dbPTM

SORL_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SORL_HUMAN
UniProt AC	Q92673
Protein Name	Sortilin-related receptor
Gene Name	SORL1
Organism	Homo sapiens (Human).
Sequence Length	2214
Subcellular Localization	Membrane Single-pass type I membrane protein . Golgi apparatus. Endosome. Secreted.
Protein Description	Likely to be a multifunctional endocytic receptor, that may be implicated in the uptake of lipoproteins and of proteases. Binds LDL, the major cholesterol-carrying lipoprotein of plasma, and transports it into cells by endocytosis. Binds the receptor-associated protein (RAP). Could play a role in cell-cell interaction. Involved in APP trafficking to and from the Golgi apparatus. It probably acts as a sorting receptor that protects APP from trafficking to late endosome and from processing into amyloid beta, thereby reducing the burden of amyloidogenic peptide formation. Involved in the regulation of smooth muscle cells migration, probably through PLAUR binding and decreased internalization..
Protein Sequence	MATRSSRRESRLPFLFTLVALLPPGALCEVWTQRLHGGSAPLPQDRGFLVVQGDPRELRLWARGDARGASRADEKPLRRKRSAALQPEPIKVYGQVSLNDSHNQMVVHWAGEKSNVIVALARDSLALARPKSSDVYVSYDYGKSFKKISDKLNFGLGNRSEAVIAQFYHSPADNKRYIFADAYAQYLWITFDFCNTLQGFSIPFRAADLLLHSKASNLLLGFDRSHPNKQLWKSDDFGQTWIMIQEHVKSFSWGIDPYDKPNTIYIERHEPSGYSTVFRSTDFFQSRENQEVILEEVRDFQLRDKYMFATKVVHLLGSEQQSSVQLWVSFGRKPMRAAQFVTRHPINEYYIADASEDQVFVCVSHSNNRTNLYISEAEGLKFSLSLENVLYYSPGGAGSDTLVRYFANEPFADFHRVEGLQGVYIATLINGSMNEENMRSVITFDKGGTWEFLQAPAFTGYGEKINCELSQGCSLHLAQRLSQLLNLQLRRMPILSKESAPGLIIATGSVGKNLASKTNVYISSSAGARWREALPGPHYYTWGDHGGIITAIAQGMETNELKYSTNEGETWKTFIFSEKPVFVYGLLTEPGEKSTVFTIFGSNKENVHSWLILQVNATDALGVPCTENDYKLWSPSDERGNECLLGHKTVFKRRTPHATCFNGEDFDRPVVVSNCSCTREDYECDFGFKMSEDLSLEVCVPDPEFSGKSYSPPVPCPVGSTYRRTRGYRKISGDTCSGGDVEARLEGELVPCPLAEENEFILYAVRKSIYRYDLASGATEQLPLTGLRAAVALDFDYEHNCLYWSDLALDVIQRLCLNGSTGQEVIINSGLETVEALAFEPLSQLLYWVDAGFKKIEVANPDGDFRLTIVNSSVLDRPRALVLVPQEGVMFWTDWGDLKPGIYRSNMDGSAAYHLVSEDVKWPNGISVDDQWIYWTDAYLECIERITFSGQQRSVILDNLPHPYAIAVFKNEIYWDDWSQLSIFRASKYSGSQMEILANQLTGLMDMKIFYKGKNTGSNACVPRPCSLLCLPKANNSRSCRCPEDVSSSVLPSGDLMCDCPQGYQLKNNTCVKQENTCLRNQYRCSNGNCINSIWWCDFDNDCGDMSDERNCPTTICDLDTQFRCQESGTCIPLSYKCDLEDDCGDNSDESHCEMHQCRSDEYNCSSGMCIRSSWVCDGDNDCRDWSDEANCTAIYHTCEASNFQCRNGHCIPQRWACDGDTDCQDGSDEDPVNCEKKCNGFRCPNGTCIPSSKHCDGLRDCSDGSDEQHCEPLCTHFMDFVCKNRQQCLFHSMVCDGIIQCRDGSDEDAAFAGCSQDPEFHKVCDEFGFQCQNGVCISLIWKCDGMDDCGDYSDEANCENPTEAPNCSRYFQFRCENGHCIPNRWKCDRENDCGDWSDEKDCGDSHILPFSTPGPSTCLPNYYRCSSGTCVMDTWVCDGYRDCADGSDEEACPLLANVTAASTPTQLGRCDRFEFECHQPKTCIPNWKRCDGHQDCQDGRDEANCPTHSTLTCMSREFQCEDGEACIVLSERCDGFLDCSDESDEKACSDELTVYKVQNLQWTADFSGDVTLTWMRPKKMPSASCVYNVYYRVVGESIWKTLETHSNKTNTVLKVLKPDTTYQVKVQVQCLSKAHNTNDFVTLRTPEGLPDAPRNLQLSLPREAEGVIVGHWAPPIHTHGLIREYIVEYSRSGSKMWASQRAASNFTEIKNLLVNTLYTVRVAAVTSRGIGNWSDSKSITTIKGKVIPPPDIHIDSYGENYLSFTLTMESDIKVNGYVVNLFWAFDTHKQERRTLNFRGSILSHKVGNLTAHTSYEISAWAKTDLGDSPLAFEHVMTRGVRPPAPSLKAKAINQTAVECTWTGPRNVVYGIFYATSFLDLYRNPKSLTTSLHNKTVIVSKDEQYLFLVRVVVPYQGPSSDYVVVKMIPDSRLPPRHLHVVHTGKTSVVIKWESPYDSPDQDLLYAVAVKDLIRKTDRSYKVKSRNSTVEYTLNKLEPGGKYHIIVQLGNMSKDSSIKITTVSLSAPDALKIITENDHVLLFWKSLALKEKHFNESRGYEIHMFDSAMNITAYLGNTTDNFFKISNLKMGHNYTFTVQARCLFGNQICGEPAILLYDELGSGADASATQAARSTDVAAVVVPILFLILLSLGVGFAILYTKHRRLQSSFTAFANSHYSSRLGSAIFSSGDDLGEDDEDAPMITGFSDDVPMVIA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
82	Phosphorylation	KPLRRKRSAALQPEP CCCCCCCCCCCCCCC	22.41	28355574
99	N-linked_Glycosylation	VYGQVSLNDSHNQMV EEEEEEECCCCCCEE	41.03	19159218
114	Phosphorylation	VHWAGEKSNVIVALA EEECCCCCCEEEEEE	31.84	20068231
124	Phosphorylation	IVALARDSLALARPK EEEEEECHHHHCCCC	15.25	24719451
136	Phosphorylation	RPKSSDVYVSYDYGK CCCCCCEEEEECCCH	6.67	22817900
139	Phosphorylation	SSDVYVSYDYGKSFK CCCEEEEECCCHHHH	11.79	22817900
149	Phosphorylation	GKSFKKISDKLNFGL CHHHHHHHHHHCCCC	37.26	23312004
158	N-linked_Glycosylation	KLNFGLGNRSEAVIA HHCCCCCCCCHHHHH	49.72	UniProtKB CARBOHYD
229	Ubiquitination	FDRSHPNKQLWKSDD CCCCCCCCCCEECCC	51.74	-
260	Ubiquitination	WGIDPYDKPNTIYIE CCCCCCCCCCEEEEE	34.03	-
276	Phosphorylation	HEPSGYSTVFRSTDF CCCCCCCEEEECCCC	18.38	24719451
305	Ubiquitination	RDFQLRDKYMFATKV HHHHCHHHHHHHHHH	31.98	-
318	Phosphorylation	KVVHLLGSEQQSSVQ HHHHHHCCCCCCCEE	32.00	20068231
322	Phosphorylation	LLGSEQQSSVQLWVS HHCCCCCCCEEEEEE	31.97	20068231
323	Phosphorylation	LGSEQQSSVQLWVSF HCCCCCCCEEEEEEE	15.00	20068231
329	Phosphorylation	SSVQLWVSFGRKPMR CCEEEEEEECCCCCH	15.48	20068231
368	N-linked_Glycosylation	VCVSHSNNRTNLYIS EEEECCCCCEEEEEE	55.99	UniProtKB CARBOHYD
375	Phosphorylation	NRTNLYISEAEGLKF CCEEEEEEECCCCCE	19.73	-
385	Phosphorylation	EGLKFSLSLENVLYY CCCCEEEEEECEEEE	32.22	-
430	N-linked_Glycosylation	VYIATLINGSMNEEN EEEEEEECCCCCCCC	39.33	UniProtKB CARBOHYD
446	Ubiquitination	RSVITFDKGGTWEFL CEEEEECCCCCEEEE	55.86	-
499	Phosphorylation	MPILSKESAPGLIIA CCCCCCCCCCCEEEE	43.42	-
595	Phosphorylation	TEPGEKSTVFTIFGS CCCCCCCEEEEEECC	30.61	21060948
598	Phosphorylation	GEKSTVFTIFGSNKE CCCCEEEEEECCCCC	15.85	21060948
