dbPTM

ITB2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ITB2_HUMAN
UniProt AC	P05107
Protein Name	Integrin beta-2
Gene Name	ITGB2
Organism	Homo sapiens (Human).
Sequence Length	769
Subcellular Localization	Cell membrane Single-pass type I membrane protein . Membrane raft Single-pass type I membrane protein .
Protein Description	Integrin ITGAL/ITGB2 is a receptor for ICAM1, ICAM2, ICAM3 and ICAM4. Integrins ITGAM/ITGB2 and ITGAX/ITGB2 are receptors for the iC3b fragment of the third complement component and for fibrinogen. Integrin ITGAX/ITGB2 recognizes the sequence G-P-R in fibrinogen alpha-chain. Integrin ITGAM/ITGB2 recognizes P1 and P2 peptides of fibrinogen gamma chain. Integrin ITGAM/ITGB2 is also a receptor for factor X. Integrin ITGAD/ITGB2 is a receptor for ICAM3 and VCAM1. Contributes to natural killer cell cytotoxicity. [PubMed: 15356110 Involved in leukocyte adhesion and transmigration of leukocytes including T-cells and neutrophils]
Protein Sequence	MLGLRPPLLALVGLLSLGCVLSQECTKFKVSSCRECIESGPGCTWCQKLNFTGPGDPDSIRCDTRPQLLMRGCAADDIMDPTSLAETQEDHNGGQKQLSPQKVTLYLRPGQAAAFNVTFRRAKGYPIDLYYLMDLSYSMLDDLRNVKKLGGDLLRALNEITESGRIGFGSFVDKTVLPFVNTHPDKLRNPCPNKEKECQPPFAFRHVLKLTNNSNQFQTEVGKQLISGNLDAPEGGLDAMMQVAACPEEIGWRNVTRLLVFATDDGFHFAGDGKLGAILTPNDGRCHLEDNLYKRSNEFDYPSVGQLAHKLAENNIQPIFAVTSRMVKTYEKLTEIIPKSAVGELSEDSSNVVQLIKNAYNKLSSRVFLDHNALPDTLKVTYDSFCSNGVTHRNQPRGDCDGVQINVPITFQVKVTATECIQEQSFVIRALGFTDIVTVQVLPQCECRCRDQSRDRSLCHGKGFLECGICRCDTGYIGKNCECQTQGRSSQELEGSCRKDNNSIICSGLGDCVCGQCLCHTSDVPGKLIYGQYCECDTINCERYNGQVCGGPGRGLCFCGKCRCHPGFEGSACQCERTTEGCLNPRRVECSGRGRCRCNVCECHSGYQLPLCQECPGCPSPCGKYISCAECLKFEKGPFGKNCSAACPGLQLSNNPVKGRTCKERDSEGCWVAYTLEQQDGMDRYLIYVDESRECVAGPNIAAIVGGTVAGIVLIGILLLVIWKALIHLSDLREYRRFEKEKLKSQWNNDNPLFKSATTTVMNPKFAES

