NCAM2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: NCAM2_HUMAN
• UniProt AC: O15394
• Protein Name: Neural cell adhesion molecule 2
• Gene Name: NCAM2
• Organism: Homo sapiens (Human).
• Sequence Length: 837
• Subcellular Localization: Cell membrane; Single-pass type I membrane protein.
• Protein Description: May play important roles in selective fasciculation and zone-to-zone projection of the primary olfactory axons..
• Protein Sequence: MSLLLSFYLLGLLVSSGQALLQVTISLSKVELSVGESKFFTCTAIGEPESIDWYNPQGEKIISTQRVVVQKEGVRSRLTIYNANIEDAGIYRCQATDAKGQTQEATVVLEIYQKLTFREVVSPQEFKQGEDAEVVCRVSSSPAPAVSWLYHNEEVTTISDNRFAMLANNNLQILNINKSDEGIYRCEGRVEARGEIDFRDIIVIVNVPPAISMPQKSFNATAERGEEMTFSCRASGSPEPAISWFRNGKLIEENEKYILKGSNTELTVRNIINSDGGPYVCRATNKAGEDEKQAFLQVFVQPHIIQLKNETTYENGQVTLVCDAEGEPIPEITWKRAVDGFTFTEGDKSLDGRIEVKGQHGSSSLHIKDVKLSDSGRYDCEAASRIGGHQKSMYLDIEYAPKFISNQTIYYSWEGNPINISCDVKSNPPASIHWRRDKLVLPAKNTTNLKTYSTGRKMILEIAPTSDNDFGRYNCTATNHIGTRFQEYILALADVPSSPYGVKIIELSQTTAKVSFNKPDSHGGVPIHHYQVDVKEVASEIWKIVRSHGVQTMVVLNNLEPNTTYEIRVAAVNGKGQGDYSKIEIFQTLPVREPSPPSIHGQPSSGKSFKLSITKQDDGGAPILEYIVKYRSKDKEDQWLEKKVQGNKDHIILEHLQWTMGYEVQITAANRLGYSEPTVYEFSMPPKPNIIKDTLFNGLGLGAVIGLGVAALLLILVVTDVSCFFIRQCGLLMCITRRMCGKKSGSSGKSKELEEGKAAYLKDGSKEPIVEMRTEDERVTNHEDGSPVNEPNETTPLTEPEKLPLKEEDGKEALNPETIEIKVSNDIIQSKEDDSKA

