SOCS6_HUMAN - dbPTM
SOCS6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SOCS6_HUMAN
UniProt AC O14544
Protein Name Suppressor of cytokine signaling 6
Gene Name SOCS6
Organism Homo sapiens (Human).
Sequence Length 535
Subcellular Localization
Protein Description SOCS family proteins form part of a classical negative feedback system that regulates cytokine signal transduction. May be a substrate recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). Regulates KIT degradation by ubiquitination of the tyrosine-phosphorylated receptor..
Protein Sequence MKKISLKTLRKSFNLNKSKEETDFMVVQQPSLASDFGKDDSLFGSCYGKDMASCDINGEDEKGGKNRSKSESLMGTLKRRLSAKQKSKGKAGTPSGSSADEDTFSSSSAPIVFKDVRAQRPIRSTSLRSHHYSPAPWPLRPTNSEETCIKMEVRVKALVHSSSPSPALNGVRKDFHDLQSETTCQEQANSLKSSASHNGDLHLHLDEHVPVVIGLMPQDYIQYTVPLDEGMYPLEGSRSYCLDSSSPMEVSAVPPQVGGRAFPEDESQVDQDLVVAPEIFVDQSVNGLLIGTTGVMLQSPRAGHDDVPPLSPLLPPMQNNQIQRNFSGLTGTEAHVAESMRCHLNFDPNSAPGVARVYDSVQSSGPMVVTSLTEELKKLAKQGWYWGPITRWEAEGKLANVPDGSFLVRDSSDDRYLLSLSFRSHGKTLHTRIEHSNGRFSFYEQPDVEGHTSIVDLIEHSIRDSENGAFCYSRSRLPGSATYPVRLTNPVSRFMQVRSLQYLCRFVIRQYTRIDLIQKLPLPNKMKDYLQEKHY
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
12PhosphorylationSLKTLRKSFNLNKSK
CHHHHHHHHCCCCCH
16.9722210691
18PhosphorylationKSFNLNKSKEETDFM
HHHCCCCCHHHCCEE
44.2027050516
22PhosphorylationLNKSKEETDFMVVQQ
CCCCHHHCCEEEEEC
35.3123090842
68PhosphorylationEKGGKNRSKSESLMG
CCCCCCCCHHHHHHH
50.3423090842
70PhosphorylationGGKNRSKSESLMGTL
CCCCCCHHHHHHHHH
33.3925159151
72PhosphorylationKNRSKSESLMGTLKR
CCCCHHHHHHHHHHH
30.6525159151
76PhosphorylationKSESLMGTLKRRLSA
HHHHHHHHHHHHHCH
18.3629978859
93PhosphorylationKSKGKAGTPSGSSAD
HCCCCCCCCCCCCCC
21.0927050516
97PhosphorylationKAGTPSGSSADEDTF
CCCCCCCCCCCCCCC
27.0424719451
98PhosphorylationAGTPSGSSADEDTFS
CCCCCCCCCCCCCCC
43.1729802988
103PhosphorylationGSSADEDTFSSSSAP
CCCCCCCCCCCCCCC
24.3028348404
105PhosphorylationSADEDTFSSSSAPIV
CCCCCCCCCCCCCEE
31.2527251275
106PhosphorylationADEDTFSSSSAPIVF
CCCCCCCCCCCCEEE
24.9127251275
107PhosphorylationDEDTFSSSSAPIVFK
CCCCCCCCCCCEEEE
29.3527251275
108PhosphorylationEDTFSSSSAPIVFKD
CCCCCCCCCCEEEEE
39.7627251275
114UbiquitinationSSAPIVFKDVRAQRP
CCCCEEEEEHHCCCC
44.4021906983
124PhosphorylationRAQRPIRSTSLRSHH
HCCCCCCCCCCCCCC
24.0627282143
126PhosphorylationQRPIRSTSLRSHHYS
CCCCCCCCCCCCCCC
24.0327282143
132PhosphorylationTSLRSHHYSPAPWPL
CCCCCCCCCCCCCCC
15.7827642862
142PhosphorylationAPWPLRPTNSEETCI
CCCCCCCCCCCCCEE
44.9627282143
144PhosphorylationWPLRPTNSEETCIKM
CCCCCCCCCCCEEEE
39.0127282143
147PhosphorylationRPTNSEETCIKMEVR
CCCCCCCCEEEEEEE
18.5827251275
161PhosphorylationRVKALVHSSSPSPAL
EEEHHCCCCCCCHHH
25.6529514088
162PhosphorylationVKALVHSSSPSPALN
EEHHCCCCCCCHHHC
31.2422496350
163PhosphorylationKALVHSSSPSPALNG
EHHCCCCCCCHHHCC
32.2025849741
165PhosphorylationLVHSSSPSPALNGVR
HCCCCCCCHHHCCHH
25.4225849741
173UbiquitinationPALNGVRKDFHDLQS
HHHCCHHHCHHHHHC
63.44-
180PhosphorylationKDFHDLQSETTCQEQ
HCHHHHHCCCHHHHH
44.1822210691
182PhosphorylationFHDLQSETTCQEQAN
