dbPTM

NRP1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NRP1_HUMAN
UniProt AC	O14786
Protein Name	Neuropilin-1
Gene Name	NRP1
Organism	Homo sapiens (Human).
Sequence Length	923
Subcellular Localization	Cell membrane Single-pass type I membrane protein. Isoform 2: Secreted.
Protein Description	The membrane-bound isoform 1 is a receptor involved in the development of the cardiovascular system, in angiogenesis, in the formation of certain neuronal circuits and in organogenesis outside the nervous system. It mediates the chemorepulsant activity of semaphorins. It binds to semaphorin 3A, The PLGF-2 isoform of PGF, The VEGF165 isoform of VEGFA and VEGFB. Coexpression with KDR results in increased VEGF165 binding to KDR as well as increased chemotaxis. Regulate VEGF-induced angiogenesis. Binding to VEGFA initiates a signaling pathway needed for motor neuron axon guidance and cell body migration, including for the caudal migration of facial motor neurons from rhombomere 4 to rhombomere 6 during embryonic development (By similarity).; The soluble isoform 2 binds VEGF-165 and appears to inhibit its binding to cells. It may also induce apoptosis by sequestering VEGF-165. May bind as well various members of the semaphorin family. Its expression has an averse effect on blood vessel number and integrity..
Protein Sequence	MERGLPLLCAVLALVLAPAGAFRNDKCGDTIKIESPGYLTSPGYPHSYHPSEKCEWLIQAPDPYQRIMINFNPHFDLEDRDCKYDYVEVFDGENENGHFRGKFCGKIAPPPVVSSGPFLFIKFVSDYETHGAGFSIRYEIFKRGPECSQNYTTPSGVIKSPGFPEKYPNSLECTYIVFVPKMSEIILEFESFDLEPDSNPPGGMFCRYDRLEIWDGFPDVGPHIGRYCGQKTPGRIRSSSGILSMVFYTDSAIAKEGFSANYSVLQSSVSEDFKCMEALGMESGEIHSDQITASSQYSTNWSAERSRLNYPENGWTPGEDSYREWIQVDLGLLRFVTAVGTQGAISKETKKKYYVKTYKIDVSSNGEDWITIKEGNKPVLFQGNTNPTDVVVAVFPKPLITRFVRIKPATWETGISMRFEVYGCKITDYPCSGMLGMVSGLISDSQITSSNQGDRNWMPENIRLVTSRSGWALPPAPHSYINEWLQIDLGEEKIVRGIIIQGGKHRENKVFMRKFKIGYSNNGSDWKMIMDDSKRKAKSFEGNNNYDTPELRTFPALSTRFIRIYPERATHGGLGLRMELLGCEVEAPTAGPTTPNGNLVDECDDDQANCHSGTGDDFQLTGGTTVLATEKPTVIDSTIQSEFPTYGFNCEFGWGSHKTFCHWEHDNHVQLKWSVLTSKTGPIQDHTGDGNFIYSQADENQKGKVARLVSPVVYSQNSAHCMTFWYHMSGSHVGTLRVKLRYQKPEEYDQLVWMAIGHQGDHWKEGRVLLHKSLKLYQVIFEGEIGKGNLGGIAVDDISINNHISQEDCAKPADLDKKNPEIKIDETGSTPGYEGEGEGDKNISRKPGNVLKTLDPILITIIAMSALGVLLGAVCGVVLYCACWHNGMSERNLSALENYNFELVDGVKLKKDKLNTQSTYSEA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
30	Phosphorylation	RNDKCGDTIKIESPG CCCCCCCEEEEECCC	14.95	-
47	Phosphorylation	TSPGYPHSYHPSEKC CCCCCCCCCCCCHHC	22.19	-
51	Phosphorylation	YPHSYHPSEKCEWLI CCCCCCCCHHCEEEE	36.05	-
53	Ubiquitination	HSYHPSEKCEWLIQA CCCCCCHHCEEEECC	41.62	21890473
53	Ubiquitination	HSYHPSEKCEWLIQA CCCCCCHHCEEEECC	41.62	21890473
53	Ubiquitination	HSYHPSEKCEWLIQA CCCCCCHHCEEEECC	41.62	21890473
53	Ubiquitination	HSYHPSEKCEWLIQA CCCCCCHHCEEEECC	41.62	21890473
53 (in isoform 2)	Ubiquitination	-	41.62	21890473
53 (in isoform 1)	Ubiquitination	-	41.62	21890473
53	Ubiquitination	HSYHPSEKCEWLIQA CCCCCCHHCEEEECC	41.62	21890473
106	Ubiquitination	FRGKFCGKIAPPPVV CCCCCCCCCCCCCEE	36.55	21890473
