ITA1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ITA1_HUMAN
• UniProt AC: P56199
• Protein Name: Integrin alpha-1
• Gene Name: ITGA1
• Organism: Homo sapiens (Human).
• Sequence Length: 1179
• Subcellular Localization: Membrane; Single-pass type I membrane protein.
• Protein Description: Integrin alpha-1/beta-1 is a receptor for laminin and collagen. It recognizes the proline-hydroxylated sequence G-F-P-G-E-R in collagen. Involved in anchorage-dependent, negative regulation of EGF-stimulated cell growth..
• Protein Sequence: MAPRPRARPGVAVACCWLLTVVLRCCVSFNVDVKNSMTFSGPVEDMFGYTVQQYENEEGKWVLIGSPLVGQPKNRTGDVYKCPVGRGESLPCVKLDLPVNTSIPNVTEVKENMTFGSTLVTNPNGGFLACGPLYAYRCGHLHYTTGICSDVSPTFQVVNSIAPVQECSTQLDIVIVLDGSNSIYPWDSVTAFLNDLLERMDIGPKQTQVGIVQYGENVTHEFNLNKYSSTEEVLVAAKKIVQRGGRQTMTALGIDTARKEAFTEARGARRGVKKVMVIVTDGESHDNHRLKKVIQDCEDENIQRFSIAILGSYNRGNLSTEKFVEEIKSIASEPTEKHFFNVSDELALVTIVKTLGERIFALEATADQSAASFEMEMSQTGFSAHYSQDWVMLGAVGAYDWNGTVVMQKASQIIIPRNTTFNVESTKKNEPLASYLGYTVNSATASSGDVLYIAGQPRYNHTGQVIIYRMEDGNIKILQTLSGEQIGSYFGSILTTTDIDKDSNTDILLVGAPMYMGTEKEEQGKVYVYALNQTRFEYQMSLEPIKQTCCSSRQHNSCTTENKNEPCGARFGTAIAAVKDLNLDGFNDIVIGAPLEDDHGGAVYIYHGSGKTIRKEYAQRIPSGGDGKTLKFFGQSIHGEMDLNGDGLTDVTIGGLGGAALFWSRDVAVVKVTMNFEPNKVNIQKKNCHMEGKETVCINATVCFDVKLKSKEDTIYEADLQYRVTLDSLRQISRSFFSGTQERKVQRNITVRKSECTKHSFYMLDKHDFQDSVRITLDFNLTDPENGPVLDDSLPNSVHEYIPFAKDCGNKEKCISDLSLHVATTEKDLLIVRSQNDKFNVSLTVKNTKDSAYNTRTIVHYSPNLVFSGIEAIQKDSCESNHNITCKVGYPFLRRGEMVTFKILFQFNTSYLMENVTIYLSATSDSEEPPETLSDNVVNISIPVKYEVGLQFYSSASEYHISIAANETVPEVINSTEDIGNEINIFYLIRKSGSFPMPELKLSISFPNMTSNGYPVLYPTGLSSSENANCRPHIFEDPFSINSGKKMTTSTDHLKRGTILDCNTCKFATITCNLTSSDISQVNVSLILWKPTFIKSYFSSLNLTIRGELRSENASLVLSSSNQKRELAIQISKDGLPGRVPLWVILLSAFAGLLLLMLLILALWKIGFFKRPLKKKMEK

