dbPTM

SORT_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SORT_HUMAN
UniProt AC	Q99523
Protein Name	Sortilin
Gene Name	SORT1
Organism	Homo sapiens (Human).
Sequence Length	831
Subcellular Localization	Membrane Single-pass type I membrane protein. Endoplasmic reticulum membrane Single-pass type I membrane protein . Endosome membrane Single-pass type I membrane protein . Golgi apparatus, Golgi stack membrane Single-pass type I membrane protein . N
Protein Description	Functions as a sorting receptor in the Golgi compartment and as a clearance receptor on the cell surface. Required for protein transport from the Golgi apparatus to the lysosomes by a pathway that is independent of the mannose-6-phosphate receptor (M6PR). Also required for protein transport from the Golgi apparatus to the endosomes. Promotes neuronal apoptosis by mediating endocytosis of the proapoptotic precursor forms of BDNF (proBDNF) and NGFB (proNGFB). Also acts as a receptor for neurotensin. May promote mineralization of the extracellular matrix during osteogenic differentiation by scavenging extracellular LPL. Probably required in adipocytes for the formation of specialized storage vesicles containing the glucose transporter SLC2A4/GLUT4 (GLUT4 storage vesicles, or GSVs). These vesicles provide a stable pool of SLC2A4 and confer increased responsiveness to insulin. May also mediate transport from the endoplasmic reticulum to the Golgi..
Protein Sequence	MERPWGAADGLSRWPHGLGLLLLLQLLPPSTLSQDRLDAPPPPAAPLPRWSGPIGVSWGLRAAAAGGAFPRGGRWRRSAPGEDEECGRVRDFVAKLANNTHQHVFDDLRGSVSLSWVGDSTGVILVLTTFHVPLVIMTFGQSKLYRSEDYGKNFKDITDLINNTFIRTEFGMAIGPENSGKVVLTAEVSGGSRGGRIFRSSDFAKNFVQTDLPFHPLTQMMYSPQNSDYLLALSTENGLWVSKNFGGKWEEIHKAVCLAKWGSDNTIFFTTYANGSCKADLGALELWRTSDLGKSFKTIGVKIYSFGLGGRFLFASVMADKDTTRRIHVSTDQGDTWSMAQLPSVGQEQFYSILAANDDMVFMHVDEPGDTGFGTIFTSDDRGIVYSKSLDRHLYTTTGGETDFTNVTSLRGVYITSVLSEDNSIQTMITFDQGGRWTHLRKPENSECDATAKNKNECSLHIHASYSISQKLNVPMAPLSEPNAVGIVIAHGSVGDAISVMVPDVYISDDGGYSWTKMLEGPHYYTILDSGGIIVAIEHSSRPINVIKFSTDEGQCWQTYTFTRDPIYFTGLASEPGARSMNISIWGFTESFLTSQWVSYTIDFKDILERNCEEKDYTIWLAHSTDPEDYEDGCILGYKEQFLRLRKSSVCQNGRDYVVTKQPSICLCSLEDFLCDFGYYRPENDSKCVEQPELKGHDLEFCLYGREEHLTTNGYRKIPGDKCQGGVNPVREVKDLKKKCTSNFLSPEKQNSKSNSVPIILAIVGLMLVTVVAGVLIVKKYVCGGRFLVHRYSVLQQHAEANGVDGVDALDTASHTNKSGYHDDSDEDLLE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
98	N-linked_Glycosylation	DFVAKLANNTHQHVF HHHHHHHCCCCCHHH	65.45	UniProtKB CARBOHYD
98	N-linked_Glycosylation	DFVAKLANNTHQHVF HHHHHHHCCCCCHHH	65.45	19349973
99	N-linked_Glycosylation	FVAKLANNTHQHVFD HHHHHHCCCCCHHHH	33.07	19349973
99	N-linked_Glycosylation	FVAKLANNTHQHVFD HHHHHHCCCCCHHHH	33.07	19349973
112	Ubiquitination	FDDLRGSVSLSWVGD HHHCCCCEEEEEECC	8.11	29967540
152	Ubiquitination	YRSEDYGKNFKDITD CCCCCCCCCHHHHHH	53.64	-
160	Ubiquitination	NFKDITDLINNTFIR CHHHHHHHHHCCEEE	3.19	29967540
162	N-linked_Glycosylation	KDITDLINNTFIRTE HHHHHHHHCCEEEEC	49.11	16263699
162	N-linked_Glycosylation	KDITDLINNTFIRTE HHHHHHHHCCEEEEC	49.11	16263699
163	N-linked_Glycosylation	DITDLINNTFIRTEF HHHHHHHCCEEEECC	29.40	19349973
163	N-linked_Glycosylation	DITDLINNTFIRTEF HHHHHHHCCEEEECC	29.40	19349973