106	Ubiquitination	FRGKFCGKIAPPPVV CCCCCCCCCCCCCEE	36.55	21890473
106	Ubiquitination	FRGKFCGKIAPPPVV CCCCCCCCCCCCCEE	36.55	21890473
106 (in isoform 2)	Ubiquitination	-	36.55	21890473
106 (in isoform 1)	Ubiquitination	-	36.55	21890473
106	Ubiquitination	FRGKFCGKIAPPPVV CCCCCCCCCCCCCEE	36.55	21890473
106	Ubiquitination	FRGKFCGKIAPPPVV CCCCCCCCCCCCCEE	36.55	21890473
150	N-linked_Glycosylation	RGPECSQNYTTPSGV CCCCCCCCCCCCCCC	21.59	17989695
166	Ubiquitination	KSPGFPEKYPNSLEC ECCCCCCCCCCCCEE	67.27	21890473
261	N-linked_Glycosylation	AKEGFSANYSVLQSS HHCCCCCCHHHHHCH	28.54	17989695
267	Phosphorylation	ANYSVLQSSVSEDFK CCHHHHHCHHCCCHH	28.66	-
297	Phosphorylation	QITASSQYSTNWSAE CEEECCCCCCCCCHH	21.29	21653826
300	N-linked_Glycosylation	ASSQYSTNWSAERSR ECCCCCCCCCHHHHC	25.43	UniProtKB CARBOHYD
306	Phosphorylation	TNWSAERSRLNYPEN CCCCHHHHCCCCCCC	32.40	28111955
310	Phosphorylation	AERSRLNYPENGWTP HHHHCCCCCCCCCCC	19.26	28111955
316	Phosphorylation	NYPENGWTPGEDSYR CCCCCCCCCCCCHHH	23.86	28111955
321	Phosphorylation	GWTPGEDSYREWIQV CCCCCCCHHHHHHHH	23.06	28111955
322	Phosphorylation	WTPGEDSYREWIQVD CCCCCCHHHHHHHHH	25.52	28111955
353	Phosphorylation	SKETKKKYYVKTYKI CHHHCCCEEEEEEEE	23.52	-
354	Phosphorylation	KETKKKYYVKTYKID HHHCCCEEEEEEEEE	12.35	-
358	Phosphorylation	KKYYVKTYKIDVSSN CCEEEEEEEEECCCC	10.55	21214269
364	Phosphorylation	TYKIDVSSNGEDWIT EEEEECCCCCCCCEE	49.02	21214269
432	Phosphorylation	KITDYPCSGMLGMVS EECCCCCCHHHHHHH	23.80	-
448	Phosphorylation	LISDSQITSSNQGDR CCCCCHHCCCCCCCC	20.61	-
467	Phosphorylation	ENIRLVTSRSGWALP CCEEEEECCCCCCCC	19.57	24719451
522	N-linked_Glycosylation	FKIGYSNNGSDWKMI EEECCCCCCCCCEEE	45.46	19159218
524	Phosphorylation	IGYSNNGSDWKMIMD ECCCCCCCCCEEEEC	42.28	-
548	Phosphorylation	EGNNNYDTPELRTFP CCCCCCCCHHHHCCC	14.33	24719451
589	O-linked_Glycosylation	GCEVEAPTAGPTTPN CCEEECCCCCCCCCC	51.82	OGP
612	O-linked_Glycosylation	DDQANCHSGTGDDFQ CCCCCCCCCCCCCEE	40.00	16763549
612	O-linked_Glycosylation	DDQANCHSGTGDDFQ CCCCCCCCCCCCCEE	40.00	16763549
637	O-linked_Glycosylation	EKPTVIDSTIQSEFP CCCEEEECCCCCCCC	19.11	OGP
638	O-linked_Glycosylation	KPTVIDSTIQSEFPT CCEEEECCCCCCCCC	21.20	OGP
744	Ubiquitination	RVKLRYQKPEEYDQL EEEEEECCHHHHHHE	45.52	-
764	Ubiquitination	GHQGDHWKEGRVLLH CCCCCCHHHCEEEEE	47.04	-
827	O-linked_Glycosylation	PEIKIDETGSTPGYE CCCEECCCCCCCCCC	32.46	50605481
827	Phosphorylation	PEIKIDETGSTPGYE CCCEECCCCCCCCCC	32.46	-
829	Phosphorylation	IKIDETGSTPGYEGE CEECCCCCCCCCCCC	38.56	-
829	O-linked_Glycosylation	IKIDETGSTPGYEGE CEECCCCCCCCCCCC	38.56	55825021
830	Phosphorylation	KIDETGSTPGYEGEG EECCCCCCCCCCCCC	23.29	-
830	O-linked_Glycosylation	KIDETGSTPGYEGEG EECCCCCCCCCCCCC	23.29	55825027
842	N-linked_Glycosylation	GEGEGDKNISRKPGN CCCCCCCCCCCCCCC	42.06	UniProtKB CARBOHYD
844	O-linked_Glycosylation	GEGDKNISRKPGNVL CCCCCCCCCCCCCHH	43.58	55828097
894	Phosphorylation	GMSERNLSALENYNF CCCHHCHHHHHHCCE	34.06	22617229
899	Phosphorylation	NLSALENYNFELVDG CHHHHHHCCEEEECC	16.32	21082442
908	Ubiquitination	FELVDGVKLKKDKLN EEEECCEEECCCCCC	61.18	-
