMANTMEM214physical
28514442
CKAP4_HUMANCKAP4physical
28514442
TM39B_HUMANTMEM39Bphysical
28514442
SL9A1_HUMANSLC9A1physical
28514442
S12A9_HUMANSLC12A9physical
28514442
AT11C_HUMANATP11Cphysical
28514442
LMF2_HUMANLMF2physical
28514442
SGPL1_HUMANSGPL1physical
28514442
CLCC1_HUMANCLCC1physical
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 SEM7A_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Structural basis of semaphorin-plexin recognition and viral mimicryfrom Sema7A and A39R complexes with PlexinC1.";
Liu H., Juo Z.S., Shim A.H., Focia P.J., Chen X., Garcia K.C., He X.;
Cell 142:749-761(2010).
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 45-634 IN COMPLEX WITHPLXNC1, SUBUNIT, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-105;ASN-157; ASN-258 AND ASN-330.

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