ANR50_HUMAN - dbPTM
ANR50_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ANR50_HUMAN
UniProt AC Q9ULJ7
Protein Name Ankyrin repeat domain-containing protein 50
Gene Name ANKRD50
Organism Homo sapiens (Human).
Sequence Length 1429
Subcellular Localization Endosome .
Protein Description Involved in the endosome-to-plasma membrane trafficking and recycling of SNX27-retromer-dependent cargo proteins, such as GLUT1. [PubMed: 25278552]
Protein Sequence MTNPWEEKVCKMAQTSLLQGKQFYCREWVFHKLQHCLQEKSNCCNSAVNAPSLVMNSGNNASGVSGKGAAWGVLLVGGPGSGKTALCTELLWPSSPASLQRGLHRQALAFHFCKAQDSDTLCVGGFIRGLVAQICRSGLLQGYEDKLRDPAVQSLLQPGECERNPAEAFKRCVLLPLLGMKPPQQSLYLLVDSVDEGCNITEGEQTSTSLSGTVAALLAGHHEFFPPWLLLLCSARKQSKAVTKMFTGFRKISLDDLRKAYIVKDVQQYILHRLDQEEALRQHLTKETAEMLNQLHIKSSGCFLYLERVLDGVVENFIMLREIRDIPGTLNGLYLWLCQRLFVRKQFAKVQPILNVILAACRPLTITELYHAVWTKNMSLTLEDFQRKLDILSKLLVDGLGNTKILFHYSFAEWLLDVKHCTQKYLCNAAEGHRMLAMSYTCQAKNLTPLEAQEFALHLINSNLQLETAELALWMIWNGTPVRDSLSTLIPKEQEVLQLLVKAGAHVNSEDDRTSCIVRQALEREDSIRTLLDNGASVNQCDSNGRTLLANAAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTLAARQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGHTEVVSALLYAGVKVDCADADSRTALRAAAWGGHEDIVLNLLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLLDHGAEVNHEDVDGRTALSVAALCVPASKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIPFILASQEGHYDCVQILLENKSNIDQRGYDGRNALRVAALEGHRDIVELLFSHGADVNCKDADGRPTLYILALENQLTMAEYFLENGANVEASDAEGRTALHVSCWQGHMEMVQVLIAYHADVNAADNEKRSALQSAAWQGHVKVVQLLIEHGAVVDHTCNQGATALCIAAQEGHIDVVQVLLEHGADPNHADQFGRTAMRVAAKNGHSQIIKLLEKYGASSLNGCSPSPVHTMEQKPLQSLSSKVQSLTIKSNSSGSTGGGDMQPSLRGLPNGPTHAFSSPSESPDSTVDRQKSSLSNNSLKSSKNSSLRTTSSTATAQTVPIDSFHNLSFTEQIQQHSLPRSRSRQSIVSPSSTTQSLGQSHNSPSSEFEWSQVKPSLKSTKASKGGKSENSAKSGSAGKKAKQSNSSQPKVLEYEMTQFDRRGPIAKSGTAAPPKQMPAESQCKIMIPSAQQEIGRSQQQFLIHQQSGEQKKRNGIMTNPNYHLQSNQVFLGRVSVPRTMQDRGHQEVLEGYPSSETELSLKQALKLQIEGSDPSFNYKKETPL
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 Orthologous
Protein Cluster
2Phosphorylation------MTNPWEEKV
------CCCHHHHHH
62.3829255136
15PhosphorylationKVCKMAQTSLLQGKQ
HHHHHHHHHHHCCCH
16.2924719451
32MalonylationCREWVFHKLQHCLQE
HHHHHHHHHHHHHHH
38.0832601280
251UbiquitinationKMFTGFRKISLDDLR
HHHHCCEECCHHHHH
34.09-
251MalonylationKMFTGFRKISLDDLR
HHHHCCEECCHHHHH
34.0926320211
253PhosphorylationFTGFRKISLDDLRKA
HHCCEECCHHHHHHH
28.8725850435
288PhosphorylationRQHLTKETAEMLNQL
HHHCCHHHHHHHHHH
29.4923532336
