SH21A_HUMAN - dbPTM
SH21A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SH21A_HUMAN
UniProt AC O60880
Protein Name SH2 domain-containing protein 1A
Gene Name SH2D1A
Organism Homo sapiens (Human).
Sequence Length 128
Subcellular Localization Cytoplasm .
Protein Description Cytoplasmic adapter regulating receptors of the signaling lymphocytic activation molecule (SLAM) family such as SLAMF1, CD244, LY9, CD84, SLAMF6 and SLAMF7. In SLAM signaling seems to cooperate with SH2D1B/EAT-2. Initially it has been proposed that association with SLAMF1 prevents SLAMF1 binding to inhibitory effectors including INPP5D/SHIP1 and PTPN11/SHP-2. [PubMed: 11806999 However, by simultaneous interactions, recruits FYN which subsequently phosphorylates and activates SLAMF1]
Protein Sequence MDAVAVYHGKISRETGEKLLLATGLDGSYLLRDSESVPGVYCLCVLYHGYIYTYRVSQTETGSWSAETAPGVHKRYFRKIKNLISAFQKPDQGIVIPLQYPVEKKSSARSTQGTTGIREDPDVCLKAP
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-MDAVAVYHGKISRE
-CCEEEEECCEECHH
8.6324719451
10UbiquitinationAVAVYHGKISRETGE
EEEEECCEECHHHCC
24.9724816145
12PhosphorylationAVYHGKISRETGEKL
EEECCEECHHHCCEE
27.7824719451
15PhosphorylationHGKISRETGEKLLLA
CCEECHHHCCEEEEE
49.9123879269
18UbiquitinationISRETGEKLLLATGL
ECHHHCCEEEEEECC
45.86-
23PhosphorylationGEKLLLATGLDGSYL
CCEEEEEECCCCCEE
37.9424719451
28PhosphorylationLATGLDGSYLLRDSE
EEECCCCCEECCCCC
16.5724719451
29PhosphorylationATGLDGSYLLRDSES
EECCCCCEECCCCCC
18.4524719451
74UbiquitinationETAPGVHKRYFRKIK
CCCCCHHHHHHHHHH
46.52-
81UbiquitinationKRYFRKIKNLISAFQ
HHHHHHHHHHHHHHC
49.0529967540
89AcetylationNLISAFQKPDQGIVI
HHHHHHCCCCCCEEE
44.0719608861
89UbiquitinationNLISAFQKPDQGIVI
HHHHHHCCCCCCEEE
44.0719608861
104UbiquitinationPLQYPVEKKSSARST
EECCEECCCCCCCCC
59.18-
105UbiquitinationLQYPVEKKSSARSTQ
ECCEECCCCCCCCCC
35.82-
106PhosphorylationQYPVEKKSSARSTQG
CCEECCCCCCCCCCC
40.0522817900
107PhosphorylationYPVEKKSSARSTQGT
CEECCCCCCCCCCCC
36.2622817900
110PhosphorylationEKKSSARSTQGTTGI
CCCCCCCCCCCCCCC
25.4627251275
111PhosphorylationKKSSARSTQGTTGIR
CCCCCCCCCCCCCCC
26.01-
114PhosphorylationSARSTQGTTGIREDP
CCCCCCCCCCCCCCC
16.42-
115PhosphorylationARSTQGTTGIREDPD
CCCCCCCCCCCCCCC
37.12-
126UbiquitinationEDPDVCLKAP-----
CCCCCCEECC-----
54.1824816145

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 SH21A_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SH21A_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 SH21A_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SLAF1_HUMANSLAMF1physical
11806999
SLAF5_HUMANCD84physical
12928397
FYN_HUMANFYNphysical
12458214
SLAF5_HUMANCD84physical
11389028
LY9_HUMANLY9physical
11389028
DOK1_HUMANDOK1physical
10852966
SLAF1_HUMANSLAMF1physical
11477068
CD244_HUMANCD244physical
11477068
LY9_HUMANLY9physical
11477068
SLAF5_HUMANCD84physical
11477068
EGFR_HUMANEGFRphysical
16273093
ERBB3_HUMANERBB3physical
16273093
ACK1_HUMANTNK2physical
25416956
LHX4_HUMANLHX4physical
25416956
FAK1_HUMANPTK2physical
25814554
ZNHI1_HUMANZNHIT1physical
25814554
ATF3_HUMANATF3physical
25814554
CC74A_HUMANCCDC74Aphysical
25814554
LTMD1_HUMANLETMD1physical
25814554
NGEF_HUMANNGEFphysical
25814554
OLIG1_HUMANOLIG1physical
25814554
TERA_HUMANVCPphysical
19570996

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
308240Lymphoproliferative syndrome, X-linked, 1 (XLP1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SH21A_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-89, AND MASS SPECTROMETRY.

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