ITB1_HUMAN - dbPTM
ITB1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ITB1_HUMAN
UniProt AC P05556
Protein Name Integrin beta-1
Gene Name ITGB1
Organism Homo sapiens (Human).
Sequence Length 798
Subcellular Localization Cell membrane
Single-pass type I membrane protein . Cell projection, invadopodium membrane
Single-pass type I membrane protein . Cell projection, ruffle membrane
Single-pass type I membrane protein . Recycling endosome . Melanosome . Cleavage furrow
Protein Description Integrins alpha-1/beta-1, alpha-2/beta-1, alpha-10/beta-1 and alpha-11/beta-1 are receptors for collagen. Integrins alpha-1/beta-1 and alpha-2/beta-2 recognize the proline-hydroxylated sequence G-F-P-G-E-R in collagen. Integrins alpha-2/beta-1, alpha-3/beta-1, alpha-4/beta-1, alpha-5/beta-1, alpha-8/beta-1, alpha-10/beta-1, alpha-11/beta-1 and alpha-V/beta-1 are receptors for fibronectin. Alpha-4/beta-1 recognizes one or more domains within the alternatively spliced CS-1 and CS-5 regions of fibronectin. Integrin alpha-5/beta-1 is a receptor for fibrinogen. Integrin alpha-1/beta-1, alpha-2/beta-1, alpha-6/beta-1 and alpha-7/beta-1 are receptors for lamimin. Integrin alpha-4/beta-1 is a receptor for VCAM1. It recognizes the sequence Q-I-D-S in VCAM1. Integrin alpha-9/beta-1 is a receptor for VCAM1, cytotactin and osteopontin. It recognizes the sequence A-E-I-D-G-I-E-L in cytotactin. Integrin alpha-3/beta-1 is a receptor for epiligrin, thrombospondin and CSPG4. Alpha-3/beta-1 may mediate with LGALS3 the stimulation by CSPG4 of endothelial cells migration. Integrin alpha-V/beta-1 is a receptor for vitronectin. Beta-1 integrins recognize the sequence R-G-D in a wide array of ligands. Isoform 2 interferes with isoform 1 resulting in a dominant negative effect on cell adhesion and migration (in vitro). When associated with alpha-7/beta-1 integrin, regulates cell adhesion and laminin matrix deposition. Involved in promoting endothelial cell motility and angiogenesis. Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process and the formation of mineralized bone nodules. May be involved in up-regulation of the activity of kinases such as PKC via binding to KRT1. Together with KRT1 and RACK1, serves as a platform for SRC activation or inactivation. Plays a mechanistic adhesive role during telophase, required for the successful completion of cytokinesis. Integrin alpha-3/beta-1 provides a docking site for FAP (seprase) at invadopodia plasma membranes in a collagen-dependent manner and hence may participate in the adhesion, formation of invadopodia and matrix degradation processes, promoting cell invasion. ITGA4:ITGB1 binds to fractalkine (CX3CL1) and may act as its coreceptor in CX3CR1-dependent fractalkine signaling. [PubMed: 23125415]
