IGBP1_HUMAN - dbPTM
IGBP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IGBP1_HUMAN
UniProt AC P78318
Protein Name Immunoglobulin-binding protein 1
Gene Name IGBP1
Organism Homo sapiens (Human).
Sequence Length 339
Subcellular Localization Cytoplasm .
Protein Description Associated to surface IgM-receptor; may be involved in signal transduction. Involved in regulation of the catalytic activity of the phosphatases PP2A, PP4 and PP6 by protecting their partially folded catalytic subunits from degradative polyubiquitination until they associate with regulatory subunits..
Protein Sequence MAAEDELQLPRLPELFETGRQLLDEVEVATEPAGSRIVQEKVFKGLDLLEKAAEMLSQLDLFSRNEDLEEIASTDLKYLLVPAFQGALTMKQVNPSKRLDHLQRAREHFINYLTQCHCYHVAEFELPKTMNNSAENHTANSSMAYPSLVAMASQRQAKIQRYKQKKELEHRLSAMKSAVESGQADDERVREYYLLHLQRWIDISLEEIESIDQEIKILRERDSSREASTSNSSRQERPPVKPFILTRNMAQAKVFGAGYPSLPTMTVSDWYEQHRKYGALPDQGIAKAAPEEFRKAAQQQEEQEEKEEEDDEQTLHRAREWDDWKDTHPRGYGNRQNMG
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
2Acetylation------MAAEDELQL
------CCHHHHCCC
21.4022814378
41AcetylationGSRIVQEKVFKGLDL
CCHHHHHHHHHCHHH
35.5627452117
41UbiquitinationGSRIVQEKVFKGLDL
CCHHHHHHHHHCHHH
35.5623000965
44UbiquitinationIVQEKVFKGLDLLEK
HHHHHHHHCHHHHHH
62.6423000965
55SulfoxidationLLEKAAEMLSQLDLF
HHHHHHHHHHHHCCC
3.6030846556
77UbiquitinationEIASTDLKYLLVPAF
HHHHCCHHHHHHHHH
36.3432015554
91UbiquitinationFQGALTMKQVNPSKR
HCCCCHHHCCCHHHH
45.95-
96PhosphorylationTMKQVNPSKRLDHLQ
HHHCCCHHHHHHHHH
25.7924719451
129PhosphorylationAEFELPKTMNNSAEN
EEECCCCCCCCCCCC
24.1625278378
133PhosphorylationLPKTMNNSAENHTAN
CCCCCCCCCCCCCCC
31.7725278378
138PhosphorylationNNSAENHTANSSMAY
CCCCCCCCCCCCCHH
38.8325278378
141PhosphorylationAENHTANSSMAYPSL
CCCCCCCCCCHHHHH
21.0125278378
142PhosphorylationENHTANSSMAYPSLV
CCCCCCCCCHHHHHH
13.7721945579
145PhosphorylationTANSSMAYPSLVAMA
CCCCCCHHHHHHHHH
5.6821945579
147PhosphorylationNSSMAYPSLVAMASQ
CCCCHHHHHHHHHHH
23.8521945579
153PhosphorylationPSLVAMASQRQAKIQ
HHHHHHHHHHHHHHH
16.8920068231
165UbiquitinationKIQRYKQKKELEHRL
HHHHHHHHHHHHHHH
44.0224816145
173PhosphorylationKELEHRLSAMKSAVE
HHHHHHHHHHHHHHH
26.6929514088
176UbiquitinationEHRLSAMKSAVESGQ
HHHHHHHHHHHHHCC
34.6721906983
177PhosphorylationHRLSAMKSAVESGQA
HHHHHHHHHHHHCCC
25.1822964224
181PhosphorylationAMKSAVESGQADDER
HHHHHHHHCCCCHHH
29.61-
184UbiquitinationSAVESGQADDERVRE
HHHHHCCCCHHHHHH
29.7333845483
195UbiquitinationRVREYYLLHLQRWID
HHHHHHHHHHHHHHC
1.8832015554
224PhosphorylationILRERDSSREASTSN
HHHHHHCCCCCCCCC
38.1330576142
225MethylationLRERDSSREASTSNS
HHHHHCCCCCCCCCC
47.6724379803
225DimethylationLRERDSSREASTSNS
HHHHHCCCCCCCCCC
47.67-
228PhosphorylationRDSSREASTSNSSRQ
HHCCCCCCCCCCCCC
27.8430576142
230PhosphorylationSSREASTSNSSRQER
CCCCCCCCCCCCCCC
32.0230576142
241UbiquitinationRQERPPVKPFILTRN
CCCCCCCCCEEEECC
39.7323000965
241AcetylationRQERPPVKPFILTRN
CCCCCCCCCEEEECC
39.7319608861
246PhosphorylationPVKPFILTRNMAQAK
CCCCEEEECCCHHHH
18.3827251275
253UbiquitinationTRNMAQAKVFGAGYP
ECCCHHHHHHCCCCC
26.4721906983
259PhosphorylationAKVFGAGYPSLPTMT
HHHHCCCCCCCCCCC
6.7927251275
261PhosphorylationVFGAGYPSLPTMTVS
HHCCCCCCCCCCCHH
38.2027251275
