dbPTM

MPRI_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MPRI_HUMAN
UniProt AC	P11717
Protein Name	Cation-independent mannose-6-phosphate receptor
Gene Name	IGF2R
Organism	Homo sapiens (Human).
Sequence Length	2491
Subcellular Localization	Lysosome membrane Single-pass type I membrane protein . Colocalized with DPP4 in internalized cytoplasmic vesicles adjacent to the cell surface.
Protein Description	Transport of phosphorylated lysosomal enzymes from the Golgi complex and the cell surface to lysosomes. Lysosomal enzymes bearing phosphomannosyl residues bind specifically to mannose-6-phosphate receptors in the Golgi apparatus and the resulting receptor-ligand complex is transported to an acidic prelyosomal compartment where the low pH mediates the dissociation of the complex. This receptor also binds IGF2. Acts as a positive regulator of T-cell coactivation, by binding DPP4..
Protein Sequence	MGAAAGRSPHLGPAPARRPQRSLLLLQLLLLVAAPGSTQAQAAPFPELCSYTWEAVDTKNNVLYKINICGSVDIVQCGPSSAVCMHDLKTRTYHSVGDSVLRSATRSLLEFNTTVSCDQQGTNHRVQSSIAFLCGKTLGTPEFVTATECVHYFEWRTTAACKKDIFKANKEVPCYVFDEELRKHDLNPLIKLSGAYLVDDSDPDTSLFINVCRDIDTLRDPGSQLRACPPGTAACLVRGHQAFDVGQPRDGLKLVRKDRLVLSYVREEAGKLDFCDGHSPAVTITFVCPSERREGTIPKLTAKSNCRYEIEWITEYACHRDYLESKTCSLSGEQQDVSIDLTPLAQSGGSSYISDGKEYLFYLNVCGETEIQFCNKKQAAVCQVKKSDTSQVKAAGRYHNQTLRYSDGDLTLIYFGGDECSSGFQRMSVINFECNKTAGNDGKGTPVFTGEVDCTYFFTWDTEYACVKEKEDLLCGATDGKKRYDLSALVRHAEPEQNWEAVDGSQTETEKKHFFINICHRVLQEGKARGCPEDAAVCAVDKNGSKNLGKFISSPMKEKGNIQLSYSDGDDCGHGKKIKTNITLVCKPGDLESAPVLRTSGEGGCFYEFEWHTAAACVLSKTEGENCTVFDSQAGFSFDLSPLTKKNGAYKVETKKYDFYINVCGPVSVSPCQPDSGACQVAKSDEKTWNLGLSNAKLSYYDGMIQLNYRGGTPYNNERHTPRATLITFLCDRDAGVGFPEYQEEDNSTYNFRWYTSYACPEEPLECVVTDPSTLEQYDLSSLAKSEGGLGGNWYAMDNSGEHVTWRKYYINVCRPLNPVPGCNRYASACQMKYEKDQGSFTEVVSISNLGMAKTGPVVEDSGSLLLEYVNGSACTTSDGRQTTYTTRIHLVCSRGRLNSHPIFSLNWECVVSFLWNTEAACPIQTTTDTDQACSIRDPNSGFVFNLNPLNSSQGYNVSGIGKIFMFNVCGTMPVCGTILGKPASGCEAETQTEELKNWKPARPVGIEKSLQLSTEGFITLTYKGPLSAKGTADAFIVRFVCNDDVYSGPLKFLHQDIDSGQGIRNTYFEFETALACVPSPVDCQVTDLAGNEYDLTGLSTVRKPWTAVDTSVDGRKRTFYLSVCNPLPYIPGCQGSAVGSCLVSEGNSWNLGVVQMSPQAAANGSLSIMYVNGDKCGNQRFSTRITFECAQISGSPAFQLQDGCEYVFIWRTVEACPVVRVEGDNCEVKDPRHGNLYDLKPLGLNDTIVSAGEYTYYFRVCGKLSSDVCPTSDKSKVVSSCQEKREPQGFHKVAGLLTQKLTYENGLLKMNFTGGDTCHKVYQRSTAIFFYCDRGTQRPVFLKETSDCSYLFEWRTQYACPPFDLTECSFKDGAGNSFDLSSLSRYSDNWEAITGTGDPEHYLINVCKSLAPQAGTEPCPPEAAACLLGGSKPVNLGRVRDGPQWRDGIIVLKYVDGDLCPDGIRKKSTTIRFTCSESQVNSRPMFISAVEDCEYTFAWPTATACPMKSNEHDDCQVTNPSTGHLFDLSSLSGRAGFTAAYSEKGLVYMSICGENENCPPGVGACFGQTRISVGKANKRLRYVDQVLQLVYKDGSPCPSKSGLSYKSVISFVCRPEARPTNRPMLISLDKQTCTLFFSWHTPLACEQATECSVRNGSSIVDLSPLIHRTGGYEAYDESEDDASDTNPDFYINICQPLNPMHGVPCPAGAAVCKVPIDGPPIDIGRVAGPPILNPIANEIYLNFESSTPCLADKHFNYTSLIAFHCKRGVSMGTPKLLRTSECDFVFEWETPVVCPDEVRMDGCTLTDEQLLYSFNLSSLSTSTFKVTRDSRTYSVGVCTFAVGPEQGGCKDGGVCLLSGTKGASFGRLQSMKLDYRHQDEAVVLSYVNGDRCPPETDDGVPCVFPFIFNGKSYEECIIESRAKLWCSTTADYDRDHEWGFCRHSNSYRTSSIIFKCDEDEDIGRPQVFSEVRGCDVTFEWKTKVVCPPKKLECKFVQKHKTYDLRLLSSLTGSWSLVHNGVSYYINLCQKIYKGPLGCSERASICRRTTTGDVQVLGLVHTQKLGVIGDKVVVTYSKGYPCGGNKTASSVIELTCTKTVGRPAFKRFDIDSCTYYFSWDSRAACAVKPQEVQMVNGTITNPINGKSFSLGDIYFKLFRASGDMRTNGDNYLYEIQLSSITSSRNPACSGANICQVKPNDQHFSRKVGTSDKTKYYLQDGDLDVVFASSSKCGKDKTKSVSSTIFFHCDPLVEDGIPEFSHETADCQYLFSWYTSAVCPLGVGFDSENPGDDGQMHKGLSERSQAVGAVLSLLLVALTCCLLALLLYKKERRETVISKLTTCCRRSSNVSYKYSKVNKEEETDENETEWLMEEIQLPPPRQGKEGQENGHITTKSVKALSSLHGDDQDSEDEVLTIPEVKVHSGRGAGAESSHPVRNAQSNALQEREDDRVGLVRGEKARKGKSSSAQQKTVSSTKLVSFHDDSDEDLLHI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
7	Methylation	-MGAAAGRSPHLGPA -CCCCCCCCCCCCCC	42.14	115384239
89	Ubiquitination	AVCMHDLKTRTYHSV EEECCCCCCCCCCCC	41.86	-
92	Phosphorylation	MHDLKTRTYHSVGDS CCCCCCCCCCCCCHH	30.71	28152594
93	Phosphorylation	HDLKTRTYHSVGDSV CCCCCCCCCCCCHHH	6.71	28152594
112	N-linked_Glycosylation	TRSLLEFNTTVSCDQ HHHHHEECCEEEECC	26.01	12754519
134	Glutathionylation	QSSIAFLCGKTLGTP HHHHHHHHCCCCCCC	4.19	22555962
140	Phosphorylation	LCGKTLGTPEFVTAT HHCCCCCCCCEEEHH	23.82	26853621
170	Ubiquitination	KDIFKANKEVPCYVF HHHHHCCCCCCEEEC	66.02	29967540
174	Glutathionylation	KANKEVPCYVFDEEL HCCCCCCEEECCHHH	5.67	22555962
183	Ubiquitination	VFDEELRKHDLNPLI ECCHHHHHCCCCHHH	54.84	29967540
253	Ubiquitination	GQPRDGLKLVRKDRL CCCCCCCEEEECCHH	50.93	-
296	Phosphorylation	PSERREGTIPKLTAK CCCCCCCCCCCCCCC	29.38	21406692
301	Phosphorylation	EGTIPKLTAKSNCRY CCCCCCCCCCCCCCE	37.86	-
390	Phosphorylation	QVKKSDTSQVKAAGR EECCCCCHHHHHCCC	37.66	25599653
400	N-linked_Glycosylation	KAAGRYHNQTLRYSD HHCCCCCCEEEEECC	27.83	UniProtKB CARBOHYD
411	Phosphorylation	RYSDGDLTLIYFGGD EECCCCEEEEEECCC	18.82	22210691
420	Glutathionylation	IYFGGDECSSGFQRM EEECCCCCCCCCEEC	4.70	22555962
422	Phosphorylation	FGGDECSSGFQRMSV ECCCCCCCCCEECEE	56.11	22210691
428	Phosphorylation	SSGFQRMSVINFECN CCCCEECEEEEEEEC	23.26	22210691
435	N-linked_Glycosylation	SVINFECNKTAGNDG EEEEEEECCCCCCCC	37.20	UniProtKB CARBOHYD
481	2-Hydroxyisobutyrylation	LCGATDGKKRYDLSA ECCCCCCCCEECHHH	36.57	-