HHHHHCCCHHHHHHH
37.8122210691
183PhosphorylationHDLQSETTCQEQANS
HHHHCCCHHHHHHHH
14.2422210691
190PhosphorylationTCQEQANSLKSSASH
HHHHHHHHHHHHHHC
39.9424245541
220PhosphorylationIGLMPQDYIQYTVPL
EEECCCCEEEEEEEC
5.67-
223PhosphorylationMPQDYIQYTVPLDEG
CCCCEEEEEEECCCC
10.51-
245PhosphorylationRSYCLDSSSPMEVSA
CEEECCCCCCCEEEC
37.8228985074
311PhosphorylationHDDVPPLSPLLPPMQ
CCCCCCCCCCCCHHC
21.1929255136
327PhosphorylationNQIQRNFSGLTGTEA
CCCCHHCCCCCCCHH
36.1228857561
330PhosphorylationQRNFSGLTGTEAHVA
CHHCCCCCCCHHHHH
45.6528348404
332PhosphorylationNFSGLTGTEAHVAES
HCCCCCCCHHHHHHH
25.4328348404
358PhosphorylationAPGVARVYDSVQSSG
CCCCHHHHHHHHCCC
9.2828442448
360PhosphorylationGVARVYDSVQSSGPM
CCHHHHHHHHCCCCE
12.3628442448
405PhosphorylationLANVPDGSFLVRDSS
CCCCCCCCEEEEECC
23.8420873877
416PhosphorylationRDSSDDRYLLSLSFR
EECCCCCEEEEEEEC
20.9924719451
419PhosphorylationSDDRYLLSLSFRSHG
CCCCEEEEEEECCCC
21.2622817900
421PhosphorylationDRYLLSLSFRSHGKT
CCEEEEEEECCCCCE
18.4224719451
443PhosphorylationSNGRFSFYEQPDVEG
CCCCEEEEECCCCCC
16.68-
502PhosphorylationMQVRSLQYLCRFVIR
HHHHHHHHHHHHHHH
17.0522461510
529PhosphorylationLPNKMKDYLQEKHY-
CCHHHHHHHHHHCC-
12.55-
533UbiquitinationMKDYLQEKHY-----
HHHHHHHHCC-----
34.93-

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 SOCS6_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SOCS6_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 SOCS6_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ELOB_HUMANTCEB2physical
12052866
ELOC_HUMANTCEB1physical
12052866
IRS4_HUMANIRS4physical
12052866
P85A_HUMANPIK3R1physical
12052866
P85B_HUMANPIK3R2physical
12052866
TBD_HUMANTUBD1physical
12052866
TBB4B_HUMANTUBB4Bphysical
12052866
TBA1A_HUMANTUBA1Aphysical
12052866
KIT_HUMANKITphysical
21030588
CUL5_HUMANCUL5physical
21030588
ELOC_HUMANTCEB1physical
21030588
ELOB_HUMANTCEB2physical
21030588
UB2D2_HUMANUBE2D2physical
21030588
WDR89_HUMANWDR89physical
21988832
ZMIZ2_HUMANZMIZ2physical
21988832
UBC9_HUMANUBE2Iphysical
21988832
KDM1A_HUMANKDM1Aphysical
23455924
ELOC_HUMANTCEB1physical
26186194
PLEC_HUMANPLECphysical
26186194
CK5P2_HUMANCDK5RAP2physical
26186194
CUL5_HUMANCUL5physical
26186194
FBX11_HUMANFBXO11physical
26186194
P55G_HUMANPIK3R3physical
26186194
DPOLA_HUMANPOLA1physical
26186194
ACACA_HUMANACACAphysical
26186194
ARI2_HUMANARIH2physical
26186194
UBP1_HUMANUSP1physical
26186194
SAV1_HUMANSAV1physical
26186194
K0232_HUMANKIAA0232physical
26186194
FA83H_HUMANFAM83Hphysical
26186194
MADD_HUMANMADDphysical
26186194
LNX1_HUMANLNX1physical
25814554
DAB1_HUMANDAB1physical
24210661
CUL5_HUMANCUL5physical
28514442
ARI2_HUMANARIH2physical
28514442
FBX11_HUMANFBXO11physical
28514442
SAV1_HUMANSAV1physical
28514442
PLEC_HUMANPLECphysical
28514442
ELOC_HUMANTCEB1physical
28514442
K0232_HUMANKIAA0232physical
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 SOCS6_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-419, AND MASSSPECTROMETRY.

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