616	N-linked_Glycosylation	SWLILQVNATDALGV EEEEEEECCCCCCCC	24.94	UniProtKB CARBOHYD
648	Ubiquitination	NECLLGHKTVFKRRT CCCCCCCCCEECCCC	44.58	-
674	N-linked_Glycosylation	DRPVVVSNCSCTRED CCCEEEEECCCCCCC	15.31	UniProtKB CARBOHYD
710	Phosphorylation	PEFSGKSYSPPVPCP CCCCCCCCCCCCCCC	28.78	30576142
711	Phosphorylation	EFSGKSYSPPVPCPV CCCCCCCCCCCCCCC	29.80	30576142
722	Phosphorylation	PCPVGSTYRRTRGYR CCCCCCCCCCCCCEE	10.37	30576142
730	Ubiquitination	RRTRGYRKISGDTCS CCCCCEEEECCCCCC	32.51	-
732	Phosphorylation	TRGYRKISGDTCSGG CCCEEEECCCCCCCC	33.38	23403867
735	Phosphorylation	YRKISGDTCSGGDVE EEEECCCCCCCCCCE	16.46	23403867
737	Phosphorylation	KISGDTCSGGDVEAR EECCCCCCCCCCEEE	48.15	23403867
779	Phosphorylation	YDLASGATEQLPLTG EECCCCCCCCCCCCC	27.99	24667141
785	Phosphorylation	ATEQLPLTGLRAAVA CCCCCCCCCHHHEEE	32.03	24667141
818	N-linked_Glycosylation	VIQRLCLNGSTGQEV HHHHHHHCCCCCCEE	41.18	UniProtKB CARBOHYD
871	N-linked_Glycosylation	DFRLTIVNSSVLDRP CEEEEEECCCCCCCC	25.39	UniProtKB CARBOHYD
988	Ubiquitination	LSIFRASKYSGSQME HHHHHHHCCCCHHHH	42.31	-
1035	N-linked_Glycosylation	LLCLPKANNSRSCRC EEEEECCCCCCCCCC	53.81	UniProtKB CARBOHYD
1068	N-linked_Glycosylation	PQGYQLKNNTCVKQE CCCEECCCCCEECCC	58.60	UniProtKB CARBOHYD
1164	N-linked_Glycosylation	QCRSDEYNCSSGMCI HCCCCCCCCCCCCEE	19.69	UniProtKB CARBOHYD
1173	Phosphorylation	SSGMCIRSSWVCDGD CCCCEEEEEEEECCC	14.51	21406692
1174	Phosphorylation	SGMCIRSSWVCDGDN CCCEEEEEEEECCCC	17.43	21406692
1187	Phosphorylation	DNDCRDWSDEANCTA CCCCCCCCCCCCEEE	29.84	21406692
1191	N-linked_Glycosylation	RDWSDEANCTAIYHT CCCCCCCCEEEEEEE	22.94	UniProtKB CARBOHYD
1193	Phosphorylation	WSDEANCTAIYHTCE CCCCCCEEEEEEEEH	18.85	21406692
1196	Phosphorylation	EANCTAIYHTCEASN CCCEEEEEEEEHHHC	6.65	21406692
1198	O-linked_Glycosylation	NCTAIYHTCEASNFQ CEEEEEEEEHHHCCC	8.62	OGP
1198	Phosphorylation	NCTAIYHTCEASNFQ CEEEEEEEEHHHCCC	8.62	21406692
1202	Phosphorylation	IYHTCEASNFQCRNG EEEEEHHHCCCCCCC	18.84	21406692
1246	N-linked_Glycosylation	CNGFRCPNGTCIPSS CCCEECCCCCCCCCC	63.13	UniProtKB CARBOHYD
1367	N-linked_Glycosylation	ENPTEAPNCSRYFQF CCCCCCCCCCCEEEE	43.36	UniProtKB CARBOHYD
1412	O-linked_Glycosylation	DSHILPFSTPGPSTC CCCEECCCCCCCCCC	31.58	OGP
1413	O-linked_Glycosylation	SHILPFSTPGPSTCL CCEECCCCCCCCCCC	32.42	OGP
1418	O-linked_Glycosylation	FSTPGPSTCLPNYYR CCCCCCCCCCCCCEE	22.61	OGP
1458	N-linked_Glycosylation	EACPLLANVTAASTP CHHHHHHHEEECCCC	31.48	UniProtKB CARBOHYD
1460	O-linked_Glycosylation	CPLLANVTAASTPTQ HHHHHHEEECCCCCC	19.13	OGP