481	Ubiquitination	LCGATDGKKRYDLSA ECCCCCCCCEECHHH	36.57	-
482	Ubiquitination	CGATDGKKRYDLSAL CCCCCCCCEECHHHH	62.82	-
487	Phosphorylation	GKKRYDLSALVRHAE CCCEECHHHHHHCCC	19.36	20068231
507	Phosphorylation	EAVDGSQTETEKKHF EECCCCCCHHHHHHH	46.72	-
511	Ubiquitination	GSQTETEKKHFFINI CCCCHHHHHHHHHHH	59.99	-
512	Ubiquitination	SQTETEKKHFFINIC CCCHHHHHHHHHHHH	39.14	-
543	N-linked_Glycosylation	AVCAVDKNGSKNLGK CEEEECCCCCCCHHH	56.35	UniProtKB CARBOHYD
546	Ubiquitination	AVDKNGSKNLGKFIS EECCCCCCCHHHHCC	58.55	-
557	Ubiquitination	KFISSPMKEKGNIQL HHCCCCCCCCCCEEE	60.71	-
572	Glutathionylation	SYSDGDDCGHGKKIK EECCCCCCCCCCEEE	5.29	22555962
581	N-linked_Glycosylation	HGKKIKTNITLVCKP CCCEEECCEEEEECC	21.90	12754519
626	N-linked_Glycosylation	LSKTEGENCTVFDSQ HHCCCCCCCEEEECC	37.30	19159218
684	Phosphorylation	GACQVAKSDEKTWNL CCCEECCCCCCCEEE	41.06	26074081
687	Ubiquitination	QVAKSDEKTWNLGLS EECCCCCCCEEECCC	64.92	-
688	Phosphorylation	VAKSDEKTWNLGLSN ECCCCCCCEEECCCC	19.96	26074081
694	Phosphorylation	KTWNLGLSNAKLSYY CCEEECCCCCEEEEE	32.70	26074081
699	Phosphorylation	GLSNAKLSYYDGMIQ CCCCCEEEEECCEEE	22.42	26074081
700	Phosphorylation	LSNAKLSYYDGMIQL CCCCEEEEECCEEEE	18.93	26074081
701	Phosphorylation	SNAKLSYYDGMIQLN CCCEEEEECCEEEEE	11.57	26074081
709	Phosphorylation	DGMIQLNYRGGTPYN CCEEEEEECCCCCCC	21.16	26074081
710	Methylation	GMIQLNYRGGTPYNN CEEEEEECCCCCCCC	35.67	115480217
747	N-linked_Glycosylation	PEYQEEDNSTYNFRW CCCCCCCCCEEEEEE	39.26	12754519
770	O-linked_Glycosylation	EPLECVVTDPSTLEQ CCEEEEEECHHHHHH	23.07	OGP
808	Ubiquitination	GEHVTWRKYYINVCR CCCCEEEEEEEEEEC	33.69	-
833	Ubiquitination	YASACQMKYEKDQGS HHHHHCCEEECCCCC	25.12	-
871	N-linked_Glycosylation	SLLLEYVNGSACTTS CEEEEEECCCCCCCC	37.49	UniProtKB CARBOHYD
951	N-linked_Glycosylation	VFNLNPLNSSQGYNV EEECCCCCCCCCCCC	40.65	UniProtKB CARBOHYD
956	Phosphorylation	PLNSSQGYNVSGIGK CCCCCCCCCCCCCCE	12.54	26657352
957	N-linked_Glycosylation	LNSSQGYNVSGIGKI CCCCCCCCCCCCCEE	28.44	19349973
957	N-linked_Glycosylation	LNSSQGYNVSGIGKI CCCCCCCCCCCCCEE	28.44	19349973
1028	Phosphorylation	LTYKGPLSAKGTADA EEEECCCCCCCCCCE	30.94	28787133
1042	Glutathionylation	AFIVRFVCNDDVYSG EEEEEEEECCCCCCC	4.20	22555962
1052	Ubiquitination	DVYSGPLKFLHQDID CCCCCCEEEEEEECC	49.35	-
1067	Phosphorylation	SGQGIRNTYFEFETA CCCCHHHCEEEEEEE	21.53	23401153
1068	Phosphorylation	GQGIRNTYFEFETAL CCCHHHCEEEEEEEE	12.50	23401153
1073	Phosphorylation	NTYFEFETALACVPS HCEEEEEEEEECCCC	32.09	23401153
1080	Phosphorylation	TALACVPSPVDCQVT EEEECCCCCCCEEEE	19.70	23401153