264PhosphorylationAGYPSLPTMTVSDWY
CCCCCCCCCCHHHHH
30.6629978859
266PhosphorylationYPSLPTMTVSDWYEQ
CCCCCCCCHHHHHHH
21.2429978859
268PhosphorylationSLPTMTVSDWYEQHR
CCCCCCHHHHHHHHH
17.1729978859
271PhosphorylationTMTVSDWYEQHRKYG
CCCHHHHHHHHHHHC
15.6528796482
276UbiquitinationDWYEQHRKYGALPDQ
HHHHHHHHHCCCCCC
46.0033845483
277PhosphorylationWYEQHRKYGALPDQG
HHHHHHHHCCCCCCH
13.9525394399
287AcetylationLPDQGIAKAAPEEFR
CCCCHHHHHCHHHHH
43.0625953088
287UbiquitinationLPDQGIAKAAPEEFR
CCCCHHHHHCHHHHH
43.0621906983
295UbiquitinationAAPEEFRKAAQQQEE
HCHHHHHHHHHHHHH
54.0922817900
306UbiquitinationQQEEQEEKEEEDDEQ
HHHHHHHHHHHHHHH
70.4524816145
325UbiquitinationAREWDDWKDTHPRGY
HHHHHCCCCCCCCCC
60.8029967540
330MethylationDWKDTHPRGYGNRQN
CCCCCCCCCCCCCCC
43.28115480179

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
-KUbiquitinationE3 ubiquitin ligaseMPGP29372
PMID:22613722

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IGBP1_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 IGBP1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TCPA_HUMANTCP1physical
16085932
TCPB_HUMANCCT2physical
16085932
TCPG_HUMANCCT3physical
16085932
TCPD_HUMANCCT4physical
16085932
TCPE_HUMANCCT5physical
16085932
TCPZ_HUMANCCT6Aphysical
16085932
TCPH_HUMANCCT7physical
16085932
TCPQ_HUMANCCT8physical
16085932
PP4C_HUMANPPP4Cphysical
16085932
PPP6_HUMANPPP6Cphysical
16085932
PP2AA_HUMANPPP2CAphysical
16085932
TRI18_HUMANMID1physical
11806752
TRIM1_HUMANMID2physical
11806752
PPP6_HUMANPPP6Cphysical
9647778
PP2AA_HUMANPPP2CAphysical
9647778
PP4C_HUMANPPP4Cphysical
9647778
TRI18_HUMANMID1physical
20092282
PP2AA_HUMANPPP2CAphysical
20092282
TRI18_HUMANMID1physical
21454489
PP2AA_HUMANPPP2CAphysical
21454489
TRI18_HUMANMID1physical
22194938
UBR5_HUMANUBR5physical
20544796
PABP1_HUMANPABPC1physical
20544796
TRI18_HUMANMID1physical
16434393
TRIM1_HUMANMID2physical
16434393
A4_HUMANAPPphysical
21832049
MCFD2_HUMANMCFD2physical
22939629
LEG3_HUMANLGALS3physical
22939629
VATF_HUMANATP6V1Fphysical
22939629
PABP4_HUMANPABPC4physical
22939629
PCBP1_HUMANPCBP1physical
22939629
PSRC1_HUMANPSRC1physical
22939629
S10AB_HUMANS100A11physical
22939629
PPIA_HUMANPPIAphysical
22939629
RAC1_HUMANRAC1physical
22939629
STAM1_HUMANSTAMphysical
22939629
PPIL3_HUMANPPIL3physical
22939629
POMP_HUMANPOMPphysical
22939629
ML12A_HUMANMYL12Aphysical
22939629
PFD1_HUMANPFDN1physical
22939629
PSF3_HUMANGINS3physical
22939629
RBM12_HUMANRBM12physical
22939629
SUMO2_HUMANSUMO2physical
22939629
PFD6_HUMANPFDN6physical
22939629
PP4R2_HUMANPPP4R2physical
22939629
NUDC_HUMANNUDCphysical
22939629
PAIP2_HUMANPAIP2physical
22939629
PHP14_HUMANPHPT1physical
22939629
PLIN3_HUMANPLIN3physical
22939629
TES_HUMANTESphysical
22939629
UBQL2_HUMANUBQLN2physical
22939629
YAP1_HUMANYAP1physical
22939629
PDCD6_HUMANPDCD6physical
22939629
MED15_HUMANMED15physical
22939629
STIP1_HUMANSTIP1physical
22939629
TYSY_HUMANTYMSphysical
22939629
S10A4_HUMANS100A4physical
22939629
SRSF1_HUMANSRSF1physical
22939629
TAGL2_HUMANTAGLN2physical
22939629
MIF_HUMANMIFphysical
22939629
NEDD8_HUMANNEDD8physical
22939629
NENF_HUMANNENFphysical