1463	O-linked_Glycosylation	LANVTAASTPTQLGR HHHEEECCCCCCCCC	32.24	OGP
1464	O-linked_Glycosylation	ANVTAASTPTQLGRC HHEEECCCCCCCCCC	26.15	OGP
1489	Ubiquitination	KTCIPNWKRCDGHQD CCCCCCCCCCCCCCC	50.19	-
1508	O-linked_Glycosylation	RDEANCPTHSTLTCM CCCCCCCCCHHHEEE	30.56	55825653
1580	Ubiquitination	LTWMRPKKMPSASCV EEEECCCCCCCCCCE	59.74	-
1583	Phosphorylation	MRPKKMPSASCVYNV ECCCCCCCCCCEEEE	29.34	28851738
1585	Phosphorylation	PKKMPSASCVYNVYY CCCCCCCCCEEEEHH	14.41	28851738
1588	Phosphorylation	MPSASCVYNVYYRVV CCCCCCEEEEHHHHH	11.84	25850435
1591	Phosphorylation	ASCVYNVYYRVVGES CCCEEEEHHHHHCHH	5.06	25850435
1592	Phosphorylation	SCVYNVYYRVVGESI CCEEEEHHHHHCHHH	7.83	25850435
1605	Phosphorylation	SIWKTLETHSNKTNT HHHHHHHHCCCCCCE	33.44	26074081
1607	Phosphorylation	WKTLETHSNKTNTVL HHHHHHCCCCCCEEE	47.65	26074081
1608	N-linked_Glycosylation	KTLETHSNKTNTVLK HHHHHCCCCCCEEEE	47.79	UniProtKB CARBOHYD
1609	Ubiquitination	TLETHSNKTNTVLKV HHHHCCCCCCEEEEE	46.28	-
1610	Phosphorylation	LETHSNKTNTVLKVL HHHCCCCCCEEEEEE	40.13	26074081
1612	Phosphorylation	THSNKTNTVLKVLKP HCCCCCCEEEEEECC	32.23	26074081
1621	Phosphorylation	LKVLKPDTTYQVKVQ EEEECCCCEEEEEEE	35.61	26074081
1622	Phosphorylation	KVLKPDTTYQVKVQV EEECCCCEEEEEEEE	21.24	26074081
1623	Phosphorylation	VLKPDTTYQVKVQVQ EECCCCEEEEEEEEE	17.25	26074081
1634	Ubiquitination	VQVQCLSKAHNTNDF EEEEEECCCCCCCCC	40.49	-
1660	Phosphorylation	APRNLQLSLPREAEG CCCCEEECCCCCCCC	24.30	24719451
1706	N-linked_Glycosylation	ASQRAASNFTEIKNL HHHHHHCCCHHHHHH	43.03	UniProtKB CARBOHYD
1719	Phosphorylation	NLLVNTLYTVRVAAV HHHHHCCHHEEEEEE	10.93	-
1733	N-linked_Glycosylation	VTSRGIGNWSDSKSI EECCCCCCCCCCCCC	32.91	19159218
1735	Phosphorylation	SRGIGNWSDSKSITT CCCCCCCCCCCCCEE	35.69	24043423
1737	Phosphorylation	GIGNWSDSKSITTIK CCCCCCCCCCCEEEC	23.84	24043423
1788	Phosphorylation	NLFWAFDTHKQERRT EEEEEECCCCCCCCC	25.23	22210691
1795	Phosphorylation	THKQERRTLNFRGSI CCCCCCCCEEECCHH	32.07	22210691
1809	N-linked_Glycosylation	ILSHKVGNLTAHTSY HHHEECCCEEEECEE	36.89	UniProtKB CARBOHYD
1811	Phosphorylation	SHKVGNLTAHTSYEI HEECCCEEEECEEEE	22.01	-
1824	Phosphorylation	EISAWAKTDLGDSPL EEEEEECCCCCCCCC	28.80	-
1854	N-linked_Glycosylation	SLKAKAINQTAVECT CHHHCEECCEEEEEE	37.70	UniProtKB CARBOHYD
1874	Phosphorylation	NVVYGIFYATSFLDL HHEEEEEEEHHHHHH	13.67	19835603
1876	Phosphorylation	VYGIFYATSFLDLYR EEEEEEEHHHHHHHC	14.50	-
1894	N-linked_Glycosylation	SLTTSLHNKTVIVSK HHCCEECCCEEEEEC	47.16	UniProtKB CARBOHYD
1976	Phosphorylation	VKDLIRKTDRSYKVK HHHHHHHCCCCCEEE	27.14	24275569