1087	Phosphorylation	SPVDCQVTDLAGNEY CCCCEEEEECCCCEE	10.22	23401153
1104	Ubiquitination	TGLSTVRKPWTAVDT CCCCCCCCCEEEEEE	40.34	29967540
1107	O-linked_Glycosylation	STVRKPWTAVDTSVD CCCCCCEEEEEECCC	25.90	OGP
1107	Phosphorylation	STVRKPWTAVDTSVD CCCCCCEEEEEECCC	25.90	20068231
1111	Phosphorylation	KPWTAVDTSVDGRKR CCEEEEEECCCCCEE	24.85	20068231
1112	Phosphorylation	PWTAVDTSVDGRKRT CEEEEEECCCCCEEE	17.47	20068231
1164	N-linked_Glycosylation	MSPQAAANGSLSIMY ECHHHHHCCCEEEEE	35.54	UniProtKB CARBOHYD
1230	Ubiquitination	EGDNCEVKDPRHGNL ECCCCEECCCCCCCC	39.46	-
1246	N-linked_Glycosylation	DLKPLGLNDTIVSAG CCCCCCCCCEEEECC	42.45	12754519
1264	Ubiquitination	YYFRVCGKLSSDVCP EEEEECCCCCCCCCC	39.82	-
1272	Phosphorylation	LSSDVCPTSDKSKVV CCCCCCCCCCHHHHH	44.42	-
1277	Sumoylation	CPTSDKSKVVSSCQE CCCCCHHHHHHHHHH	53.01	-
1277	Sumoylation	CPTSDKSKVVSSCQE CCCCCHHHHHHHHHH	53.01	-
1280	Phosphorylation	SDKSKVVSSCQEKRE CCHHHHHHHHHHHCC	28.52	-
1281	Phosphorylation	DKSKVVSSCQEKREP CHHHHHHHHHHHCCC	14.28	-
1293	Ubiquitination	REPQGFHKVAGLLTQ CCCCCHHHHHHHHHC	31.36	29967540
1301	Ubiquitination	VAGLLTQKLTYENGL HHHHHHCEEEECCCE	37.25	-
1304	Phosphorylation	LLTQKLTYENGLLKM HHHCEEEECCCEEEE	20.17	24260401
1312	N-linked_Glycosylation	ENGLLKMNFTGGDTC CCCEEEEEECCCCHH	29.73	UniProtKB CARBOHYD
1327	Phosphorylation	HKVYQRSTAIFFYCD HHHEECCEEEEEEEC	26.43	25599653
1346	Phosphorylation	RPVFLKETSDCSYLF CCEEEEECCCCCEEE	28.42	-
1347	Phosphorylation	PVFLKETSDCSYLFE CEEEEECCCCCEEEE	37.40	-
1349	Glutathionylation	FLKETSDCSYLFEWR EEEECCCCCEEEEEC	2.63	22555962
1359	Phosphorylation	LFEWRTQYACPPFDL EEEECCCCCCCCCCC	15.01	30576142
1378	Phosphorylation	FKDGAGNSFDLSSLS ECCCCCCCCCHHHHH	21.15	23403867
1382	Phosphorylation	AGNSFDLSSLSRYSD CCCCCCHHHHHCCCC	30.95	23403867
1383	Phosphorylation	GNSFDLSSLSRYSDN CCCCCHHHHHCCCCC	37.35	30576142
1408	Glutathionylation	EHYLINVCKSLAPQA HHHHHHHHHHHCCCC	1.83	22555962
1592	Phosphorylation	DQVLQLVYKDGSPCP HHHHHHHCCCCCCCC	16.38	-
1601	Ubiquitination	DGSPCPSKSGLSYKS CCCCCCCCCCCCHHH	33.41	29967540
1656	N-linked_Glycosylation	ATECSVRNGSSIVDL CHHCCCCCCCCEEEC	53.17	UniProtKB CARBOHYD
1757	N-linked_Glycosylation	CLADKHFNYTSLIAF CCCCCCCCCHHHEEH	38.60	UniProtKB CARBOHYD
1771	Phosphorylation	FHCKRGVSMGTPKLL HHHCCCCCCCCCCCC	17.83	22468782
1774	Phosphorylation	KRGVSMGTPKLLRTS CCCCCCCCCCCCCCC	14.49	22210691
1776	Ubiquitination	GVSMGTPKLLRTSEC CCCCCCCCCCCCCCC	61.05	-
1816	N-linked_Glycosylation	EQLLYSFNLSSLSTS HHHHHEEECCCCCCC	32.83	UniProtKB CARBOHYD
