ANK1_HUMAN - dbPTM
ANK1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ANK1_HUMAN
UniProt AC P16157
Protein Name Ankyrin-1
Gene Name ANK1
Organism Homo sapiens (Human).
Sequence Length 1881
Subcellular Localization Isoform Er1: Cytoplasm, cytoskeleton. Probably the other erythrocyte (Er) isoforms, are located near the surface of erythrocytic plasma membrane.
Isoform Mu17: Membrane. Cytoplasm, myofibril, sarcomere, M line. Colocalizes with OBSCN isoform 3/
Protein Description Attaches integral membrane proteins to cytoskeletal elements; binds to the erythrocyte membrane protein band 4.2, to Na-K ATPase, to the lymphocyte membrane protein GP85, and to the cytoskeletal proteins fodrin, tubulin, vimentin and desmin. Erythrocyte ankyrins also link spectrin (beta chain) to the cytoplasmic domain of the erythrocytes anion exchange protein; they retain most or all of these binding functions.; Isoform Mu17 together with obscurin in skeletal muscle may provide a molecular link between the sarcoplasmic reticulum and myofibrils..
Protein Sequence MPYSVGFREADAATSFLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLINYGTKGKVRLPALHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLLDRGAQIETKTKDELTPLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLLQYDAEIDDITLDHLTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHVRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKAKVNAKAKDDQTPLHCAARIGHTNMVKLLLENNANPNLATTAGHTPLHIAAREGHVETVLALLEKEASQACMTKKGFTPLHVAAKYGKVRVAELLLERDAHPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQVEVARSLLQYGGSANAESVQGVTPLHLAAQEGHAEMVALLLSKQANGNLGNKSGLTPLHLVAQEGHVPVADVLIKHGVMVDATTRMGYTPLHVASHYGNIKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASPNEVSSDGTTPLAIAKRLGYISVTDVLKVVTDETSFVLVSDKHRMSFPETVDEILDVSEDEGEELISFKAERRDSRDVDEEKELLDFVPKLDQVVESPAIPRIPCAMPETVVIRSEEQEQASKEYDEDSLIPSSPATETSDNISPVASPVHTGFLVSFMVDARGGSMRGSRHNGLRVVIPPRTCAAPTRITCRLVKPQKLSTPPPLAEEEGLASRIIALGPTGAQFLSPVIVEIPHFASHGRGDRELVVLRSENGSVWKEHRSRYGESYLDQILNGMDEELGSLEELEKKRVCRIITTDFPLYFVIMSRLCQDYDTIGPEGGSLKSKLVPLVQATFPENAVTKRVKLALQAQPVPDELVTKLLGNQATFSPIVTVEPRRRKFHRPIGLRIPLPPSWTDNPRDSGEGDTTSLRLLCSVIGGTDQAQWEDITGTTKLVYANECANFTTNVSARFWLSDCPRTAEAVNFATLLYKELTAVPYMAKFVIFAKMNDPREGRLRCYCMTDDKVDKTLEQHENFVEVARSRDIEVLEGMSLFAELSGNLVPVKKAAQQRSFHFQSFRENRLAMPVKVRDSSREPGGSLSFLRKAMKYEDTQHILCHLNITMPPCAKGSGAEDRRRTPTPLALRYSILSESTPGSLSGTEQAEMKMAVISEHLGLSWAELARELQFSVEDINRIRVENPNSLLEQSVALLNLWVIREGQNANMENLYTALQSIDRGEIVNMLEGSGRQSRNLKPDRRHTDRDYSLSPSQMNGYSSLQDELLSPASLGCALSSPLRADQYWNEVAVLDAIPLAATEHDTMLEMSDMQVWSAGLTPSLVTAEDSSLECSKAEDSDATGHEWKLEGALSEEPRGPELGSLELVEDDTVDSDATNGLIDLLEQEEGQRSEEKLPGSKRQDDATGAGQDSENEVSLVSGHQRGQARITHSPTVSQVTERSQDRLQDWDADGSIVSYLQDAAQGSWQEEVTQGPHSFQGTSTMTEGLEPGGSQEYEKVLVSVSEHTWTEQPEAESSQADRDRRQQGQEEQVQEAKNTFTQVVQGNEFQNIPGEQVTEEQFTDEQGNIVTKKIIRKVVRQIDLSSADAAQEHEEVTVEGPLEDPSELEVDIDYFMKHSKDHTSTPNP