365PhosphorylationLAACRPLTITELYHA
HHHHCCCCHHHHHHH
28.6524117733
367PhosphorylationACRPLTITELYHAVW
HHCCCCHHHHHHHHH
18.0724117733
370PhosphorylationPLTITELYHAVWTKN
CCCHHHHHHHHHCCC
4.9824117733
375PhosphorylationELYHAVWTKNMSLTL
HHHHHHHCCCCCCCH
13.1224117733
378SulfoxidationHAVWTKNMSLTLEDF
HHHHCCCCCCCHHHH
3.5621406390
379PhosphorylationAVWTKNMSLTLEDFQ
HHHCCCCCCCHHHHH
27.8224117733
381PhosphorylationWTKNMSLTLEDFQRK
HCCCCCCCHHHHHHH
22.3146164357
388UbiquitinationTLEDFQRKLDILSKL
CHHHHHHHHHHHHHH
39.46-
388MalonylationTLEDFQRKLDILSKL
CHHHHHHHHHHHHHH
39.4626320211
393PhosphorylationQRKLDILSKLLVDGL
HHHHHHHHHHHHCCC
22.9121815630
514PhosphorylationVNSEDDRTSCIVRQA
CCCCCHHHHHHHHHH
34.64113334339
515PhosphorylationNSEDDRTSCIVRQAL
CCCCHHHHHHHHHHH
11.6228555341
527PhosphorylationQALEREDSIRTLLDN
HHHHCCCHHHHHHHC
14.8225849741
566PhosphorylationDVVNLLVSRGADLEI
HHHHHHHHCCCCCEE
25.6024719451
580PhosphorylationIEDAHGHTPLTLAAR
EECCCCCCCEEHHHH
25.2846164361
729PhosphorylationPASKGHASVVSLLID
CCCCCCHHHHHHHEE
19.8520873877
732PhosphorylationKGHASVVSLLIDRGA
CCCHHHHHHHEECCC
18.4620873877
942AcetylationHGADVNCKDADGRPT
CCCCCCCCCCCCCCE
51.237308189
986PhosphorylationGRTALHVSCWQGHME
CCCEEEEEEHHHHHH
10.0119651622
1091PhosphorylationVAAKNGHSQIIKLLE
HHHHHCHHHHHHHHH
25.1946164341
1095UbiquitinationNGHSQIIKLLEKYGA
HCHHHHHHHHHHHCC
48.96-
1100PhosphorylationIIKLLEKYGASSLNG
HHHHHHHHCCCCCCC
14.4625002506
1103PhosphorylationLLEKYGASSLNGCSP
HHHHHCCCCCCCCCC
30.8729214152
1104PhosphorylationLEKYGASSLNGCSPS
HHHHCCCCCCCCCCC
25.8925002506
1109PhosphorylationASSLNGCSPSPVHTM
CCCCCCCCCCCCCCC
29.7922199227
1111PhosphorylationSLNGCSPSPVHTMEQ
CCCCCCCCCCCCCCC
24.2225159151
1113PhosphorylationNGCSPSPVHTMEQKP
CCCCCCCCCCCCCCC
7.4318669648
1115PhosphorylationCSPSPVHTMEQKPLQ
CCCCCCCCCCCCCHH
23.7222199227
1116PhosphorylationSPSPVHTMEQKPLQS
CCCCCCCCCCCCHHH
2.8718669648
1119UbiquitinationPVHTMEQKPLQSLSS
CCCCCCCCCHHHHHH
34.10-
1123PhosphorylationMEQKPLQSLSSKVQS
CCCCCHHHHHHHCEE
37.5925002506
1127UbiquitinationPLQSLSSKVQSLTIK
CHHHHHHHCEEEEEE
40.70-
1130PhosphorylationSLSSKVQSLTIKSNS
HHHHHCEEEEEECCC
30.3924719451
1132PhosphorylationSSKVQSLTIKSNSSG
HHHCEEEEEECCCCC
31.4423909892
1135PhosphorylationVQSLTIKSNSSGSTG
CEEEEEECCCCCCCC
37.7922777824
1137PhosphorylationSLTIKSNSSGSTGGG
EEEEECCCCCCCCCC
43.0725849741
1138PhosphorylationLTIKSNSSGSTGGGD
EEEECCCCCCCCCCC
40.8025159151