1828	Phosphorylation	STSTFKVTRDSRTYS CCCEEEEECCCCEEE	29.37	20068231
1831	Phosphorylation	TFKVTRDSRTYSVGV EEEEECCCCEEEEEE	24.19	20068231
1862	Ubiquitination	VCLLSGTKGASFGRL EEEEECCCCCCHHHC	56.88	29967540
1865	Phosphorylation	LSGTKGASFGRLQSM EECCCCCCHHHCEEC	36.58	-
1871	Phosphorylation	ASFGRLQSMKLDYRH CCHHHCEECCCCCCC	23.60	-
1873	Ubiquitination	FGRLQSMKLDYRHQD HHHCEECCCCCCCCC	43.37	-
1970	Phosphorylation	IGRPQVFSEVRGCDV CCCCCHHHHHCCCCE	36.00	24719451
2002	Phosphorylation	KFVQKHKTYDLRLLS EEEECCCCCCHHHHH	23.22	-
2024	Phosphorylation	LVHNGVSYYINLCQK EEECCHHHHHHCHHH	13.12	-
2025	Phosphorylation	VHNGVSYYINLCQKI EECCHHHHHHCHHHH	3.94	-
2040	Phosphorylation	YKGPLGCSERASICR HCCCCCCCCCHHHCC	28.46	23403867
2085	N-linked_Glycosylation	KGYPCGGNKTASSVI CCCCCCCCCCCCCEE	24.64	UniProtKB CARBOHYD
2087	Phosphorylation	YPCGGNKTASSVIEL CCCCCCCCCCCEEEE	35.45	20068231
2089	Phosphorylation	CGGNKTASSVIELTC CCCCCCCCCEEEEEE	30.30	20068231
2090	Phosphorylation	GGNKTASSVIELTCT CCCCCCCCEEEEEEE	25.34	20068231
2095	Phosphorylation	ASSVIELTCTKTVGR CCCEEEEEEECCCCC	12.82	20068231
2097	Phosphorylation	SVIELTCTKTVGRPA CEEEEEEECCCCCCC	25.23	20068231
2136	N-linked_Glycosylation	PQEVQMVNGTITNPI CCEEEEECCEEECCC	36.23	UniProtKB CARBOHYD
2154	Phosphorylation	SFSLGDIYFKLFRAS EEEHHHHHHHEEEEC	10.21	-
2189	Phosphorylation	SSRNPACSGANICQV CCCCCCCCCCCEEEC	42.94	-
2209	Phosphorylation	HFSRKVGTSDKTKYY CCCCCCCCCCCCEEE	36.42	-
2210	Phosphorylation	FSRKVGTSDKTKYYL CCCCCCCCCCCEEEC	31.05	-
2338	Ubiquitination	RRETVISKLTTCCRR HHHHHHHHHHHHHHH	38.43	-
2340	Phosphorylation	ETVISKLTTCCRRSS HHHHHHHHHHHHHCC	22.86	23882029
2341	Phosphorylation	TVISKLTTCCRRSSN HHHHHHHHHHHHCCC	21.75	23882029
2342	S-palmitoylation	VISKLTTCCRRSSNV HHHHHHHHHHHCCCC	1.11	29575903
2343	S-palmitoylation	ISKLTTCCRRSSNVS HHHHHHHHHHCCCCC	3.68	29575903
2346	Phosphorylation	LTTCCRRSSNVSYKY HHHHHHHCCCCCEEE	13.60	30576142
2347	Phosphorylation	TTCCRRSSNVSYKYS HHHHHHCCCCCEEEE	39.17	27273156
2350	Phosphorylation	CRRSSNVSYKYSKVN HHHCCCCCEEEEECC	21.84	30576142
2351	Phosphorylation	RRSSNVSYKYSKVNK HHCCCCCEEEEECCC	15.06	29514088
2352	Acetylation	RSSNVSYKYSKVNKE HCCCCCEEEEECCCH	35.23	19608861
2352	Ubiquitination	RSSNVSYKYSKVNKE HCCCCCEEEEECCCH	35.23	23000965
2353	Phosphorylation	SSNVSYKYSKVNKEE CCCCCEEEEECCCHH	12.90	23186163
2354	Phosphorylation	SNVSYKYSKVNKEEE CCCCEEEEECCCHHC	26.44	30576142
2355	Ubiquitination	NVSYKYSKVNKEEET CCCEEEEECCCHHCC	46.89	23000965