168	Phosphorylation	INNTFIRTEFGMAIG HHCCEEEECCCEEEC	30.74	20068231
179	Phosphorylation	MAIGPENSGKVVLTA EEECCCCCCEEEEEE	38.03	20068231
185	Phosphorylation	NSGKVVLTAEVSGGS CCCEEEEEEEECCCC	14.79	20068231
189	Phosphorylation	VVLTAEVSGGSRGGR EEEEEEECCCCCCCE	29.01	20068231
192	Phosphorylation	TAEVSGGSRGGRIFR EEEECCCCCCCEEEC	31.14	20068231
248	Ubiquitination	VSKNFGGKWEEIHKA EECCCCCCHHHHHHH	52.38	29967540
251	Ubiquitination	NFGGKWEEIHKAVCL CCCCCHHHHHHHHHH	49.64	27667366
252	Ubiquitination	FGGKWEEIHKAVCLA CCCCHHHHHHHHHHH	2.47	27667366
263	Phosphorylation	VCLAKWGSDNTIFFT HHHHHCCCCCEEEEE	26.94	-
274	N-linked_Glycosylation	IFFTTYANGSCKADL EEEEEECCCCEEECC	32.28	UniProtKB CARBOHYD
294	Ubiquitination	WRTSDLGKSFKTIGV HHHCCCCCCCCEEEE	61.08	29967540
295	Phosphorylation	RTSDLGKSFKTIGVK HHCCCCCCCCEEEEE	30.12	22210691
297	Ubiquitination	SDLGKSFKTIGVKIY CCCCCCCCEEEEEEE	46.45	29967540
298	Phosphorylation	DLGKSFKTIGVKIYS CCCCCCCEEEEEEEE	22.43	20068231
304	Phosphorylation	KTIGVKIYSFGLGGR CEEEEEEEEECCCCC	7.70	20068231
305	Phosphorylation	TIGVKIYSFGLGGRF EEEEEEEEECCCCCE	19.13	20068231
316	Phosphorylation	GGRFLFASVMADKDT CCCEEEEEEECCCCC	12.70	20068231
387	Ubiquitination	DDRGIVYSKSLDRHL CCCCEEEECCCCCEE	12.60	27667366
388	Ubiquitination	DRGIVYSKSLDRHLY CCCEEEECCCCCEEE	37.03	27667366
406	N-linked_Glycosylation	GGETDFTNVTSLRGV CCCCCCCCCCCCCEE	34.75	19122660
525	Phosphorylation	MLEGPHYYTILDSGG ECCCCEEEEEEECCC	5.58	24275569
530	Phosphorylation	HYYTILDSGGIIVAI EEEEEEECCCEEEEE	35.16	24275569
582	N-linked_Glycosylation	EPGARSMNISIWGFT CCCCCCCEEEEEEEC	26.54	19122660
681	Ubiquitination	LCDFGYYRPENDSKC HHHCCCCCCCCCCCC	24.46	21963094
682	Ubiquitination	CDFGYYRPENDSKCV HHCCCCCCCCCCCCC	28.73	21963094
684	N-linked_Glycosylation	FGYYRPENDSKCVEQ CCCCCCCCCCCCCCC	62.63	UniProtKB CARBOHYD
684	Phosphorylation	FGYYRPENDSKCVEQ CCCCCCCCCCCCCCC	62.63	32142685
688	Phosphorylation	RPENDSKCVEQPELK CCCCCCCCCCCCCCC	4.76	33259812
741	Phosphorylation	KDLKKKCTSNFLSPE HHHHHHHHHCCCCHH	35.27	30177828
742	Phosphorylation	DLKKKCTSNFLSPEK HHHHHHHHCCCCHHH	34.75	30177828
746	Phosphorylation	KCTSNFLSPEKQNSK HHHHCCCCHHHHCCC	27.20	30177828
783	S-palmitoylation	LIVKKYVCGGRFLVH HHHHHCEECCCHHHH	4.31	18817523
792	Phosphorylation	GRFLVHRYSVLQQHA CCHHHHHHHHHHHHH	6.56	26657352
793	Phosphorylation	RFLVHRYSVLQQHAE CHHHHHHHHHHHHHH	19.13	29255136
812	Phosphorylation	DGVDALDTASHTNKS CCCHHHHCCCCCCCC	30.80	30266825
814	Phosphorylation	VDALDTASHTNKSGY CHHHHCCCCCCCCCC	32.70	30266825
816	Phosphorylation	ALDTASHTNKSGYHD HHHCCCCCCCCCCCC	41.67	30266825
817	Ubiquitination	LDTASHTNKSGYHDD HHCCCCCCCCCCCCC	30.95	21963094
818	Ubiquitination	DTASHTNKSGYHDDS HCCCCCCCCCCCCCC	46.54	21963094
819	Phosphorylation	TASHTNKSGYHDDSD CCCCCCCCCCCCCCC	46.80	22167270
821	Phosphorylation	SHTNKSGYHDDSDED CCCCCCCCCCCCCHH	14.79	23927012
825	Phosphorylation	KSGYHDDSDEDLLE- CCCCCCCCCHHHCC-	49.29	22167270

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
793	S	Phosphorylation	Kinase	PAK2	Q13177	PSP
825	S	Phosphorylation	Kinase	CK2B	P67870	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
825	S	Phosphorylation		11390366
Phosphorylation at Ser-825 facilitates the interaction with GGA1.