Protein Sequence MNLQPIFWIGLISSVCCVFAQTDENRCLKANAKSCGECIQAGPNCGWCTNSTFLQEGMPTSARCDDLEALKKKGCPPDDIENPRGSKDIKKNKNVTNRSKGTAEKLKPEDITQIQPQQLVLRLRSGEPQTFTLKFKRAEDYPIDLYYLMDLSYSMKDDLENVKSLGTDLMNEMRRITSDFRIGFGSFVEKTVMPYISTTPAKLRNPCTSEQNCTSPFSYKNVLSLTNKGEVFNELVGKQRISGNLDSPEGGFDAIMQVAVCGSLIGWRNVTRLLVFSTDAGFHFAGDGKLGGIVLPNDGQCHLENNMYTMSHYYDYPSIAHLVQKLSENNIQTIFAVTEEFQPVYKELKNLIPKSAVGTLSANSSNVIQLIIDAYNSLSSEVILENGKLSEGVTISYKSYCKNGVNGTGENGRKCSNISIGDEVQFEISITSNKCPKKDSDSFKIRPLGFTEEVEVILQYICECECQSEGIPESPKCHEGNGTFECGACRCNEGRVGRHCECSTDEVNSEDMDAYCRKENSSEICSNNGECVCGQCVCRKRDNTNEIYSGKFCECDNFNCDRSNGLICGGNGVCKCRVCECNPNYTGSACDCSLDTSTCEASNGQICNGRGICECGVCKCTDPKFQGQTCEMCQTCLGVCAEHKECVQCRAFNKGEKKDTCTQECSYFNITKVESRDKLPQPVQPDPVSHCKEKDVDDCWFYFTYSVNGNNEVMVHVVENPECPTGPDIIPIVAGVVAGIVLIGLALLLIWKLLMIIHDRREFAKFEKEKMNAKWDTGENPIYKSAVTTVVNPKYEGK
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
13PhosphorylationIFWIGLISSVCCVFA
HHHHHHHHHHHHHHH		23.0420068231
14PhosphorylationFWIGLISSVCCVFAQ
HHHHHHHHHHHHHHC		16.5120068231
22PhosphorylationVCCVFAQTDENRCLK
HHHHHHCCCCCHHHH		41.6820068231
50N-linked_GlycosylationPNCGWCTNSTFLQEG
CCCCCCCCCHHHHCC		35.6016157583
60PhosphorylationFLQEGMPTSARCDDL
HHHCCCCCCCCCHHH		26.5729083192
61PhosphorylationLQEGMPTSARCDDLE
HHCCCCCCCCCHHHH		14.0829083192
71UbiquitinationCDDLEALKKKGCPPD
CHHHHHHHHCCCCCC		60.5333845483
73UbiquitinationDLEALKKKGCPPDDI
HHHHHHHCCCCCCCC		65.2533845483
87UbiquitinationIENPRGSKDIKKNKN
CCCCCCCCCHHHCCC		67.3124816145
94N-linked_GlycosylationKDIKKNKNVTNRSKG
CCHHHCCCCCCCCCC		56.06UniProtKB CARBOHYD
97N-linked_GlycosylationKKNKNVTNRSKGTAE
HHCCCCCCCCCCCHH		41.7816157583
100UbiquitinationKNVTNRSKGTAEKLK
CCCCCCCCCCHHHCC		57.9829967540
105UbiquitinationRSKGTAEKLKPEDIT
CCCCCHHHCCHHHHC		60.3933845483
107UbiquitinationKGTAEKLKPEDITQI
CCCHHHCCHHHHCCC		58.3833845483
107 (in isoform 1)Ubiquitination-58.3821890473
107 (in isoform 2)Ubiquitination-58.3821906983
107 (in isoform 3)Ubiquitination-58.3821906983
107 (in isoform 4)Ubiquitination-58.3821906983
107 (in isoform 5)Ubiquitination-58.3821906983
125PhosphorylationQLVLRLRSGEPQTFT
EEEEEECCCCCEEEE		52.6921406692
130PhosphorylationLRSGEPQTFTLKFKR
ECCCCCEEEEEEEEE		29.3321406692
132PhosphorylationSGEPQTFTLKFKRAE
CCCCEEEEEEEEECC		32.2121406692
134AcetylationEPQTFTLKFKRAEDY
CCEEEEEEEEECCCC		45.87129259
134UbiquitinationEPQTFTLKFKRAEDY
CCEEEEEEEEECCCC		45.8733845483
136UbiquitinationQTFTLKFKRAEDYPI
EEEEEEEEECCCCCE		49.4633845483
141PhosphorylationKFKRAEDYPIDLYYL
EEEECCCCCEEEEEE		8.1323663014
146PhosphorylationEDYPIDLYYLMDLSY
CCCCEEEEEEEECCC		7.2723663014
147PhosphorylationDYPIDLYYLMDLSYS
CCCEEEEEEEECCCC		11.6623663014
156UbiquitinationMDLSYSMKDDLENVK
EECCCCCHHHHHHHH		41.9933845483
163UbiquitinationKDDLENVKSLGTDLM
HHHHHHHHHHCHHHH		52.0921906983