2358	Ubiquitination	YKYSKVNKEEETDEN EEEEECCCHHCCCCC	70.28	23000965
2362	Phosphorylation	KVNKEEETDENETEW ECCCHHCCCCCHHHH	52.47	30266825
2367	Phosphorylation	EETDENETEWLMEEI HCCCCCHHHHHHHHC	44.00	30266825
2383	Ubiquitination	LPPPRQGKEGQENGH CCCCCCCCCCCCCCC	50.78	23000965
2392	Phosphorylation	GQENGHITTKSVKAL CCCCCCCCHHHHHHH	23.61	26074081
2393	Phosphorylation	QENGHITTKSVKALS CCCCCCCHHHHHHHH	22.25	26074081
2394	Acetylation	ENGHITTKSVKALSS CCCCCCHHHHHHHHH	44.60	25953088
2394	Ubiquitination	ENGHITTKSVKALSS CCCCCCHHHHHHHHH	44.60	23000965
2395	Phosphorylation	NGHITTKSVKALSSL CCCCCHHHHHHHHHC	27.10	28464451
2397	Ubiquitination	HITTKSVKALSSLHG CCCHHHHHHHHHCCC	51.18	23000965
2400	Phosphorylation	TKSVKALSSLHGDDQ HHHHHHHHHCCCCCC	35.40	22167270
2401	Phosphorylation	KSVKALSSLHGDDQD HHHHHHHHCCCCCCC	25.82	22167270
2409	Phosphorylation	LHGDDQDSEDEVLTI CCCCCCCCCCCEEEC	41.12	19664994
2415	Phosphorylation	DSEDEVLTIPEVKVH CCCCCEEECCEEEEE	39.39	30266825
2420	Ubiquitination	VLTIPEVKVHSGRGA EEECCEEEEECCCCC	32.35	29967540
2423	Phosphorylation	IPEVKVHSGRGAGAE CCEEEEECCCCCCCC	32.92	28555341
2425	Methylation	EVKVHSGRGAGAESS EEEEECCCCCCCCCC	34.50	58857975
2440	Phosphorylation	HPVRNAQSNALQERE CHHCCHHHHHHHHCC	22.97	30576142
2470	Ubiquitination	KSSSAQQKTVSSTKL CCCCCCCCCCCCCEE	38.52	29967540
2476	Acetylation	QKTVSSTKLVSFHDD CCCCCCCEEEEECCC	49.17	25953088
2476	Ubiquitination	QKTVSSTKLVSFHDD CCCCCCCEEEEECCC	49.17	29967540
2479	Phosphorylation	VSSTKLVSFHDDSDE CCCCEEEEECCCCCC	27.57	22167270
2484	Phosphorylation	LVSFHDDSDEDLLHI EEEECCCCCCCCCCC	49.29	19664994

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
2409	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
2484	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CREG1_HUMAN	CREG1	physical	12934103
PLIN3_HUMAN	PLIN3	physical	9590177
PLIN3_HUMAN	PLIN3	physical	10908666
GGA3_HUMAN	GGA3	physical	16135791
GGA3_HUMAN	GGA3	physical	12032548
GGA1_HUMAN	GGA1	physical	14567678
GGA2_HUMAN	GGA2	physical	14567678
GGA3_HUMAN	GGA3	physical	14567678
GGA1_HUMAN	GGA1	physical	12060753
GGA3_HUMAN	GGA3	physical	12060753
GGA1_HUMAN	GGA1	physical	11390366
GGA2_HUMAN	GGA2	physical	11390366
GGA3_HUMAN	GGA3	physical	11390366
GGA3_HUMAN	GGA3	physical	11859375
GGA1_HUMAN	GGA1	physical	11859375
GGA2_HUMAN	GGA2	physical	11859375
TM9S4_HUMAN	TM9SF4	physical	22939629
SERC1_HUMAN	SERINC1	physical	22939629
T10B_HUMAN	TIMM10B	physical	22939629

Drug and Disease Associations

Kegg Disease
H00048	Hepatocellular carcinoma