1140PhosphorylationIKSNSSGSTGGGDMQ
EECCCCCCCCCCCCC
26.3125159151
1141PhosphorylationKSNSSGSTGGGDMQP
ECCCCCCCCCCCCCC
43.2928985074
1146SulfoxidationGSTGGGDMQPSLRGL
CCCCCCCCCCHHCCC
7.7421406390
1149PhosphorylationGGGDMQPSLRGLPNG
CCCCCCCHHCCCCCC
17.5130177828
1158PhosphorylationRGLPNGPTHAFSSPS
CCCCCCCCCCCCCCC
27.5125159151
1162PhosphorylationNGPTHAFSSPSESPD
CCCCCCCCCCCCCCC
41.9730266825
1163PhosphorylationGPTHAFSSPSESPDS
CCCCCCCCCCCCCCC
26.4530266825
1165PhosphorylationTHAFSSPSESPDSTV
CCCCCCCCCCCCCHH
53.2930266825
1167PhosphorylationAFSSPSESPDSTVDR
CCCCCCCCCCCHHHH
38.0430266825
1168PhosphorylationFSSPSESPDSTVDRQ
CCCCCCCCCCHHHHH
35.2018220336
1170PhosphorylationSPSESPDSTVDRQKS
CCCCCCCCHHHHHHH
33.4430266825
1171PhosphorylationPSESPDSTVDRQKSS
CCCCCCCHHHHHHHH
33.5330266825
1177PhosphorylationSTVDRQKSSLSNNSL
CHHHHHHHHCCCCCC
28.3327732954
1178PhosphorylationTVDRQKSSLSNNSLK
HHHHHHHHCCCCCCC
42.7423403867
1180PhosphorylationDRQKSSLSNNSLKSS
HHHHHHCCCCCCCCC
35.5925159151
1183PhosphorylationKSSLSNNSLKSSKNS
HHHCCCCCCCCCCCC
41.2325159151
1186PhosphorylationLSNNSLKSSKNSSLR
CCCCCCCCCCCCCCC
52.4125849741
1187PhosphorylationSNNSLKSSKNSSLRT
CCCCCCCCCCCCCCC
33.9827732954
1194PhosphorylationSKNSSLRTTSSTATA
CCCCCCCCCCCCCCC
36.0023927012
1195PhosphorylationKNSSLRTTSSTATAQ
CCCCCCCCCCCCCCE
17.7823927012
1196PhosphorylationNSSLRTTSSTATAQT
CCCCCCCCCCCCCEE
25.6923927012
1197PhosphorylationSSLRTTSSTATAQTV
CCCCCCCCCCCCEEE
21.7023927012
1198PhosphorylationSLRTTSSTATAQTVP
CCCCCCCCCCCEEEC
28.0023927012
1200PhosphorylationRTTSSTATAQTVPID
CCCCCCCCCEEECCC
21.2723927012
1203PhosphorylationSSTATAQTVPIDSFH
CCCCCCEEECCCCCC
26.2828348404
1208PhosphorylationAQTVPIDSFHNLSFT
CEEECCCCCCCCCHH
29.1763711767
1213PhosphorylationIDSFHNLSFTEQIQQ
CCCCCCCCHHHHHHH
35.1225159151
1215PhosphorylationSFHNLSFTEQIQQHS
CCCCCCHHHHHHHCC
24.4930576142
1222PhosphorylationTEQIQQHSLPRSRSR
HHHHHHCCCCCCCCC
35.4123927012
1226PhosphorylationQQHSLPRSRSRQSIV
HHCCCCCCCCCCCCC
32.4429449344
1228PhosphorylationHSLPRSRSRQSIVSP
CCCCCCCCCCCCCCC
35.6025849741
1231PhosphorylationPRSRSRQSIVSPSST
CCCCCCCCCCCCCHH
24.6925849741
1234PhosphorylationRSRQSIVSPSSTTQS
CCCCCCCCCCHHHHC
19.8625159151
1236PhosphorylationRQSIVSPSSTTQSLG
CCCCCCCCHHHHCCC
32.5825627689
1237PhosphorylationQSIVSPSSTTQSLGQ
CCCCCCCHHHHCCCC
38.5728348404
1238PhosphorylationSIVSPSSTTQSLGQS
CCCCCCHHHHCCCCC
32.9428348404
1239PhosphorylationIVSPSSTTQSLGQSH