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
23	Pyrrolidone_carboxylic_acid	SLGCVLSQECTKFKV HHHHHHCHHHHCCCC	45.69	-
23	Pyrrolidone_carboxylic_acid	SLGCVLSQECTKFKV HHHHHHCHHHHCCCC	45.69	2954816
23	Pyrrolidone_carboxylic_acid	SLGCVLSQECTKFKV HHHHHHCHHHHCCCC	45.69	2954816
29	Ubiquitination	SQECTKFKVSSCREC CHHHHCCCCCCHHHH	42.64	-
50	N-linked_Glycosylation	CTWCQKLNFTGPGDP CEEECCCCCCCCCCH	39.20	17623646
50	N-linked_Glycosylation	CTWCQKLNFTGPGDP CEEECCCCCCCCCCH	39.20	19349973
96	Ubiquitination	EDHNGGQKQLSPQKV CCCCCCCCCCCCCEE	57.38	-
116	N-linked_Glycosylation	PGQAAAFNVTFRRAK CCCCEEEEEEEEECC	27.48	20033057
118	Phosphorylation	QAAAFNVTFRRAKGY CCEEEEEEEEECCCC	16.72	24719451
148	Ubiquitination	DDLRNVKKLGGDLLR HHHHHHHHHCHHHHH	48.35	-
174	Ubiquitination	GFGSFVDKTVLPFVN CCCCCCCCCCCCCCC	34.92	-
186	Ubiquitination	FVNTHPDKLRNPCPN CCCCCHHHCCCCCCC	54.52	-
194	Ubiquitination	LRNPCPNKEKECQPP CCCCCCCCCCCCCCC	56.13	-
196	Ubiquitination	NPCPNKEKECQPPFA CCCCCCCCCCCCCCH	66.45	-
212	N-linked_Glycosylation	RHVLKLTNNSNQFQT HHHHHHCCCCCCCHH	61.44	19159218
212	N-linked_Glycosylation	RHVLKLTNNSNQFQT HHHHHHCCCCCCCHH	61.44	16335952
213	N-linked_Glycosylation	HVLKLTNNSNQFQTE HHHHHCCCCCCCHHH	36.78	19349973
215	N-linked_Glycosylation	LKLTNNSNQFQTEVG HHHCCCCCCCHHHHH	49.13	19349973
254	N-linked_Glycosylation	PEEIGWRNVTRLLVF HHHHCCCCEEEEEEE	32.76	UniProtKB CARBOHYD
294	Ubiquitination	HLEDNLYKRSNEFDY CCCCCCCCCCCCCCC	53.14	-
328	Ubiquitination	AVTSRMVKTYEKLTE HHHHHHHHHHHHHHH	35.73	-
332	Ubiquitination	RMVKTYEKLTEIIPK HHHHHHHHHHHHCCH	50.74	-
362	Ubiquitination	LIKNAYNKLSSRVFL HHHHHHHHHHCCEEC	36.75	-
379	Ubiquitination	NALPDTLKVTYDSFC CCCCCCEEEEHHHHH	34.32	-
462	Ubiquitination	DRSLCHGKGFLECGI CCCCCCCCCCEECCE	23.87	-
479	Ubiquitination	CDTGYIGKNCECQTQ ECCCCCCCCCEEECC	49.19	-
489	Phosphorylation	ECQTQGRSSQELEGS EEECCCCCCHHHCCC	43.10	28450419
490	Phosphorylation	CQTQGRSSQELEGSC EECCCCCCHHHCCCC	26.72	22210691
496	Phosphorylation	SSQELEGSCRKDNNS CCHHHCCCCCCCCCC	11.02	22210691
501	N-linked_Glycosylation	EGSCRKDNNSIICSG CCCCCCCCCCEECCC	47.38	UniProtKB CARBOHYD
561	Ubiquitination	RGLCFCGKCRCHPGF CCEEECCCCCCCCCC	21.49	-
591	Phosphorylation	NPRRVECSGRGRCRC CCCCEEECCCCCEEC	20.30	-
633	Ubiquitination	ISCAECLKFEKGPFG ECHHHHHCCCCCCCC	64.24	-
636	Ubiquitination	AECLKFEKGPFGKNC HHHHCCCCCCCCCCC	75.03	-
641	Ubiquitination	FEKGPFGKNCSAACP CCCCCCCCCCCCCCC	55.98	-
642	N-linked_Glycosylation	EKGPFGKNCSAACPG CCCCCCCCCCCCCCC	25.92	17623646
642	N-linked_Glycosylation	EKGPFGKNCSAACPG CCCCCCCCCCCCCCC	25.92	17623646
658	Ubiquitination	QLSNNPVKGRTCKER EECCCCCCCCCCCCC	43.88	-
730	Phosphorylation	WKALIHLSDLREYRR HHHHHHHHHHHHHHH	22.04	24719451
735	Phosphorylation	HLSDLREYRRFEKEK HHHHHHHHHHHHHHH	10.72	-
740	Acetylation	REYRRFEKEKLKSQW HHHHHHHHHHHHHHH	58.39	19666903
744	Ubiquitination	RFEKEKLKSQWNNDN HHHHHHHHHHHCCCC	52.23	21890473
745	Phosphorylation	FEKEKLKSQWNNDNP HHHHHHHHHHCCCCC	51.36	28857561
755	Ubiquitination	NNDNPLFKSATTTVM CCCCCCHHHHHEEEC	47.03	-
756	Phosphorylation	NDNPLFKSATTTVMN CCCCCHHHHHEEECC	24.42	23911959
758	Phosphorylation	NPLFKSATTTVMNPK CCCHHHHHEEECCHH	30.05	16301335
759	Phosphorylation	PLFKSATTTVMNPKF CCHHHHHEEECCHHH	19.67	26074081
760	Phosphorylation	LFKSATTTVMNPKFA CHHHHHEEECCHHHC	17.25	1968911
765	Ubiquitination	TTTVMNPKFAES--- HEEECCHHHCCC---	52.80	-