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
74	N-linked_Glycosylation	PLVGQPKNRTGDVYK CCCCCCCCCCCCEEE	54.12	UniProtKB CARBOHYD
76	Phosphorylation	VGQPKNRTGDVYKCP CCCCCCCCCCEEECC	47.31	22210691
80	Phosphorylation	KNRTGDVYKCPVGRG CCCCCCEEECCCCCC	16.18	22210691
81	Ubiquitination	NRTGDVYKCPVGRGE CCCCCEEECCCCCCC	31.73	29967540
89	Phosphorylation	CPVGRGESLPCVKLD CCCCCCCCCCEEEEE	40.20	22210691
100	N-linked_Glycosylation	VKLDLPVNTSIPNVT EEEECCCCCCCCCCC	26.60	19349973
100	N-linked_Glycosylation	VKLDLPVNTSIPNVT EEEECCCCCCCCCCC	26.60	19159218
105	N-linked_Glycosylation	PVNTSIPNVTEVKEN CCCCCCCCCCEEECC	52.23	19349973
105	N-linked_Glycosylation	PVNTSIPNVTEVKEN CCCCCCCCCCEEECC	52.23	19159218
112	N-linked_Glycosylation	NVTEVKENMTFGSTL CCCEEECCCEECCEE	29.13	UniProtKB CARBOHYD
217	N-linked_Glycosylation	GIVQYGENVTHEFNL EEEEECCCEEEEEEC	39.36	19159218
227	Phosphorylation	HEFNLNKYSSTEEVL EEEECCCCCCHHHHH	13.54	26074081
228	Phosphorylation	EFNLNKYSSTEEVLV EEECCCCCCHHHHHH	32.18	26074081
229	Phosphorylation	FNLNKYSSTEEVLVA EECCCCCCHHHHHHH	36.43	26074081
230	Phosphorylation	NLNKYSSTEEVLVAA ECCCCCCHHHHHHHH	30.17	26074081
248	Phosphorylation	VQRGGRQTMTALGID HHCCCCHHHHCCCCH	18.35	26074081
250	Phosphorylation	RGGRQTMTALGIDTA CCCCHHHHCCCCHHH	23.32	26074081
256	Phosphorylation	MTALGIDTARKEAFT HHCCCCHHHHHHHHH	26.83	26074081
274	Acetylation	GARRGVKKVMVIVTD HHHCCCCEEEEEEEC	32.91	7308077
317	N-linked_Glycosylation	LGSYNRGNLSTEKFV ECCCCCCCCCHHHHH	27.81	UniProtKB CARBOHYD
328	Ubiquitination	EKFVEEIKSIASEPT HHHHHHHHHHCCCCC	38.80	29967540
341	N-linked_Glycosylation	PTEKHFFNVSDELAL CCHHHCCCCCHHHHH	31.29	19159218
402	N-linked_Glycosylation	AVGAYDWNGTVVMQK EEEEECCCCEEEEEE	33.10	UniProtKB CARBOHYD
418	N-linked_Glycosylation	SQIIIPRNTTFNVES CEEEECCCCEECCCC	37.81	19159218
419	Phosphorylation	QIIIPRNTTFNVEST EEEECCCCEECCCCC	33.76	29083192
420	Phosphorylation	IIIPRNTTFNVESTK EEECCCCEECCCCCC	19.43	29083192
425	Phosphorylation	NTTFNVESTKKNEPL CCEECCCCCCCCCCC	41.04	29083192
426	Phosphorylation	TTFNVESTKKNEPLA CEECCCCCCCCCCCH	32.31	29083192
460	N-linked_Glycosylation	IAGQPRYNHTGQVII EECCCCCCCCCCEEE	27.76	19159218
527	Phosphorylation	KEEQGKVYVYALNQT CHHCCEEEEEEEECC	7.39	-
532	N-linked_Glycosylation	KVYVYALNQTRFEYQ EEEEEEEECCEEEEE	32.76	16335952
538	Phosphorylation	LNQTRFEYQMSLEPI EECCEEEEEECCHHH	13.55	20068231
541	Phosphorylation	TRFEYQMSLEPIKQT CEEEEEECCHHHHHH	17.66	20068231
548	Phosphorylation	SLEPIKQTCCSSRQH CCHHHHHHHCCCCCC	15.52	24043423
551	Phosphorylation	PIKQTCCSSRQHNSC HHHHHHCCCCCCCCC	30.60	24043423
552	Phosphorylation	IKQTCCSSRQHNSCT HHHHHCCCCCCCCCC	23.26	24043423
604	Phosphorylation	DDHGGAVYIYHGSGK CCCCCEEEEECCCCC	8.67	-
612	Phosphorylation	IYHGSGKTIRKEYAQ EECCCCCEEHHHHHH	29.55	-
617	Phosphorylation	GKTIRKEYAQRIPSG CCEEHHHHHHHCCCC	15.86	30257219
623	Phosphorylation	EYAQRIPSGGDGKTL HHHHHCCCCCCCCEE	53.70	23403867
629	Phosphorylation	PSGGDGKTLKFFGQS CCCCCCCEEEECCCC	40.48	30175587
664	Phosphorylation	GGAALFWSRDVAVVK CHHEEEEECCEEEEE	15.98	30175587