CCCCCHHHHCCCCCC
20.3622210691
1241PhosphorylationSPSSTTQSLGQSHNS
CCCHHHHCCCCCCCC
32.1628348404
1245PhosphorylationTTQSLGQSHNSPSSE
HHHCCCCCCCCCCCC
23.8825159151
1248PhosphorylationSLGQSHNSPSSEFEW
CCCCCCCCCCCCCCH
22.2725849741
1250PhosphorylationGQSHNSPSSEFEWSQ
CCCCCCCCCCCCHHH
42.1728348404
1251PhosphorylationQSHNSPSSEFEWSQV
CCCCCCCCCCCHHHC
50.0828348404
1256PhosphorylationPSSEFEWSQVKPSLK
CCCCCCHHHCCHHHH
20.2129449344
1261PhosphorylationEWSQVKPSLKSTKAS
CHHHCCHHHHCCCCC
42.5981442427
1269TrimethylationLKSTKASKGGKSENS
HHCCCCCCCCCCCCC
76.24-
1269MethylationLKSTKASKGGKSENS
HHCCCCCCCCCCCCC
76.24-
1273PhosphorylationKASKGGKSENSAKSG
CCCCCCCCCCCCCCC
45.3368720971
1276PhosphorylationKGGKSENSAKSGSAG
CCCCCCCCCCCCCHH
32.7868720977
1278TrimethylationGKSENSAKSGSAGKK
CCCCCCCCCCCHHHH
55.99-
1278MethylationGKSENSAKSGSAGKK
CCCCCCCCCCCHHHH
55.99-
1279PhosphorylationKSENSAKSGSAGKKA
CCCCCCCCCCHHHHH
37.3868720983
1281PhosphorylationENSAKSGSAGKKAKQ
CCCCCCCCHHHHHCC
40.7224365823
1284TrimethylationAKSGSAGKKAKQSNS
CCCCCHHHHHCCCCC
49.64-
1284MethylationAKSGSAGKKAKQSNS
CCCCCHHHHHCCCCC
49.64-
1289PhosphorylationAGKKAKQSNSSQPKV
HHHHHCCCCCCCCCE
37.6630576142
1292PhosphorylationKAKQSNSSQPKVLEY
HHCCCCCCCCCEEEE
55.5430576142
1299PhosphorylationSQPKVLEYEMTQFDR
CCCCEEEEEECCCCC
13.5721945579
1302PhosphorylationKVLEYEMTQFDRRGP
CEEEEEECCCCCCCC
17.7227251275
1352PhosphorylationQFLIHQQSGEQKKRN
HHHHHHCCCCHHHHC
37.4129457462
1367PhosphorylationGIMTNPNYHLQSNQV
CCCCCCCCCCCCCCE
12.7430835499
1397PhosphorylationHQEVLEGYPSSETEL
CHHHHCCCCCCHHHC
7.2023186163
1399PhosphorylationEVLEGYPSSETELSL
HHHCCCCCCHHHCCH
32.1123403867
1400PhosphorylationVLEGYPSSETELSLK
HHCCCCCCHHHCCHH
43.9925849741
1402PhosphorylationEGYPSSETELSLKQA
CCCCCCHHHCCHHHH
44.1423403867
1405PhosphorylationPSSETELSLKQALKL
CCCHHHCCHHHHHHH
27.5623403867
1417PhosphorylationLKLQIEGSDPSFNYK
HHHHCCCCCCCCCCC
33.29113334331

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
-KUbiquitinationE3 ubiquitin ligaseSMURF1Q9HCE7
PMID:22199232

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ANR50_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 ANR50_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049

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 ANR50_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-1222, AND MASSSPECTROMETRY.

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