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
3Phosphorylation-----MPYSVGFREA
-----CCCCCCCCHH
28.0423917254
4Phosphorylation----MPYSVGFREAD
----CCCCCCCCHHH
26.8723025827
14PhosphorylationFREADAATSFLRAAR
CCHHHHHHHHHHHHH
23.0229970186
15PhosphorylationREADAATSFLRAARS
CHHHHHHHHHHHHHH
19.9823025827
41 (in isoform 21)Acetylation-4.22-
42 (in isoform 21)Acetylation-35.99-
55 (in isoform 17)Phosphorylation-52.6226437602
55 (in isoform 18)Phosphorylation-52.6226437602
55 (in isoform 19)Phosphorylation-52.6226437602
55 (in isoform 22)Phosphorylation-52.6226437602
55 (in isoform 23)Phosphorylation-52.6226437602
59UbiquitinationASKEGHVKMVVELLH
CCCCCCHHHHHHHHH
21.94-
100PhosphorylationVVRELVNYGANVNAQ
HHHHHHHCCCCCCCC
15.3318083107
105HydroxylationVNYGANVNAQSQKGF
HHCCCCCCCCCCCCC
31.8821177872
114 (in isoform 17)Phosphorylation-21.1626437602
208PhosphorylationVLSKTGFTPLHIAAH
HHHHCCCCCHHHHHH
26.7030835369
216PhosphorylationPLHIAAHYENLNVAQ
CHHHHHHHCCCCHHH
11.2017360941
231PhosphorylationLLLNRGASVNFTPQN
HHHHCCCCCCCCCCC
22.0318669648
233HydroxylationLNRGASVNFTPQNGI
HHCCCCCCCCCCCCC
32.3621177872
235PhosphorylationRGASVNFTPQNGITP
CCCCCCCCCCCCCCC
20.8228857561
241PhosphorylationFTPQNGITPLHIASR
CCCCCCCCCEEEEEC
22.6124719451
247PhosphorylationITPLHIASRRGNVIM
CCCEEEEECCCCEEE
23.1624719451
288O-linked_GlycosylationRNGHVRISEILLDHG
HCCCEEHHHHEECCC
14.1830379171
366PhosphorylationDKGAKPNSRALNGFT
CCCCCCCCCCCCCCC
27.7010529531
380AcetylationTPLHIACKKNHVRVM
CCHHHHHCCCCHHHH
47.8130586893
429PhosphorylationNLLQRGASPNVSNVK
HHHHCCCCCCCCCCE
21.6021082442
431HydroxylationLQRGASPNVSNVKVE
HHCCCCCCCCCCEEC
47.5621177872
433PhosphorylationRGASPNVSNVKVETP
CCCCCCCCCCEECCH
42.4129691806
436UbiquitinationSPNVSNVKVETPLHM
CCCCCCCEECCHHHH
38.31-
439PhosphorylationVSNVKVETPLHMAAR
CCCCEECCHHHHHHH
33.8523186163
454UbiquitinationAGHTEVAKYLLQNKA
CCCHHHHHHHHHCCC
41.42-
464HydroxylationLQNKAKVNAKAKDDQ
HHCCCHHCCCCCCCC
34.7121177872
500PhosphorylationNANPNLATTAGHTPL
CCCCCCCCCCCCCCC
21.9869102133
534UbiquitinationASQACMTKKGFTPLH
HHHHHHCCCCCCHHH
24.82-
546PhosphorylationPLHVAAKYGKVRVAE
HHHHHHHHCCHHHHH
19.9080514409
594PhosphorylationLLLPRGGSPHSPAWN
HHCCCCCCCCCCCCC
23.4328857561
597PhosphorylationPRGGSPHSPAWNGYT
CCCCCCCCCCCCCCC
21.5023025827
603PhosphorylationHSPAWNGYTPLHIAA
CCCCCCCCCHHHHHH
11.2825884760
604PhosphorylationSPAWNGYTPLHIAAK
CCCCCCCCHHHHHHH
22.2969103035
624PhosphorylationVARSLLQYGGSANAE
HHHHHHHHCCCCCHH
24.3546163277
629HydroxylationLQYGGSANAESVQGV
HHHCCCCCHHHCCCC
46.0321177872
662HydroxylationLSKQANGNLGNKSGL