163 (in isoform 1)Ubiquitination-52.0921890473
163 (in isoform 2)Ubiquitination-52.0921906983
163 (in isoform 3)Ubiquitination-52.0921906983
163 (in isoform 4)Ubiquitination-52.0921906983
163 (in isoform 5)Ubiquitination-52.0921906983
178PhosphorylationNEMRRITSDFRIGFG
HHHHHHHCCCCCCCH		32.1730576142
186PhosphorylationDFRIGFGSFVEKTVM
CCCCCCHHHHCCCCC		24.6929970186
190UbiquitinationGFGSFVEKTVMPYIS
CCHHHHCCCCCCCCC		40.9121963094
190 (in isoform 1)Ubiquitination-40.9121890473
190 (in isoform 2)Ubiquitination-40.9121906983
190 (in isoform 3)Ubiquitination-40.9121906983
190 (in isoform 4)Ubiquitination-40.9121906983
190 (in isoform 5)Ubiquitination-40.9121906983
191PhosphorylationFGSFVEKTVMPYIST
CHHHHCCCCCCCCCC		14.4530206219
195PhosphorylationVEKTVMPYISTTPAK
HCCCCCCCCCCCCHH		6.8730206219
197PhosphorylationKTVMPYISTTPAKLR
CCCCCCCCCCCHHHC		22.0129396449
198PhosphorylationTVMPYISTTPAKLRN
CCCCCCCCCCHHHCC		27.5230206219
199PhosphorylationVMPYISTTPAKLRNP
CCCCCCCCCHHHCCC		17.9225159151
202UbiquitinationYISTTPAKLRNPCTS
CCCCCCHHHCCCCCC		49.5423000965
202 (in isoform 1)Ubiquitination-49.5421890473
202 (in isoform 2)Ubiquitination-49.5421906983
202 (in isoform 3)Ubiquitination-49.5421906983
202 (in isoform 4)Ubiquitination-49.5421906983
202 (in isoform 5)Ubiquitination-49.5421906983
209PhosphorylationKLRNPCTSEQNCTSP
HHCCCCCCCCCCCCC		43.8526657352
212N-linked_GlycosylationNPCTSEQNCTSPFSY
CCCCCCCCCCCCCCH		27.2916157583
214O-linked_GlycosylationCTSEQNCTSPFSYKN
CCCCCCCCCCCCHHC		47.1626853435
220UbiquitinationCTSPFSYKNVLSLTN
CCCCCCHHCHHHHCC		39.1129967540
224PhosphorylationFSYKNVLSLTNKGEV
CCHHCHHHHCCCHHH		28.9420068231
226PhosphorylationYKNVLSLTNKGEVFN
HHCHHHHCCCHHHHH		31.3520068231
2282-HydroxyisobutyrylationNVLSLTNKGEVFNEL
CHHHHCCCHHHHHHH		51.73-
228UbiquitinationNVLSLTNKGEVFNEL
CHHHHCCCHHHHHHH		51.7323000965
228 (in isoform 1)Ubiquitination-51.7321890473
228 (in isoform 2)Ubiquitination-51.7321906983
228 (in isoform 3)Ubiquitination-51.7321906983
228 (in isoform 4)Ubiquitination-51.7321906983
228 (in isoform 5)Ubiquitination-51.7321906983
2382-HydroxyisobutyrylationVFNELVGKQRISGNL
HHHHHHCCCCCCCCC		28.99-
238UbiquitinationVFNELVGKQRISGNL
HHHHHHCCCCCCCCC		28.9921906983
238 (in isoform 1)Ubiquitination-28.9921890473
238 (in isoform 2)Ubiquitination-28.9921906983
238 (in isoform 3)Ubiquitination-28.9921906983
238 (in isoform 4)Ubiquitination-28.9921906983
238 (in isoform 5)Ubiquitination-28.9921906983
263PhosphorylationMQVAVCGSLIGWRNV
HHHHHCHHHHCCCCC		16.2227251275
269N-linked_GlycosylationGSLIGWRNVTRLLVF
HHHHCCCCCEEEEEE		32.7616157583
271PhosphorylationLIGWRNVTRLLVFST
HHCCCCCEEEEEEEC		21.1027251275
289AcetylationFHFAGDGKLGGIVLP
EECCCCCCCCCEECC		49.0124180075
327PhosphorylationAHLVQKLSENNIQTI
HHHHHHHHHCCCEEE		45.3620068231