699	N-linked_Glycosylation	GKETVCINATVCFDV CCCEEEEEEEEEEEE	25.16	UniProtKB CARBOHYD
709	Ubiquitination	VCFDVKLKSKEDTIY EEEEEEECCCCCCEE	54.48	-
748	N-linked_Glycosylation	QERKVQRNITVRKSE CCEEEECCEEEEHHH	19.72	UniProtKB CARBOHYD
780	N-linked_Glycosylation	VRITLDFNLTDPENG EEEEEECCCCCCCCC	41.52	19159218
816	Phosphorylation	GNKEKCISDLSLHVA CCHHHHHHHEEEEEE	41.80	30631047
819	Phosphorylation	EKCISDLSLHVATTE HHHHHHEEEEEECCC	22.78	30631047
825	Phosphorylation	LSLHVATTEKDLLIV EEEEEECCCCCEEEE	31.16	30631047
834	Phosphorylation	KDLLIVRSQNDKFNV CCEEEEECCCCCEEE	23.57	-
840	N-linked_Glycosylation	RSQNDKFNVSLTVKN ECCCCCEEEEEEEEE	28.36	19159218
883	N-linked_Glycosylation	DSCESNHNITCKVGY CCCCCCCCCEEEECC	35.20	UniProtKB CARBOHYD
890	Phosphorylation	NITCKVGYPFLRRGE CCEEEECCCEECCCC	8.19	-
908	N-linked_Glycosylation	FKILFQFNTSYLMEN EEEEEEECHHHEEEC	19.82	UniProtKB CARBOHYD
915	N-linked_Glycosylation	NTSYLMENVTIYLSA CHHHEEECEEEEEEE	23.44	UniProtKB CARBOHYD
939	N-linked_Glycosylation	TLSDNVVNISIPVKY CCCCCEEEEECCEEE	20.29	UniProtKB CARBOHYD
966	N-linked_Glycosylation	YHISIAANETVPEVI EEEEEECCCCCCCHH	36.13	19159218
974	N-linked_Glycosylation	ETVPEVINSTEDIGN CCCCCHHHCCHHHCC	48.32	19159218
992	Phosphorylation	IFYLIRKSGSFPMPE EEEEEECCCCCCCCC	29.80	22673903
994	Phosphorylation	YLIRKSGSFPMPELK EEEECCCCCCCCCEE	33.01	22673903
1008	N-linked_Glycosylation	KLSISFPNMTSNGYP EEEEECCCCCCCCEE	44.33	19159218
1046	Ubiquitination	FSINSGKKMTTSTDH CCCCCCCCCCCCCCC	45.03	29967540
1073	N-linked_Glycosylation	KFATITCNLTSSDIS CEEEEEEECCCCCCC	37.39	UniProtKB CARBOHYD
1083	N-linked_Glycosylation	SSDISQVNVSLILWK CCCCCCCEEEEEEEC	15.26	UniProtKB CARBOHYD
1102	N-linked_Glycosylation	KSYFSSLNLTIRGEL HHHHHHCCEEEECEE	36.77	UniProtKB CARBOHYD
1104	Phosphorylation	YFSSLNLTIRGELRS HHHHCCEEEECEECC	13.93	24719451
1113	N-linked_Glycosylation	RGELRSENASLVLSS ECEECCCCCEEEECC	35.76	UniProtKB CARBOHYD
1115	Phosphorylation	ELRSENASLVLSSSN EECCCCCEEEECCCC	30.50	24043423
1119	Phosphorylation	ENASLVLSSSNQKRE CCCEEEECCCCCCEE	25.00	24043423
1120	Phosphorylation	NASLVLSSSNQKREL CCEEEECCCCCCEEE	29.19	24043423
1121	Phosphorylation	ASLVLSSSNQKRELA CEEEECCCCCCEEEE	39.65	24043423
1132	Phosphorylation	RELAIQISKDGLPGR EEEEEEECCCCCCCC	14.33	20068231

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of ITA1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ITA1_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of ITA1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
BIN1_HUMAN	BIN1	physical	10094488
TLN1_HUMAN	TLN1	physical	11336656
MATN1_HUMAN	MATN1	physical	10196235
SHRPN_HUMAN	SHARPIN	physical	21947080

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.

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"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-100; ASN-105; ASN-217;ASN-341; ASN-418; ASN-460; ASN-532; ASN-780; ASN-840; ASN-966; ASN-974AND ASN-1008, AND MASS SPECTROMETRY.
PubMed: 19159218

"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-532, AND MASSSPECTROMETRY.
PubMed: 16335952