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 SORT_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GGA2_HUMAN	GGA2	physical	11331584
NGF_HUMAN	NGF	physical	14985763
AMRP_HUMAN	LRPAP1	physical	9013611
GGA1_HUMAN	GGA1	physical	11821067
GGA2_HUMAN	GGA2	physical	11821067
GGA1_HUMAN	GGA1	physical	11390366
GGA2_HUMAN	GGA2	physical	11390366
GGA3_HUMAN	GGA3	physical	11390366
STAM1_HUMAN	STAM	physical	11390366
APBB2_HUMAN	APBB2	physical	26496610
XIAP_HUMAN	XIAP	physical	26496610
ASSY_HUMAN	ASS1	physical	26496610
BAD_HUMAN	BAD	physical	26496610
BLMH_HUMAN	BLMH	physical	26496610
CDK1_HUMAN	CDK1	physical	26496610
CDK2_HUMAN	CDK2	physical	26496610
COPA_HUMAN	COPA	physical	26496610
KC1G2_HUMAN	CSNK1G2	physical	26496610
CSPG4_HUMAN	CSPG4	physical	26496610
PHC2_HUMAN	PHC2	physical	26496610
EI2BA_HUMAN	EIF2B1	physical	26496610
GOGA3_HUMAN	GOLGA3	physical	26496610
HPT_HUMAN	HP	physical	26496610
DHB4_HUMAN	HSD17B4	physical	26496610
KLC1_HUMAN	KLC1	physical	26496610
M3K4_HUMAN	MAP3K4	physical	26496610
MYH1_HUMAN	MYH1	physical	26496610
MYH6_HUMAN	MYH6	physical	26496610
NDUB5_HUMAN	NDUFB5	physical	26496610
NHS_HUMAN	NHS	physical	26496610
NOP2_HUMAN	NOP2	physical	26496610
YBOX1_HUMAN	YBX1	physical	26496610
PLCB3_HUMAN	PLCB3	physical	26496610
PRCC_HUMAN	PRCC	physical	26496610
RAB13_HUMAN	RAB13	physical	26496610
RENT1_HUMAN	UPF1	physical	26496610
RET_HUMAN	RET	physical	26496610
SRSF2_HUMAN	SRSF2	physical	26496610
UAP1_HUMAN	UAP1	physical	26496610
SPTN2_HUMAN	SPTBN2	physical	26496610
SSRA_HUMAN	SSR1	physical	26496610
TCOF_HUMAN	TCOF1	physical	26496610
TEC_HUMAN	TEC	physical	26496610
ICAM5_HUMAN	ICAM5	physical	26496610
TLN1_HUMAN	TLN1	physical	26496610
UBP1_HUMAN	USP1	physical	26496610
XRCC2_HUMAN	XRCC2	physical	26496610
UBP11_HUMAN	USP11	physical	26496610
SYYC_HUMAN	YARS	physical	26496610
OASL_HUMAN	OASL	physical	26496610
K2C75_HUMAN	KRT75	physical	26496610
GT2D1_HUMAN	GTF2IRD1	physical	26496610
RHG32_HUMAN	ARHGAP32	physical	26496610
URB2_HUMAN	URB2	physical	26496610
C2CD5_HUMAN	C2CD5	physical	26496610
NPA1P_HUMAN	URB1	physical	26496610
UBP15_HUMAN	USP15	physical	26496610
MPH6_HUMAN	MPHOSPH6	physical	26496610
VPP3_HUMAN	TCIRG1	physical	26496610
ABCA7_HUMAN	ABCA7	physical	26496610
HNRPQ_HUMAN	SYNCRIP	physical	26496610
LTOR5_HUMAN	LAMTOR5	physical	26496610
WWP2_HUMAN	WWP2	physical	26496610
TARA_HUMAN	TRIOBP	physical	26496610
COBL1_HUMAN	COBLL1	physical	26496610
LMTK2_HUMAN	LMTK2	physical	26496610
FND3A_HUMAN	FNDC3A	physical	26496610
MORC2_HUMAN	MORC2	physical	26496610
RRP44_HUMAN	DIS3	physical	26496610
RRP1B_HUMAN	RRP1B	physical	26496610
FAF2_HUMAN	FAF2	physical	26496610
MD13L_HUMAN	MED13L	physical	26496610
DICER_HUMAN	DICER1	physical	26496610
SIR5_HUMAN	SIRT5	physical	26496610
KLDC2_HUMAN	KLHDC2	physical	26496610
RFIP5_HUMAN	RAB11FIP5	physical	26496610
LS14A_HUMAN	LSM14A	physical	26496610
TXD11_HUMAN	TXNDC11	physical	26496610
FXL19_HUMAN	FBXL19	physical	26496610
APTX_HUMAN	APTX	physical	26496610
PALMD_HUMAN	PALMD	physical	26496610