333PhosphorylationLSENNIQTIFAVTEE
HHHCCCEEEEEECHH		17.7920068231
338O-linked_GlycosylationIQTIFAVTEEFQPVY
CEEEEEECHHHHHHH		26.77OGP
338PhosphorylationIQTIFAVTEEFQPVY
CEEEEEECHHHHHHH		26.7720068231
345PhosphorylationTEEFQPVYKELKNLI
CHHHHHHHHHHHHHC		12.8720068231
346UbiquitinationEEFQPVYKELKNLIP
HHHHHHHHHHHHHCC		57.7233845483
349UbiquitinationQPVYKELKNLIPKSA
HHHHHHHHHHCCHHH		51.2923503661
363N-linked_GlycosylationAVGTLSANSSNVIQL
HCCCCCCCCCCHHHH		42.4616157583
394O-linked_GlycosylationGKLSEGVTISYKSYC
CCCCCCEEEEEECHH		18.3155831673
394PhosphorylationGKLSEGVTISYKSYC
CCCCCCEEEEEECHH		18.3120860994
397PhosphorylationSEGVTISYKSYCKNG
CCCEEEEEECHHCCC		10.4920049867
398UbiquitinationEGVTISYKSYCKNGV
CCEEEEEECHHCCCC		28.3233845483
400PhosphorylationVTISYKSYCKNGVNG
EEEEEECHHCCCCCC		11.8620049867
402UbiquitinationISYKSYCKNGVNGTG
EEEECHHCCCCCCCC		48.8029967540
403N-linked_GlycosylationSYKSYCKNGVNGTGE
EEECHHCCCCCCCCC		56.9619349973
406N-linked_GlycosylationSYCKNGVNGTGENGR
CHHCCCCCCCCCCCC		43.6416157583
411N-linked_GlycosylationGVNGTGENGRKCSNI
CCCCCCCCCCCCCCC		57.8419349973
417N-linked_GlycosylationENGRKCSNISIGDEV
CCCCCCCCCCCCCEE		41.3116157583
4382-HydroxyisobutyrylationTSNKCPKKDSDSFKI
ECCCCCCCCCCCCEE		47.83-
481N-linked_GlycosylationSPKCHEGNGTFECGA
CCCCCCCCCEEECCC		43.2617660510
520N-linked_GlycosylationDAYCRKENSSEICSN
HHHHHHCCCCCCCCC		54.6016157583
540UbiquitinationCGQCVCRKRDNTNEI
ECEEEEEECCCCCCE		60.0029967540
549PhosphorylationDNTNEIYSGKFCECD
CCCCCEECCCCCCCC		40.9621712546
551UbiquitinationTNEIYSGKFCECDNF
CCCEECCCCCCCCCC		40.6833845483
575UbiquitinationCGGNGVCKCRVCECN
CCCCCEEEEEEEECC		23.7523000965
584N-linked_GlycosylationRVCECNPNYTGSACD
EEEECCCCCCCCCCC		32.76UniProtKB CARBOHYD
585PhosphorylationVCECNPNYTGSACDC
EEECCCCCCCCCCCE		17.4628060719
586PhosphorylationCECNPNYTGSACDCS
EECCCCCCCCCCCEE		31.1628060719
588PhosphorylationCNPNYTGSACDCSLD
CCCCCCCCCCCEEEC		20.2328060719
593PhosphorylationTGSACDCSLDTSTCE
CCCCCCEEECCCCCC		18.9428060719
596PhosphorylationACDCSLDTSTCEASN
CCCEEECCCCCCCCC		31.0928060719
597PhosphorylationCDCSLDTSTCEASNG
CCEEECCCCCCCCCC		30.6328060719
598PhosphorylationDCSLDTSTCEASNGQ
CEEECCCCCCCCCCC		19.2328060719
602PhosphorylationDTSTCEASNGQICNG
CCCCCCCCCCCCCCC		21.1428060719
619AcetylationICECGVCKCTDPKFQ
EEECCEEEECCCCCC		37.4526051181
619UbiquitinationICECGVCKCTDPKFQ
EEECCEEEECCCCCC		37.4533845483
6542-HydroxyisobutyrylationVQCRAFNKGEKKDTC
HCCCCCCCCCCCCCC		63.09-
669N-linked_GlycosylationTQECSYFNITKVESR
CCCCCCEEEEEEECC		32.5517660510
672UbiquitinationCSYFNITKVESRDKL
CCCEEEEEEECCCCC		39.9621906983
672 (in isoform 1)Ubiquitination-39.9621890473
672 (in isoform 2)Ubiquitination-39.9621906983
672 (in isoform 3)Ubiquitination-39.9621906983
672 (in isoform 4)Ubiquitination-39.9621906983
672 (in isoform 5)Ubiquitination-39.9621906983
