dbPTM

ALS_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ALS_HUMAN
UniProt AC	P35858
Protein Name	Insulin-like growth factor-binding protein complex acid labile subunit
Gene Name	IGFALS
Organism	Homo sapiens (Human).
Sequence Length	605
Subcellular Localization	Secreted, extracellular space.
Protein Description	Involved in protein-protein interactions that result in protein complexes, receptor-ligand binding or cell adhesion..
Protein Sequence	MALRKGGLALALLLLSWVALGPRSLEGADPGTPGEAEGPACPAACVCSYDDDADELSVFCSSRNLTRLPDGVPGGTQALWLDGNNLSSVPPAAFQNLSSLGFLNLQGGQLGSLEPQALLGLENLCHLHLERNQLRSLALGTFAHTPALASLGLSNNRLSRLEDGLFEGLGSLWDLNLGWNSLAVLPDAAFRGLGSLRELVLAGNRLAYLQPALFSGLAELRELDLSRNALRAIKANVFVQLPRLQKLYLDRNLIAAVAPGAFLGLKALRWLDLSHNRVAGLLEDTFPGLLGLRVLRLSHNAIASLRPRTFKDLHFLEELQLGHNRIRQLAERSFEGLGQLEVLTLDHNQLQEVKAGAFLGLTNVAVMNLSGNCLRNLPEQVFRGLGKLHSLHLEGSCLGRIRPHTFTGLSGLRRLFLKDNGLVGIEEQSLWGLAELLELDLTSNQLTHLPHRLFQGLGKLEYLLLSRNRLAELPADALGPLQRAFWLDVSHNRLEALPNSLLAPLGRLRYLSLRNNSLRTFTPQPPGLERLWLEGNPWDCGCPLKALRDFALQNPSAVPRFVQAICEGDDCQPPAYTYNNITCASPPEVVGLDLRDLSEAHFAPC

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
32	O-linked_Glycosylation	LEGADPGTPGEAEGP CCCCCCCCCCCCCCC	33.24	OGP
64	N-linked_Glycosylation	SVFCSSRNLTRLPDG EEEECCCCCCCCCCC	47.95	UniProtKB CARBOHYD
85	N-linked_Glycosylation	ALWLDGNNLSSVPPA EEEECCCCCCCCCCH	46.99	UniProtKB CARBOHYD
96	N-linked_Glycosylation	VPPAAFQNLSSLGFL CCCHHHCCHHHCCCE	35.12	UniProtKB CARBOHYD
195	Phosphorylation	AAFRGLGSLRELVLA HHHCCCCCHHHHHHH	29.33	24719451
304	Phosphorylation	LSHNAIASLRPRTFK HCHHHHHHCCCCCHH	20.85	24719451
342	Phosphorylation	EGLGQLEVLTLDHNQ CCCCEEEEEECCHHH	7.23	24719451
368	N-linked_Glycosylation	LTNVAVMNLSGNCLR CCCEEEEECCCCHHH	25.18	16335952
407	Phosphorylation	RIRPHTFTGLSGLRR CCCCCCCCCCHHHHH	38.07	-
410	Phosphorylation	PHTFTGLSGLRRLFL CCCCCCCHHHHHHHC	36.81	24719451
510	Phosphorylation	APLGRLRYLSLRNNS HHHHHHHHHHHCCCC	12.77	24719451
512	Phosphorylation	LGRLRYLSLRNNSLR HHHHHHHHHCCCCCC	19.15	24719451
515	N-linked_Glycosylation	LRYLSLRNNSLRTFT HHHHHHCCCCCCCCC	47.97	16335952
517	Phosphorylation	YLSLRNNSLRTFTPQ HHHHCCCCCCCCCCC	23.83	24719451
548	Phosphorylation	GCPLKALRDFALQNP CCCHHHHHHHHHHCC	41.69	24719451
550	Phosphorylation	PLKALRDFALQNPSA CHHHHHHHHHHCCCH	6.21	24719451
555	Phosphorylation	RDFALQNPSAVPRFV HHHHHHCCCHHHHHH	15.65	24719451
580	N-linked_Glycosylation	PPAYTYNNITCASPP CCCEEECCEEECCCC	22.12	UniProtKB CARBOHYD

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 ALS_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ALS_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 ALS_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
IBP3_HUMAN	IGFBP3	physical	9497324
IBP5_HUMAN	IGFBP5	physical	9497324
IBP3_HUMAN	IGFBP3	physical	9446566

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615961	Acid-labile subunit deficiency (ACLSD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of ALS_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"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-368, 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-368 AND ASN-515, AND MASSSPECTROMETRY.	16335952 [Abstract]