HHHHHCCCCCCCCCC
44.5821177872
695HydroxylationIKHGVMVDATTRMGY
EECCCEEECCCCCCC
21.8021177872
702PhosphorylationDATTRMGYTPLHVAS
ECCCCCCCCCHHHHH
8.8846163283
703PhosphorylationATTRMGYTPLHVASH
CCCCCCCCCHHHHHH
17.4046163271
711PhosphorylationPLHVASHYGNIKLVK
CHHHHHHHCCHHHHH
14.9046163289
728HydroxylationLQHQADVNAKTKLGY
HHHHCCCCCCCCCCC
35.9521177872
735PhosphorylationNAKTKLGYSPLHQAA
CCCCCCCCCHHHHHH
19.979428705
736PhosphorylationAKTKLGYSPLHQAAQ
CCCCCCCCHHHHHHH
21.1335091265
747PhosphorylationQAAQQGHTDIVTLLL
HHHHCCCCHHHHHHH
33.9628270605
751PhosphorylationQGHTDIVTLLLKNGA
CCCCHHHHHHHHCCC
16.4228270605
759PhosphorylationLLLKNGASPNEVSSD
HHHHCCCCCCCCCCC
29.6523025827
761HydroxylationLKNGASPNEVSSDGT
HHCCCCCCCCCCCCC
60.8621177872
779PhosphorylationAIAKRLGYISVTDVL
HHHHHHCCEEHHEEE
8.4628060719
781PhosphorylationAKRLGYISVTDVLKV
HHHHCCEEHHEEEEE
15.5220058876
783PhosphorylationRLGYISVTDVLKVVT
HHCCEEHHEEEEEEC
17.3823025827
794O-linked_GlycosylationKVVTDETSFVLVSDK
EEECCCCCEEEEECC
16.0030379171
794PhosphorylationKVVTDETSFVLVSDK
EEECCCCCEEEEECC
16.0023025827
817PhosphorylationVDEILDVSEDEGEEL
HHHHCCCCCCCCCCE
38.7127499020
826PhosphorylationDEGEELISFKAERRD
CCCCCEEEEEEECCC
33.0629691806
834PhosphorylationFKAERRDSRDVDEEK
EEEECCCCCCCHHHH
28.6823898821
856PhosphorylationKLDQVVESPAIPRIP
HHHHHCCCCCCCCCC
14.1819664994
884PhosphorylationQEQASKEYDEDSLIP
HHHHHHHCCCCCCCC
28.5028270605
888PhosphorylationSKEYDEDSLIPSSPA
HHHCCCCCCCCCCCC
26.5928270605
892PhosphorylationDEDSLIPSSPATETS
CCCCCCCCCCCCCCC
41.7928270605
893PhosphorylationEDSLIPSSPATETSD
CCCCCCCCCCCCCCC
17.1328270605
896PhosphorylationLIPSSPATETSDNIS
CCCCCCCCCCCCCCC
43.0828270605
898PhosphorylationPSSPATETSDNISPV
CCCCCCCCCCCCCCC
36.7128270605
899PhosphorylationSSPATETSDNISPVA
CCCCCCCCCCCCCCC
23.5628270605
903PhosphorylationTETSDNISPVASPVH
CCCCCCCCCCCCCCC
21.4128270605
907PhosphorylationDNISPVASPVHTGFL
CCCCCCCCCCCCCEE
27.91113306327
911PhosphorylationPVASPVHTGFLVSFM
CCCCCCCCCEEEEEE
29.8428270605
916PhosphorylationVHTGFLVSFMVDARG
CCCCEEEEEEEECCC
15.1228270605
960O-linked_GlycosylationLVKPQKLSTPPPLAE
ECCCCCCCCCCCCCC
46.0030379171
960PhosphorylationLVKPQKLSTPPPLAE
ECCCCCCCCCCCCCC
46.0022617229
961PhosphorylationVKPQKLSTPPPLAEE
CCCCCCCCCCCCCCC
50.6921082442
1042PhosphorylationGMDEELGSLEELEKK
CCCHHCCCHHHHHHH
45.2729691806
1073PhosphorylationMSRLCQDYDTIGPEG
HHHHCCCCCCCCCCC
6.7923917254
1082PhosphorylationTIGPEGGSLKSKLVP
CCCCCCCCHHHCHHH
43.40-
1085PhosphorylationPEGGSLKSKLVPLVQ
CCCCCHHHCHHHHHH
36.1928270605
1094PhosphorylationLVPLVQATFPENAVT
HHHHHHCCCCCCHHC
23.7228270605
1102AcetylationFPENAVTKRVKLALQ
CCCCHHCHHHHHHHH
48.9030586887
1156PhosphorylationIPLPPSWTDNPRDSG
CCCCCCCCCCCCCCC
30.1824260401