SSH3_HUMAN	SSH3	physical	26496610
UACA_HUMAN	UACA	physical	26496610
RBM28_HUMAN	RBM28	physical	26496610
BRX1_HUMAN	BRIX1	physical	26496610
UFSP2_HUMAN	UFSP2	physical	26496610
DNJA4_HUMAN	DNAJA4	physical	26496610
DDX60_HUMAN	DDX60	physical	26496610
IPO9_HUMAN	IPO9	physical	26496610
UGGG2_HUMAN	UGGT2	physical	26496610
BIN3_HUMAN	BIN3	physical	26496610
BI2L1_HUMAN	BAIAP2L1	physical	26496610
ZCCHV_HUMAN	ZC3HAV1	physical	26496610
P33MX_HUMAN	KIAA1191	physical	26496610
FANCM_HUMAN	FANCM	physical	26496610
PAPD5_HUMAN	PAPD5	physical	26496610
GPBP1_HUMAN	GPBP1	physical	26496610
NOL6_HUMAN	NOL6	physical	26496610
RM24_HUMAN	MRPL24	physical	26496610
ICE2_HUMAN	ICE2	physical	26496610
ZN768_HUMAN	ZNF768	physical	26496610
PEAK1_HUMAN	PEAK1	physical	26496610
MRM1_HUMAN	MRM1	physical	26496610
MUS81_HUMAN	MUS81	physical	26496610
SEN2_HUMAN	TSEN2	physical	26496610
MTMRD_HUMAN	SBF2	physical	26496610
PARP9_HUMAN	PARP9	physical	26496610
UTP15_HUMAN	UTP15	physical	26496610
UBP32_HUMAN	USP32	physical	26496610
TBA1C_HUMAN	TUBA1C	physical	26496610
SCMC2_HUMAN	SLC25A25	physical	26496610
RM55_HUMAN	MRPL55	physical	26496610
EME1_HUMAN	EME1	physical	26496610
CENPV_HUMAN	CENPV	physical	26496610
PDE12_HUMAN	PDE12	physical	26496610
TBB5_HUMAN	TUBB	physical	26496610
CB069_HUMAN	C2orf69	physical	26496610
LEMD2_HUMAN	LEMD2	physical	26496610
TMEM9_HUMAN	TMEM9	physical	26496610
CDRT4_HUMAN	CDRT4	physical	26496610
SPD2B_HUMAN	SH3PXD2B	physical	26496610
NSE2_HUMAN	NSMCE2	physical	26496610
DDX51_HUMAN	DDX51	physical	26496610
TGO1_HUMAN	MIA3	physical	26496610
BACE1_HUMAN	BACE1	physical	21245145

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 SORT_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Ligands bind to Sortilin in the tunnel of a ten-bladed beta-propellerdomain."; Quistgaard E.M., Madsen P., Groftehauge M.K., Nissen P.,Petersen C.M., Thirup S.S.; Nat. Struct. Mol. Biol. 16:96-98(2009). Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 78-756 IN COMPLEX WITH NTS,SUBUNIT, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-406 AND ASN-582.	19122660 [Abstract]
"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."; Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.; Nat. Biotechnol. 27:378-386(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-162 AND ASN-163, AND MASSSPECTROMETRY.	19349973 [Abstract]
"Elucidation of N-glycosylation sites on human platelet proteins: aglycoproteomic approach."; Lewandrowski U., Moebius J., Walter U., Sickmann A.; Mol. Cell. Proteomics 5:226-233(2006). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-162, AND MASSSPECTROMETRY.	16263699 [Abstract]
Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-825, AND MASSSPECTROMETRY.	19690332 [Abstract]
"Phosphoproteome of resting human platelets."; Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.; J. Proteome Res. 7:526-534(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-825, AND MASSSPECTROMETRY.	18088087 [Abstract]

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