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
2	Phosphorylation	------MSLLLSFYL ------CCHHHHHHH	27.94	24043423
6	Phosphorylation	--MSLLLSFYLLGLL --CCHHHHHHHHHHH	16.30	24043423
8	Phosphorylation	MSLLLSFYLLGLLVS CCHHHHHHHHHHHHH	9.53	24043423
15	Phosphorylation	YLLGLLVSSGQALLQ HHHHHHHHCCCHHHE	28.81	24043423
16	Phosphorylation	LLGLLVSSGQALLQV HHHHHHHCCCHHHEE	27.69	24043423
24	Phosphorylation	GQALLQVTISLSKVE CCHHHEEEEEEEEEE	7.59	24043423
26	Phosphorylation	ALLQVTISLSKVELS HHHEEEEEEEEEEEE	19.75	24719451
28	Phosphorylation	LQVTISLSKVELSVG HEEEEEEEEEEEEEC	28.06	24043423
33	Phosphorylation	SLSKVELSVGESKFF EEEEEEEEECCCCEE	17.99	29514088
37	Phosphorylation	VELSVGESKFFTCTA EEEEECCCCEEEEEE	28.91	29514088
91	Phosphorylation	NIEDAGIYRCQATDA CHHHCEEEEEEEECC	12.38	-
116	Phosphorylation	LEIYQKLTFREVVSP HHHHHHCCCEECCCH	27.90	20058876
122	Phosphorylation	LTFREVVSPQEFKQG CCCEECCCHHHHHCC	26.49	20058876
177	N-linked_Glycosylation	NLQILNINKSDEGIY CEEEEECCCCCCCEE	36.38	UniProtKB CARBOHYD
219	N-linked_Glycosylation	SMPQKSFNATAERGE CCCHHCCCCCCCCCC	43.39	UniProtKB CARBOHYD
309	N-linked_Glycosylation	PHIIQLKNETTYENG CEEEECCCEEEEECC	61.51	UniProtKB CARBOHYD
406	N-linked_Glycosylation	YAPKFISNQTIYYSW EECHHCCCCEEEEEE	37.89	UniProtKB CARBOHYD
419	N-linked_Glycosylation	SWEGNPINISCDVKS EECCCEEEEEEECCC	22.75	UniProtKB CARBOHYD
445	N-linked_Glycosylation	KLVLPAKNTTNLKTY EEEEECCCCCCCEEE	55.00	12754519
451	Phosphorylation	KNTTNLKTYSTGRKM CCCCCCEEECCCCEE	26.35	-
453	Phosphorylation	TTNLKTYSTGRKMIL CCCCEEECCCCEEEE	29.62	-
474	N-linked_Glycosylation	DNDFGRYNCTATNHI CCCCCCCCCCCCCCC	18.46	UniProtKB CARBOHYD
562	N-linked_Glycosylation	VLNNLEPNTTYEIRV EECCCCCCCEEEEEE	35.36	12754519
598	Ubiquitination	VREPSPPSIHGQPSS CCCCCCCCCCCCCCC	30.51	22817900
602	Ubiquitination	SPPSIHGQPSSGKSF CCCCCCCCCCCCCCE	22.12	22817900
608	Phosphorylation	GQPSSGKSFKLSITK CCCCCCCCEEEEEEE	31.01	29083192
612	Phosphorylation	SGKSFKLSITKQDDG CCCCEEEEEEECCCC	28.89	24719451
614	Phosphorylation	KSFKLSITKQDDGGA CCEEEEEEECCCCCC	21.19	26074081
626	Phosphorylation	GGAPILEYIVKYRSK CCCCCHHHHHHCCCC	13.94	26074081
630	Phosphorylation	ILEYIVKYRSKDKED CHHHHHHCCCCCHHH	14.82	26074081
632	Phosphorylation	EYIVKYRSKDKEDQW HHHHHCCCCCHHHHH	41.96	26074081
723	S-palmitoylation	LVVTDVSCFFIRQCG HHHHCHHHHHHHHHH	3.03	10223357
729	S-palmitoylation	SCFFIRQCGLLMCIT HHHHHHHHHHHHHHH	2.73	10223357
734	S-palmitoylation	RQCGLLMCITRRMCG HHHHHHHHHHHHHHC	2.65	10223357
740	S-palmitoylation	MCITRRMCGKKSGSS HHHHHHHHCCCCCCC	7.39	10223357
757	Ubiquitination	SKELEEGKAAYLKDG CCCHHCCCEEEECCC	32.88	-
760	Phosphorylation	LEEGKAAYLKDGSKE HHCCCEEEECCCCCC	21.10	25219547
762	Ubiquitination	EGKAAYLKDGSKEPI CCCEEEECCCCCCCC	47.57	22817900
765	Phosphorylation	AAYLKDGSKEPIVEM EEEECCCCCCCCEEE	43.93	25849741
766	Ubiquitination	AYLKDGSKEPIVEMR EEECCCCCCCCEEEE	73.39	22817900
774	Phosphorylation	EPIVEMRTEDERVTN CCCEEEECCCCCCCC	46.61	25849741
780	Phosphorylation	RTEDERVTNHEDGSP ECCCCCCCCCCCCCC	36.76	25849741
786	Phosphorylation	VTNHEDGSPVNEPNE CCCCCCCCCCCCCCC	37.69	18510355
787	Ubiquitination	TNHEDGSPVNEPNET CCCCCCCCCCCCCCC	38.18	22817900
791	Ubiquitination	DGSPVNEPNETTPLT CCCCCCCCCCCCCCC	38.46	22817900
794	Phosphorylation	PVNEPNETTPLTEPE CCCCCCCCCCCCCCC	40.11	18510355
795	Phosphorylation	VNEPNETTPLTEPEK CCCCCCCCCCCCCCC	15.32	18510355
811	Acetylation	PLKEEDGKEALNPET CCCCCCCCCCCCHHH	52.73	22368915
818	Phosphorylation	KEALNPETIEIKVSN CCCCCHHHEEEEEEC	25.76	27251275
824	Phosphorylation	ETIEIKVSNDIIQSK HHEEEEEECCHHCCC	24.63	25849741
836	Acetylation	QSKEDDSKA------ CCCCCCCCC------	66.17	22368923

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

Oops, there are no upstream regulatory protein records of NCAM2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of NCAM2_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 NCAM2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DHPR_HUMAN	QDPR	physical	26344197

Drug and Disease Associations

• Kegg Disease
• H00010: Multiple myeloma
• 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

"Identification and quantification of N-linked glycoproteins usinghydrazide chemistry, stable isotope labeling and mass spectrometry.";
Zhang H., Li X.-J., Martin D.B., Aebersold R.;
Nat. Biotechnol. 21:660-666(2003).
Cited for: GLYCOSYLATION AT ASN-445 AND ASN-562.
PubMed: 12754519