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 MPRI_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-2352, AND MASS SPECTROMETRY.	19608861 [Abstract]
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-626 AND ASN-747, AND MASSSPECTROMETRY.	19159218 [Abstract]
"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-112; ASN-581; ASN-747 AND ASN-1246.	12754519 [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-2401; SER-2409; SER-2479AND SER-2484, AND MASS SPECTROMETRY.	19690332 [Abstract]
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2409 AND SER-2484, ANDMASS SPECTROMETRY.	19369195 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2401 AND SER-2409, ANDMASS SPECTROMETRY.	19413330 [Abstract]
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography."; Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.; Proteomics 8:1346-1361(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2484, AND MASSSPECTROMETRY.	18318008 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2409; SER-2479 ANDSER-2484, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2409 AND SER-2484, ANDMASS SPECTROMETRY.	18691976 [Abstract]
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment."; Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.; J. Proteome Res. 7:5167-5176(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2484, AND MASSSPECTROMETRY.	19367720 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2484, AND MASSSPECTROMETRY.	18220336 [Abstract]
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2484, AND MASSSPECTROMETRY.	18187866 [Abstract]
"Quantitative phosphoproteome profiling of Wnt3a-mediated signalingnetwork: indicating the involvement of ribonucleoside-diphosphatereductase M2 subunit phosphorylation at residue serine 20 in canonicalWnt signal transduction."; Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.; Mol. Cell. Proteomics 6:1952-1967(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2484, AND MASSSPECTROMETRY.	17693683 [Abstract]
"Toward a global characterization of the phosphoproteome in prostatecancer cells: identification of phosphoproteins in the LNCaP cellline."; Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.; Electrophoresis 28:2027-2034(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2484, AND MASSSPECTROMETRY.	17487921 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2409; SER-2479 ANDSER-2484, AND MASS SPECTROMETRY.	17081983 [Abstract]