913 (in isoform 1)	Ubiquitination	-	53.14	21890473
913	Ubiquitination	GVKLKKDKLNTQSTY CEEECCCCCCCCCCC	53.14	2190698
916	Phosphorylation	LKKDKLNTQSTYSEA ECCCCCCCCCCCCCC	34.04	28152594
918	Phosphorylation	KDKLNTQSTYSEA-- CCCCCCCCCCCCC--	27.55	28152594
919	Phosphorylation	DKLNTQSTYSEA--- CCCCCCCCCCCC---	22.65	28152594
920	Phosphorylation	KLNTQSTYSEA---- CCCCCCCCCCC----	15.12	27273156
921	Phosphorylation	LNTQSTYSEA----- CCCCCCCCCC-----	27.43	23403867

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 NRP1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of NRP1_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 NRP1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
VEGFA_HUMAN	VEGFA	physical	11986311
PLGF_HUMAN	PGF	physical	11986311
VEGFB_HUMAN	VEGFB	physical	10409677
VEGFA_HUMAN	VEGFA	physical	9529250
TGFR2_HUMAN	TGFBR2	physical	20675371
TGFR1_HUMAN	TGFBR1	physical	20675371
VEGFA_HUMAN	VEGFA	physical	22318724
PLVAP_HUMAN	PLVAP	physical	22627768
PDGFB_HUMAN	PDGFB	physical	16847823
RL27_HUMAN	RPL27	physical	21988832
TGFR1_HUMAN	TGFBR1	physical	21186301
TGFR2_HUMAN	TGFBR2	physical	21186301
TGBR3_HUMAN	TGFBR3	physical	21186301
VEGFA_HUMAN	VEGFA	physical	20363638
PDGFB_HUMAN	PDGFB	physical	20577048
VGFR2_HUMAN	KDR	physical	19857463
KCTD9_HUMAN	KCTD9	physical	28514442
BCS1_HUMAN	BCS1L	physical	28514442
ODFP2_HUMAN	ODF2	physical	28514442
BACD2_HUMAN	TNFAIP1	physical	28514442
UBR2_HUMAN	UBR2	physical	28514442
CSK21_HUMAN	CSNK2A1	physical	28514442
UBR1_HUMAN	UBR1	physical	28514442
CSK22_HUMAN	CSNK2A2	physical	28514442
NSUN2_HUMAN	NSUN2	physical	28514442
UBR4_HUMAN	UBR4	physical	28514442
BACD3_HUMAN	KCTD10	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.

Regulatory Network of NRP1_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Structural studies of neuropilin/antibody complexes provide insightsinto semaphorin and VEGF binding."; Appleton B.A., Wu P., Maloney J., Yin J., Liang W.C., Stawicki S.,Mortara K., Bowman K.K., Elliott J.M., Desmarais W., Bazan J.F.,Bagri A., Tessier-Lavigne M., Koch A.W., Wu Y., Watts R.J.,Wiesmann C.; EMBO J. 26:4902-4912(2007). Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 141-586 ALONE AND IN COMPLEXWITH ANTIBODY, GLYCOSYLATION AT ASN-150 AND ASN-261, SUBUNIT,CALCIUM-BINDING SITES, HEPARIN-BINDING, AND DISULFIDE BONDS.	17989695 [Abstract]
"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-150; ASN-261 AND ASN-522,AND MASS SPECTROMETRY.	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-150, AND MASSSPECTROMETRY.	16335952 [Abstract]
O-linked Glycosylation
Reference	PubMed
"Glycosaminoglycan modification of neuropilin-1 modulates VEGFR2signaling."; Shintani Y., Takashima S., Asano Y., Kato H., Liao Y., Yamazaki S.,Tsukamoto O., Seguchi O., Yamamoto H., Fukushima T., Sugahara K.,Kitakaze M., Hori M.; EMBO J. 25:3045-3055(2006). Cited for: GLYCOSYLATION AT SER-612.	16763549 [Abstract]
Phosphorylation
Reference	PubMed
"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-920, AND MASSSPECTROMETRY.	18083107 [Abstract]