6782-HydroxyisobutyrylationTKVESRDKLPQPVQP
EEEECCCCCCCCCCC		62.04-
678AcetylationTKVESRDKLPQPVQP
EEEECCCCCCCCCCC		62.0426051181
678UbiquitinationTKVESRDKLPQPVQP
EEEECCCCCCCCCCC		62.0433845483
692UbiquitinationPDPVSHCKEKDVDDC
CCCCCCCCCCCCCCC		63.4833845483
7652-HydroxyisobutyrylationHDRREFAKFEKEKMN
HCHHHHHHHHHHHHH		60.42-
765MalonylationHDRREFAKFEKEKMN
HCHHHHHHHHHHHHH		60.4232601280
765UbiquitinationHDRREFAKFEKEKMN
HCHHHHHHHHHHHHH		60.4227667366
768UbiquitinationREFAKFEKEKMNAKW
HHHHHHHHHHHHCCC		66.8123000965
770UbiquitinationFAKFEKEKMNAKWDT
HHHHHHHHHHCCCCC		48.8223000965
7742-HydroxyisobutyrylationEKEKMNAKWDTGENP
HHHHHHCCCCCCCCC		40.37-
774AcetylationEKEKMNAKWDTGENP
HHHHHHCCCCCCCCC		40.3723236377
774UbiquitinationEKEKMNAKWDTGENP
HHHHHHCCCCCCCCC		40.3723000965
774 (in isoform 1)Ubiquitination-40.3721890473
774 (in isoform 5)Ubiquitination-40.37-
777PhosphorylationKMNAKWDTGENPIYK
HHHCCCCCCCCCCCC		45.3319664994
777 (in isoform 5)Phosphorylation-45.3320068231
780 (in isoform 2)Phosphorylation-29.61-
783PhosphorylationDTGENPIYKSAVTTV
CCCCCCCCCCCEEEE		10.5123927012
783 (in isoform 5)Phosphorylation-10.5120068231
7842-HydroxyisobutyrylationTGENPIYKSAVTTVV
CCCCCCCCCCEEEEC		32.43-
784NeddylationTGENPIYKSAVTTVV
CCCCCCCCCCEEEEC		32.4332015554
784UbiquitinationTGENPIYKSAVTTVV
CCCCCCCCCCEEEEC		32.4323000965
784 (in isoform 1)Ubiquitination-32.4321890473
784 (in isoform 5)Ubiquitination-32.43-
785PhosphorylationGENPIYKSAVTTVVN
CCCCCCCCCEEEECC		15.8230266825
788PhosphorylationPIYKSAVTTVVNPKY
CCCCCCEEEECCCCC		17.3721945579
789PhosphorylationIYKSAVTTVVNPKYE
CCCCCEEEECCCCCC		18.8321945579
791 (in isoform 5)Ubiquitination-10.76-
7942-HydroxyisobutyrylationVTTVVNPKYEGK---
EEEECCCCCCCC---		51.21-
794AcetylationVTTVVNPKYEGK---
EEEECCCCCCCC---		51.2119608861
794MalonylationVTTVVNPKYEGK---
EEEECCCCCCCC---		51.2126320211
794SumoylationVTTVVNPKYEGK---
EEEECCCCCCCC---		51.2125114211
794UbiquitinationVTTVVNPKYEGK---
EEEECCCCCCCC---		51.2123000965
794 (in isoform 1)Ubiquitination-51.2121890473
795PhosphorylationTTVVNPKYEGK----
EEECCCCCCCC----		31.0421945579
798UbiquitinationVNPKYEGK-------
CCCCCCCC-------		45.2723000965
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
783YPhosphorylationKinaseABL2P42684
GPS
785SPhosphorylationKinasePRKCAP17252
GPS
785SPhosphorylationKinasePKC-FAMILY-GPS
788TPhosphorylationKinaseCAMK2AQ9UQM7
PSP
788TPhosphorylationKinasePRKCEQ02156
GPS
789TPhosphorylationKinaseCAMK2AQ9UQM7
PSP
789TPhosphorylationKinasePRKCEQ02156
GPS
-KUbiquitinationE3 ubiquitin ligaseFBXO2Q9UK22
PMID:16275327
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ITB1_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 ITB1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ITA3_HUMANITGA3physical
15254262