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
735	Y	Phosphorylation	Kinase	LCK	P06239	PSP
745	S	Phosphorylation	Kinase	PKC_GROUP	-	PhosphoELM
745	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
745	S	Phosphorylation	Kinase	PKC	-	Uniprot
745	S	Phosphorylation	Kinase	PRKCB	P05771	GPS
745	S	Phosphorylation	Kinase	PKCB ISO2	P05771-2	PSP
745	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
745	S	Phosphorylation	Kinase	PRKCD	Q05655	GPS
745	S	Phosphorylation	Kinase	PRKCH	P24723	GPS
756	S	Phosphorylation	Kinase	PKC_GROUP	-	PhosphoELM
756	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
758	T	Phosphorylation	Kinase	PRKCH	P24723	GPS
758	T	Phosphorylation	Kinase	PRKCD	Q05655	GPS
758	T	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
758	T	Phosphorylation	Kinase	PKCB ISO2	P05771-2	PSP
758	T	Phosphorylation	Kinase	PRKCB	P05771	GPS
758	T	Phosphorylation	Kinase	PKC	-	Uniprot
758	T	Phosphorylation	Kinase	PRKCA	P17252	GPS
758	T	Phosphorylation	Kinase	PKC_GROUP	-	PhosphoELM
760	T	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
760	T	Phosphorylation	Kinase	PKC_GROUP	-	PhosphoELM
760	T	Phosphorylation	Kinase	PKCA	P17252	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
745	S	Phosphorylation	11700305
Both Ser-745 and Ser-756 become phosphorylated when T-cells are exposed to phorbol esters.
756	S	Phosphorylation	11700305
Both Ser-745 and Ser-756 become phosphorylated when T-cells are exposed to phorbol esters.
756	S	Phosphorylation	11700305
Phosphorylation on Thr-758 (but not on Ser-756) allows interaction with 14-3-3 proteins.
758	T	Phosphorylation	11700305
Phosphorylation on Thr-758 (but not on Ser-756) allows interaction with 14-3-3 proteins.

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 ITB2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RACK1_HUMAN	GNB2L1	physical	9442085
UPAR_HUMAN	PLAUR	physical	10388537
ICAM1_HUMAN	ICAM1	physical	10352278
ITAL_HUMAN	ITGAL	physical	9442085
CYH1_HUMAN	CYTH1	physical	9765275
CYH1_HUMAN	CYTH1	physical	10835351
VNN2_HUMAN	VNN2	physical	12056825
1433B_HUMAN	YWHAB	physical	18239087
CSN5_HUMAN	COPS5	physical	10766246
1433Z_HUMAN	YWHAZ	physical	11700305
1433B_HUMAN	YWHAB	physical	11700305
RANB9_HUMAN	RANBP9	physical	14722085
NT2NL_HUMAN	NOTCH2NL	physical	25416956
SHRPN_HUMAN	SHARPIN	physical	26600301
FHL2_HUMAN	FHL2	physical	10906324

Drug and Disease Associations

Kegg Disease
H00099	Leukocyte adhesion deficiency (LAD), including the following four diseases: Leukocyte adhesion defic
OMIM Disease
116920	Leukocyte adhesion deficiency 1 (LAD1)
Kegg Drug
D08993	Rovelizumab (USAN/INN)
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of ITB2_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"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-50; ASN-116; ASN-212;ASN-213 AND ASN-215, AND MASS SPECTROMETRY.	19349973 [Abstract]
"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-50 AND ASN-212, AND MASSSPECTROMETRY.	19159218 [Abstract]
"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-212, AND MASSSPECTROMETRY.	16335952 [Abstract]
Phosphorylation
Reference	PubMed
"Phosphorylation of the cytoplasmic domain of the integrin CD18 chainby protein kinase C isoforms in leukocytes."; Fagerholm S., Morrice N., Gahmberg C.G., Cohen P.; J. Biol. Chem. 277:1728-1738(2002). Cited for: PHOSPHORYLATION AT SER-745; SER-756; THR-758 AND THR-760.	11700305 [Abstract]

show

show

show

show