1162O-linked_GlycosylationWTDNPRDSGEGDTTS
CCCCCCCCCCCCCHH
39.7730379171
1162PhosphorylationWTDNPRDSGEGDTTS
CCCCCCCCCCCCCHH
39.7723025827
1227PhosphorylationAEAVNFATLLYKELT
HHHHHHHHHHHHHHC
17.1068730329
1230PhosphorylationVNFATLLYKELTAVP
HHHHHHHHHHHCCHH
12.9168730331
1239SulfoxidationELTAVPYMAKFVIFA
HHCCHHHHEEEEEEE
2.4030846556
1259PhosphorylationREGRLRCYCMTDDKV
CCCCEEEEEECCCHH
4.4626657352
1312PhosphorylationKKAAQQRSFHFQSFR
HHHHHHCCCCCHHHH
20.8023186163
1349PhosphorylationFLRKAMKYEDTQHIL
HHHHHHCCCCCCEEE
13.1225693802
1352PhosphorylationKAMKYEDTQHILCHL
HHHCCCCCCEEEEEE
15.3125693802
1362PhosphorylationILCHLNITMPPCAKG
EEEEECCCCCCCCCC
23.6625693802
1378PhosphorylationGAEDRRRTPTPLALR
CCCHHCCCCCCCHHH
29.6921712546
1380PhosphorylationEDRRRTPTPLALRYS
CHHCCCCCCCHHHHH
30.2622617229
1386PhosphorylationPTPLALRYSILSEST
CCCCHHHHHHHCCCC
10.8323186163
1387PhosphorylationTPLALRYSILSESTP
CCCHHHHHHHCCCCC
15.6023025827
1390PhosphorylationALRYSILSESTPGSL
HHHHHHHCCCCCCCC
28.0323186163
1392PhosphorylationRYSILSESTPGSLSG
HHHHHCCCCCCCCCC
36.2023025827
1393PhosphorylationYSILSESTPGSLSGT
HHHHCCCCCCCCCCC
27.8428857561
1396PhosphorylationLSESTPGSLSGTEQA
HCCCCCCCCCCCHHH
22.1428857561
1398PhosphorylationESTPGSLSGTEQAEM
CCCCCCCCCCHHHHH
45.4262175333
1400PhosphorylationTPGSLSGTEQAEMKM
CCCCCCCCHHHHHHH
22.8823186163
1428PhosphorylationLARELQFSVEDINRI
HHHHHCCCHHHHHCC
16.1923025827
1468PhosphorylationNANMENLYTALQSID
CCCHHHHHHHHHHCC
11.1062217
1469PhosphorylationANMENLYTALQSIDR
CCHHHHHHHHHHCCH
24.8627251275
1473PhosphorylationNLYTALQSIDRGEIV
HHHHHHHHCCHHHHH
27.5727251275
1486PhosphorylationIVNMLEGSGRQSRNL
HHHHHCCCCCCCCCC
22.7923917254
1490PhosphorylationLEGSGRQSRNLKPDR
HCCCCCCCCCCCCCC
23.0628857561
1500PhosphorylationLKPDRRHTDRDYSLS
CCCCCCCCCCCCCCC
30.80-
1504PhosphorylationRRHTDRDYSLSPSQM
CCCCCCCCCCCHHHH
16.65-
1505PhosphorylationRHTDRDYSLSPSQMN
CCCCCCCCCCHHHHC
27.0222210691
1509 (in isoform 11)Phosphorylation-38.3928842319
1509 (in isoform 13)Phosphorylation-38.3928842319
1509 (in isoform 15)Phosphorylation-38.3928842319
1509 (in isoform 4)Phosphorylation-38.3928842319
1509 (in isoform 6)Phosphorylation-38.3928842319
1509 (in isoform 7)Phosphorylation-38.3928842319
1509 (in isoform 9)Phosphorylation-38.3928842319
1514PhosphorylationSPSQMNGYSSLQDEL
CHHHHCCCHHHHHHH
7.0622210691
1523PhosphorylationSLQDELLSPASLGCA
HHHHHHCCHHHHHCH
30.9224275569
1533PhosphorylationSLGCALSSPLRADQY
HHHCHHCCCCCHHHC
28.8924275569
1593PhosphorylationECSKAEDSDATGHEW
CCCCCCCCCCCCCCE
22.2023025827
1596PhosphorylationKAEDSDATGHEWKLE
CCCCCCCCCCCEEEE
44.0223286773
1607PhosphorylationWKLEGALSEEPRGPE
EEEEECCCCCCCCCC
39.1023025827
1617PhosphorylationPRGPELGSLELVEDD
CCCCCCCCEEEECCC
31.15-
