NADL2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: NADL2_HUMAN
• UniProt AC: Q58DX5
• Protein Name: Inactive N-acetylated-alpha-linked acidic dipeptidase-like protein 2
• Gene Name: NAALADL2
• Organism: Homo sapiens (Human).
• Sequence Length: 795
• Subcellular Localization: Membrane ; Single-pass type II membrane protein .
• Protein Description: May be catalytically inactive..
• Protein Sequence: MGENEASLPNTSLQGKKMAYQKVHADQRAPGHSQYLDNDDLQATALDLEWDMEKELEESGFDQFQLDGAENQNLGHSETIDLNLDSIQPATSPKGRFQRLQEESDYITHYTRSAPKSNRCNFCHVLKILCTATILFIFGILIGYYVHTNCPSDAPSSGTVDPQLYQEILKTIQAEDIKKSFRNLVQLYKNEDDMEISKKIKTQWTSLGLEDVQFVNYSVLLDLPGPSPSTVTLSSSGQCFHPNGQPCSEEARKDSSQDLLYSYAAYSAKGTLKAEVIDVSYGMADDLKRIRKIKNVTNQIALLKLGKLPLLYKLSSLEKAGFGGVLLYIDPCDLPKTVNPSHDTFMVSLNPGGDPSTPGYPSVDESFRQSRSNLTSLLVQPISAPLVAKLISSPKARTKNEACSSLELPNNEIRVVSMQVQTVTKLKTVTNVVGFVMGLTSPDRYIIVGSHHHTAHSYNGQEWASSTAIITAFIRALMSKVKRGWRPDRTIVFCSWGGTAFGNIGSYEWGEDFKKVLQKNVVAYISLHSPIRGNSSLYPVASPSLQQLVVEKNNFNCTRRAQCPETNISSIQIQGDADYFINHLGVPIVQFAYEDIKTLEGPSFLSEARFSTRATKIEEMDPSFNLHETITKLSGEVILQIANEPVLPFNALDIALEVQNNLKGDQPNTHQLLAMALRLRESAELFQSDEMRPANDPKERAPIRIRMLNDILQDMEKSFLVKQAPPGFYRNILYHLDEKTSRFSILIEAWEHCKPLASNETLQEALSEVLNSINSAQVYFKAGLDVFKSVLDGKN

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
33	Phosphorylation	DQRAPGHSQYLDNDD CCCCCCCHHCCCCCH	26.83	28348404
35	Phosphorylation	RAPGHSQYLDNDDLQ CCCCCHHCCCCCHHH	21.02	27642862
92	Phosphorylation	DSIQPATSPKGRFQR CCCCCCCCCCCCHHH	27.07	15168106
104	Phosphorylation	FQRLQEESDYITHYT HHHHHHHHHHHHCCC	34.65	27642862
106	Phosphorylation	RLQEESDYITHYTRS HHHHHHHHHHCCCCC	19.59	25884760
108	Phosphorylation	QEESDYITHYTRSAP HHHHHHHHCCCCCCC	11.55	28331001
110	Phosphorylation	ESDYITHYTRSAPKS HHHHHHCCCCCCCCC	8.66	19060867
111	Phosphorylation	SDYITHYTRSAPKSN HHHHHCCCCCCCCCC	15.56	27642862
188	Phosphorylation	FRNLVQLYKNEDDME HHHHHHHHCCCCHHH	8.48	29083192
263	Phosphorylation	SQDLLYSYAAYSAKG CHHHHHHHHHHHCCC	5.02	-
266	Phosphorylation	LLYSYAAYSAKGTLK HHHHHHHHHCCCCEE	10.86	-
271	Phosphorylation	AAYSAKGTLKAEVID HHHHCCCCEEEEEEE	25.12	19845377
280	Phosphorylation	KAEVIDVSYGMADDL EEEEEECCCCCHHHH	16.54	25159151
281	Phosphorylation	AEVIDVSYGMADDLK EEEEECCCCCHHHHH	15.69	25159151
295	N-linked_Glycosylation	KRIRKIKNVTNQIAL HHHHHHCCCCHHHHH	49.68	UniProtKB CARBOHYD
312	Phosphorylation	LGKLPLLYKLSSLEK HCCCHHHHHHHHHHH	19.98	20049867
373	N-linked_Glycosylation	SFRQSRSNLTSLLVQ HHHHHHHCHHHHHCC	46.35	UniProtKB CARBOHYD
392	Phosphorylation	PLVAKLISSPKARTK HHHHHHHCCCCCCCC	51.53	28060719
393	Phosphorylation	LVAKLISSPKARTKN HHHHHHCCCCCCCCC	24.35	28060719
404	Phosphorylation	RTKNEACSSLELPNN CCCCCCCCCCCCCCC	45.03	29978859
405	Phosphorylation	TKNEACSSLELPNNE CCCCCCCCCCCCCCC	26.25	29978859
524	Phosphorylation	LQKNVVAYISLHSPI HHHCCEEEEEECCCC	4.57	-
526	Phosphorylation	KNVVAYISLHSPIRG HCCEEEEEECCCCCC	13.83	-
529	Phosphorylation	VAYISLHSPIRGNSS EEEEEECCCCCCCCC	27.58	-
534	N-linked_Glycosylation	LHSPIRGNSSLYPVA ECCCCCCCCCCCCCC	20.69	UniProtKB CARBOHYD
603	Phosphorylation	IKTLEGPSFLSEARF HHHCCCCCHHHHHHH	50.07	26074081
606	Phosphorylation	LEGPSFLSEARFSTR CCCCCHHHHHHHCCC	27.48	26074081
740	Phosphorylation	LYHLDEKTSRFSILI HHHCCCCCCCCHHHH	24.08	-
759	N-linked_Glycosylation	HCKPLASNETLQEAL HCCCCCCCHHHHHHH	40.44	UniProtKB CARBOHYD

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

Oops, there are no upstream regulatory protein records of NADL2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of NADL2_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 NADL2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
SCAP_HUMAN	SCAP	physical	26186194
KLC2_HUMAN	KLC2	physical	26186194
NALD2_HUMAN	NAALAD2	physical	26186194
KCD17_HUMAN	KCTD17	physical	26186194
IGSF3_HUMAN	IGSF3	physical	26186194
ERBB2_HUMAN	ERBB2	physical	26186194
KCNJ8_HUMAN	KCNJ8	physical	26186194
CELR2_HUMAN	CELSR2	physical	26186194
SCRB2_HUMAN	SCARB2	physical	26186194
2B1F_HUMAN	HLA-DRB1	physical	26186194
2B13_HUMAN	HLA-DRB1	physical	26186194
2B1G_HUMAN	HLA-DRB1	physical	26186194
IGSF3_HUMAN	IGSF3	physical	28514442
NALD2_HUMAN	NAALAD2	physical	28514442
KLC2_HUMAN	KLC2	physical	28514442
ERBB2_HUMAN	ERBB2	physical	28514442
CELR2_HUMAN	CELSR2	physical	28514442
KCNJ8_HUMAN	KCNJ8	physical	28514442

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

Phosphorylation

"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-106, AND MASSSPECTROMETRY.
PubMed: 18083107