dbPTM

APLP1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	APLP1_HUMAN
UniProt AC	P51693
Protein Name	Amyloid-like protein 1
Gene Name	APLP1
Organism	Homo sapiens (Human).
Sequence Length	650
Subcellular Localization	Cell membrane Single-pass type I membrane protein. C30: Cytoplasm. C-terminally processed in the Golgi complex.
Protein Description	May play a role in postsynaptic function. The C-terminal gamma-secretase processed fragment, ALID1, activates transcription activation through APBB1 (Fe65) binding (By similarity). Couples to JIP signal transduction through C-terminal binding. May interact with cellular G-protein signaling pathways. Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I.; The gamma-CTF peptide, C30, is a potent enhancer of neuronal apoptosis..
Protein Sequence	MGPASPAARGLSRRPGQPPLPLLLPLLLLLLRAQPAIGSLAGGSPGAAEAPGSAQVAGLCGRLTLHRDLRTGRWEPDPQRSRRCLRDPQRVLEYCRQMYPELQIARVEQATQAIPMERWCGGSRSGSCAHPHHQVVPFRCLPGEFVSEALLVPEGCRFLHQERMDQCESSTRRHQEAQEACSSQGLILHGSGMLLPCGSDRFRGVEYVCCPPPGTPDPSGTAVGDPSTRSWPPGSRVEGAEDEEEEESFPQPVDDYFVEPPQAEEEEETVPPPSSHTLAVVGKVTPTPRPTDGVDIYFGMPGEISEHEGFLRAKMDLEERRMRQINEVMREWAMADNQSKNLPKADRQALNEHFQSILQTLEEQVSGERQRLVETHATRVIALINDQRRAALEGFLAALQADPPQAERVLLALRRYLRAEQKEQRHTLRHYQHVAAVDPEKAQQMRFQVHTHLQVIEERVNQSLGLLDQNPHLAQELRPQIQELLHSEHLGPSELEAPAPGGSSEDKGGLQPPDSKDDTPMTLPKGSTEQDAASPEKEKMNPLEQYERKVNASVPRGFPFHSSEIQRDELAPAGTGVSREAVSGLLIMGAGGGSLIVLSMLLLRRKKPYGAISHGVVEVDPMLTLEEQQLRELQRHGYENPTYRFLEERP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5	Phosphorylation	---MGPASPAARGLS ---CCCCCHHHHCCC	20.43	26329039
12	Phosphorylation	SPAARGLSRRPGQPP CHHHHCCCCCCCCCC	29.12	25002506
215	O-linked_Glycosylation	VCCPPPGTPDPSGTA EECCCCCCCCCCCCC	30.23	19838169
227	O-linked_Glycosylation	GTAVGDPSTRSWPPG CCCCCCCCCCCCCCC	40.99	19838169
228	O-linked_Glycosylation	TAVGDPSTRSWPPGS CCCCCCCCCCCCCCC	33.83	19838169
277	O-linked_Glycosylation	VPPPSSHTLAVVGKV CCCCCCCEEEEEEEE	20.54	OGP
337	N-linked_Glycosylation	REWAMADNQSKNLPK HHHHHHCCCCCCCCH	38.19	9428684
366	Phosphorylation	QTLEEQVSGERQRLV HHHHHHHCCHHHHHH	34.33	27732954
461	N-linked_Glycosylation	QVIEERVNQSLGLLD HHHHHHHHHHCCCCC	31.76	9428684
551	N-linked_Glycosylation	EQYERKVNASVPRGF HHHHHHHHCCCCCCC	29.54	9428684
553	Phosphorylation	YERKVNASVPRGFPF HHHHHHCCCCCCCCC	27.70	24719451
578	Phosphorylation	APAGTGVSREAVSGL CCCCCCCCHHHHHCE	26.25	23879269
599	Phosphorylation	GGSLIVLSMLLLRRK HHHHHHHHHHHHHCC	9.11	22210691
638	Phosphorylation	RELQRHGYENPTYRF HHHHHCCCCCCHHHH	13.35	25884760
642	Phosphorylation	RHGYENPTYRFLEER HCCCCCCHHHHHCCC	38.62	28152594
643	Phosphorylation	HGYENPTYRFLEERP CCCCCCHHHHHCCCC	10.71	25884760

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 APLP1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
227	S	Glycosylation	19838169
Glycosylation on Ser-227 is the preferred site to Thr-228.
228	T	Glycosylation	19838169
Glycosylation on Ser-227 is the preferred site to Thr-228.

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 APLP1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DAB1_HUMAN	DAB1	physical	10460257
UT14A_HUMAN	UTP14A	physical	16169070
EF1A1_HUMAN	EEF1A1	physical	15383276
ING5_HUMAN	ING5	physical	15383276
GDF9_HUMAN	GDF9	physical	15383276
SETB1_HUMAN	SETDB1	physical	15383276
UT14A_HUMAN	UTP14A	physical	15383276
LRIF1_HUMAN	LRIF1	physical	15383276
HAP1_HUMAN	HAP1	physical	15383276
RBM48_HUMAN	RBM48	physical	15383276
ZNF24_HUMAN	ZNF24	physical	16169070

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.

Regulatory Network of APLP1_HUMAN

Related Literatures of Post-Translational Modification

O-linked Glycosylation
Reference	PubMed
"Enrichment of glycopeptides for glycan structure and attachment siteidentification."; Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E.,Brinkmalm G., Larson G.; Nat. Methods 6:809-811(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT THR-215; SER-227 AND THR-228,STRUCTURE OF CARBOHYDRATES, AND MASS SPECTROMETRY.	19838169 [Abstract]

show

show