22939629
NUBP2_HUMANNUBP2physical
22939629
PDLI1_HUMANPDLIM1physical
22939629
PP14B_HUMANPPP1R14Bphysical
22939629
SNX12_HUMANSNX12physical
22939629
TM1L2_HUMANTOM1L2physical
22939629
RLA1_HUMANRPLP1physical
22939629
LIMD1_HUMANLIMD1physical
22939629
SC24A_HUMANSEC24Aphysical
22939629
IPO7_HUMANIPO7physical
22939629
RD23B_HUMANRAD23Bphysical
22939629
SH3L1_HUMANSH3BGRLphysical
22939629
UBE4B_HUMANUBE4Bphysical
22939629
PAXI_HUMANPXNphysical
22939629
NUDC2_HUMANNUDCD2physical
22939629
MUC16_HUMANMUC16physical
22939629
MEA1_HUMANMEA1physical
22939629
P4R3A_HUMANSMEK1physical
22939629
RN214_HUMANRNF214physical
22939629
RPAP1_HUMANRPAP1physical
22939629
TLE3_HUMANTLE3physical
22939629
PFD2_HUMANPFDN2physical
22939629
PRDX5_HUMANPRDX5physical
22939629
LEG1_HUMANLGALS1physical
22939629
LGUL_HUMANGLO1physical
22939629
NDRG1_HUMANNDRG1physical
22939629
UB2D1_HUMANUBE2D1physical
22939629
UBE2B_HUMANUBE2Bphysical
22939629
UBXN1_HUMANUBXN1physical
22939629
ITSN1_HUMANITSN1physical
22939629
RUXF_HUMANSNRPFphysical
22939629
TKT_HUMANTKTphysical
22939629
STMN2_HUMANSTMN2physical
22939629
MBD3_HUMANMBD3physical
22939629
PALLD_HUMANPALLDphysical
22939629
OTUD5_HUMANOTUD5physical
22939629
PEBP1_HUMANPEBP1physical
22939629
THADA_HUMANTHADAphysical
22939629
PDIA6_HUMANPDIA6physical
22939629
VPS4B_HUMANVPS4Bphysical
22939629
SNX3_HUMANSNX3physical
22939629
S100P_HUMANS100Pphysical
22939629
SP100_HUMANSP100physical
22939629
STAT6_HUMANSTAT6physical
22939629
USP9X_HUMANUSP9Xphysical
22939629
SRXN1_HUMANSRXN1physical
22939629
SLD5_HUMANGINS4physical
22939629
ANCHR_HUMANZFYVE19physical
22939629
SIN3A_HUMANSIN3Aphysical
22939629
UNK_HUMANUNKphysical
22939629
KCRU_HUMANCKMT1Bphysical
22939629
REXO5_HUMANLOC81691physical
21988832
PP2AA_HUMANPPP2CAphysical
21988832
S10AD_HUMANS100A13physical
21988832
TRI18_HUMANMID1physical
24484909
PP2AA_HUMANPPP2CAphysical
24484909
TRI18_HUMANMID1physical
11685209
PP2AA_HUMANPPP2CAphysical
23892082
TIPRL_HUMANTIPRLphysical
23892082
1433S_HUMANSFNphysical
26344197
TIPRL_HUMANTIPRLphysical
26344197
KCC2G_HUMANCAMK2Gphysical
26496610
TCPZ_HUMANCCT6Aphysical
26496610
OST48_HUMANDDOSTphysical
26496610
TRI18_HUMANMID1physical
26496610
PP2AA_HUMANPPP2CAphysical
26496610
PP2AB_HUMANPPP2CBphysical
26496610
PP4C_HUMANPPP4Cphysical
26496610
PPP6_HUMANPPP6Cphysical
26496610
RAD51_HUMANRAD51physical
26496610
SPSY_HUMANSMSphysical
26496610
TCPA_HUMANTCP1physical
26496610
TCPG_HUMANCCT3physical
26496610
NUMB_HUMANNUMBphysical
26496610
TCPH_HUMANCCT7physical
26496610
TCPD_HUMANCCT4physical
26496610
TCPB_HUMANCCT2physical
26496610
TCPQ_HUMANCCT8physical
26496610
TCPE_HUMANCCT5physical
26496610
NHEJ1_HUMANNHEJ1physical
26496610
PNCB_HUMANNAPRTphysical
26496610
NOP9_HUMANNOP9physical
26496610

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
300472Mental retardation, X-linked, syndromic, 28 (MRXS28)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of IGBP1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
"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-241, AND MASS SPECTROMETRY.

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