1646PhosphorylationEQEEGQRSEEKLPGS
HHHCCCCCCCCCCCC
42.0723286773
1660PhosphorylationSKRQDDATGAGQDSE
CCCCCCCCCCCCCCC
34.2623025827
1666PhosphorylationATGAGQDSENEVSLV
CCCCCCCCCCCEEEE
34.1423401153
1671PhosphorylationQDSENEVSLVSGHQR
CCCCCCEEEECCCCC
19.5123025827
1674PhosphorylationENEVSLVSGHQRGQA
CCCEEEECCCCCCCE
35.5328060719
1677 (in isoform 7)Phosphorylation-55.5126437602
1684PhosphorylationQRGQARITHSPTVSQ
CCCCEECCCCCCHHH
15.6725159151
1686PhosphorylationGQARITHSPTVSQVT
CCEECCCCCCHHHHC
17.3923401153
1688PhosphorylationARITHSPTVSQVTER
EECCCCCCHHHHCHH
35.4922617229
1690PhosphorylationITHSPTVSQVTERSQ
CCCCCCHHHHCHHHH
22.7823911959
1693PhosphorylationSPTVSQVTERSQDRL
CCCHHHHCHHHHHHH
20.3123025827
1696PhosphorylationVSQVTERSQDRLQDW
HHHHCHHHHHHHHHC
30.1511102985
1750PhosphorylationEPGGSQEYEKVLVSV
CCCCCHHHEEEEEEE
17.2621951684
1839 (in isoform 3)Phosphorylation-37.1526437602

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 ANK1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ANK1_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 ANK1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RHAG_HUMANRHAGphysical
12719424
OBSCN_HUMANOBSCNphysical
12631729
TITIN_HUMANTTNphysical
12444090
TIAM1_HUMANTIAM1physical
10893266
KCTD6_HUMANKCTD6physical
22573887
CD44_HUMANCD44physical
9519902
FIG4_HUMANFIG4physical
28514442
FYV1_HUMANPIKFYVEphysical
28514442
PDS5B_HUMANPDS5Bphysical
28514442
VAC14_HUMANVAC14physical
28514442
NELFB_HUMANNELFBphysical
28514442

Drug and Disease Associations
Kegg Disease
H00230 Hereditary spherocytosis (SPH)
OMIM Disease
182900Spherocytosis 1 (SPH1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ANK1_HUMAN

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Related Literatures of Post-Translational Modification
Hydroxylation
ReferencePubMed
"Asparagine and aspartate hydroxylation of the cytoskeletal ankyrinfamily is catalyzed by factor-inhibiting hypoxia-inducible factor.";
Yang M., Ge W., Chowdhury R., Claridge T.D., Kramer H.B.,Schmierer B., McDonough M.A., Gong L., Kessler B.M., Ratcliffe P.J.,Coleman M.L., Schofield C.J.;
J. Biol. Chem. 286:7648-7660(2011).
Cited for: PROTEIN SEQUENCE OF 99-110; 129-169 AND 233-248, INTERACTION WITHHIF1AN, AND HYDROXYLATION AT ASN-105; ASN-233; ASN-431; ASN-464;ASN-629; ASN-662; ASP-695; ASN-728 AND ASN-761.
Phosphorylation
ReferencePubMed
"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-834, AND MASSSPECTROMETRY.
"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-1686, AND MASSSPECTROMETRY.
"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 THR-1684 AND SER-1686, ANDMASS SPECTROMETRY.

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