1980	Phosphorylation	IRKTDRSYKVKSRNS HHHCCCCCEEECCCC	22.24	24275569
1984	Phosphorylation	DRSYKVKSRNSTVEY CCCCEEECCCCEEEE	39.42	24275569
1986	N-linked_Glycosylation	SYKVKSRNSTVEYTL CCEEECCCCEEEEEE	49.47	UniProtKB CARBOHYD
1987	Phosphorylation	YKVKSRNSTVEYTLN CEEECCCCEEEEEEC	32.49	24275569
2002	Phosphorylation	KLEPGGKYHIIVQLG CCCCCCEEEEEEEEC	11.09	-
2010	N-linked_Glycosylation	HIIVQLGNMSKDSSI EEEEEECCCCCCCCC	39.90	19159218
2054	N-linked_Glycosylation	ALKEKHFNESRGYEI HHHHHHCCCCCCCEE	46.16	UniProtKB CARBOHYD
2069	N-linked_Glycosylation	HMFDSAMNITAYLGN EEECCCCCEEEECCC	28.33	UniProtKB CARBOHYD
2076	N-linked_Glycosylation	NITAYLGNTTDNFFK CEEEECCCCCCCEEE	36.89	19159218
2092	N-linked_Glycosylation	SNLKMGHNYTFTVQA CCCCCCCCEEEEEEE	31.63	19159218
2159	Phosphorylation	GVGFAILYTKHRRLQ CHHHHHHHHHHHHHH	13.97	-
2160	Phosphorylation	VGFAILYTKHRRLQS HHHHHHHHHHHHHHH	19.54	-
2167	Phosphorylation	TKHRRLQSSFTAFAN HHHHHHHHHHHHHHC	31.82	-
2175	Phosphorylation	SFTAFANSHYSSRLG HHHHHHCCHHHHCCC	22.00	28857561
2178	Phosphorylation	AFANSHYSSRLGSAI HHHCCHHHHCCCCEE	11.98	28857561
2179	Phosphorylation	FANSHYSSRLGSAIF HHCCHHHHCCCCEEE	25.10	28857561
2183	Phosphorylation	HYSSRLGSAIFSSGD HHHHCCCCEEECCCC	23.84	25954137
2206	Phosphorylation	APMITGFSDDVPMVI CCCCCCCCCCCCEEC	33.96	18407551

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
2206	S	Phosphorylation	Kinase	ROCK2	O75116	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
2206	S	Phosphorylation		21147781
Phosphorylation at Ser-2206 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 SORL_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GGA1_HUMAN	GGA1	physical	11821067
GGA2_HUMAN	GGA2	physical	11821067
A4_HUMAN	APP	physical	17855360
GGA1_HUMAN	GGA1	physical	17855360

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
104300	Alzheimer disease (AD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of SORL_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"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-99; ASN-1733; ASN-2010;ASN-2076 AND ASN-2092, AND MASS SPECTROMETRY.	19159218 [Abstract]
Phosphorylation
Reference	PubMed
"Rho kinase II phosphorylation of the lipoprotein receptor LR11/SORLAalters amyloid-beta production."; Herskowitz J.H., Seyfried N.T., Gearing M., Kahn R.A., Peng J.,Levey A.I., Lah J.J.; J. Biol. Chem. 286:6117-6127(2011). Cited for: PHOSPHORYLATION AT SER-2206, AND INTERACTION WITH ROCK2.	21147781 [Abstract]

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