ITBP1_HUMANITGB1BP1physical
9281591
ILK_HUMANILKphysical
8538749
ITA8_HUMANITGA8physical
7768999
MCP_HUMANCD46physical
10741407
FLNB_HUMANFLNBphysical
11807098
FLNA_HUMANFLNAphysical
11807098
RACK1_HUMANGNB2L1physical
9442085
M4K4_HUMANMAP4K4physical
11967148
ACTN1_HUMANACTN1physical
2116421
TSN4_HUMANTSPAN4physical
9360996
FLNA_HUMANFLNAphysical
9722563
CALX_HUMANCANXphysical
8163531
ITA9_HUMANITGA9physical
8245132
FAK1_CHICKPTK2physical
7657702
PAXI_CHICKPXNphysical
7657702
TLN1_HUMANTLN1physical
11279249
KPCA_HUMANPRKCAphysical
12435334
RACK1_HUMANGNB2L1physical
12435334
NDKA_HUMANNME1physical
11919189
4F2_HUMANSLC3A2physical
12181350
ITA3_HUMANITGA3physical
16878156
ITA5_HUMANITGA5physical
20643357
DAG1_HUMANDAG1physical
18341635
TBA1A_HUMANTUBA1Aphysical
18341635
MMP2_HUMANMMP2physical
22349830
ITA1_HUMANITGA1physical
12883474
ITA5_HUMANITGA5physical
12883474
ITA6_HUMANITGA6physical
12883474
ITA7_HUMANITGA7physical
11278916
TLN1_HUMANTLN1physical
22939629
VINC_HUMANVCLphysical
22939629
ODPB_HUMANPDHBphysical
21988832
TSP1_HUMANTHBS1physical
14963009
EPHA2_HUMANEPHA2physical
23874206
RANB9_HUMANRANBP9physical
14722085
SE1L1_HUMANSEL1Lphysical
24324549
ACAP1_HUMANACAP1physical
16256741
LG3BP_HUMANLGALS3BPphysical
24362527
FHL2_HUMANFHL2physical
10906324
PAXI_HUMANPXNphysical
26992741
FAK1_HUMANPTK2physical
26992741
SHC1_HUMANSHC1physical
19889638
FAK1_HUMANPTK2physical
19889638
ITA5_HUMANITGA5physical
25237190
ANGP2_HUMANANGPT2physical
16424009
ITAV_HUMANITGAVphysical
16424009
ITBP1_HUMANITGB1BP1physical
28049720
PI51C_HUMANPIP5K1Cphysical
12782621
TLN1_HUMANTLN1physical
19843520
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
D06319 Volociximab (USAN)
D10028 Valategrast hydrochloride (USAN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ITB1_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-794, AND MASS SPECTROMETRY.
N-linked Glycosylation
ReferencePubMed
"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.";
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.;
Nat. Biotechnol. 27:378-386(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-403; ASN-406 AND ASN-411,AND MASS SPECTROMETRY.
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-212; ASN-481 AND ASN-669,AND MASS SPECTROMETRY.
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry.";
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.;
J. Proteome Res. 4:2070-2080(2005).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-406, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-777, AND MASSSPECTROMETRY.
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-783 AND TYR-795, ANDMASS SPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-783, AND MASSSPECTROMETRY.

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