SPTA1_HUMAN - dbPTM
SPTA1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SPTA1_HUMAN
UniProt AC P02549
Protein Name Spectrin alpha chain, erythrocytic 1
Gene Name SPTA1
Organism Homo sapiens (Human).
Sequence Length 2419
Subcellular Localization Cytoplasm, cytoskeleton. Cytoplasm, cell cortex.
Protein Description Spectrin is the major constituent of the cytoskeletal network underlying the erythrocyte plasma membrane. It associates with band 4.1 and actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane..
Protein Sequence MEQFPKETVVESSGPKVLETAEEIQERRQEVLTRYQSFKERVAERGQKLEDSYHLQVFKRDADDLGKWIMEKVNILTDKSYEDPTNIQGKYQKHQSLEAEVQTKSRLMSELEKTREERFTMGHSAHEETKAHIEELRHLWDLLLELTLEKGDQLLRALKFQQYVQECADILEWIGDKEAIATSVELGEDWERTEVLHKKFEDFQVELVAKEGRVVEVNQYANECAEENHPDLPLIQSKQNEVNAAWERLRGLALQRQKALSNAANLQRFKRDVTEAIQWIKEKEPVLTSEDYGKDLVASEGLFHSHKGLERNLAVMSDKVKELCAKAEKLTLSHPSDAPQIQEMKEDLVSSWEHIRALATSRYEKLQATYWYHRFSSDFDELSGWMNEKTAAINADELPTDVAGGEVLLDRHQQHKHEIDSYDDRFQSADETGQDLVNANHEASDEVREKMEILDNNWTALLELWDERHRQYEQCLDFHLFYRDSEQVDSWMSRQEAFLENEDLGNSLGSAEALLQKHEDFEEAFTAQEEKIITVDKTATKLIGDDHYDSENIKAIRDGLLARRDALREKAATRRRLLKESLLLQKLYEDSDDLKNWINKKKKLADDEDYKDIQNLKSRVQKQQVFEKELAVNKTQLENIQKTGQEMIEGGHYASDNVTTRLSEVASLWEELLEATKQKGTQLHEANQQLQFENNAEDLQRWLEDVEWQVTSEDYGKGLAEVQNRLRKHGLLESAVAARQDQVDILTDLAAYFEEIGHPDSKDIRARQESLVCRFEALKEPLATRKKKLLDLLHLQLICRDTEDEEAWIQETEPSATSTYLGKDLIASKKLLNRHRVILENIASHEPRIQEITERGNKMVEEGHFAAEDVASRVKSLNQNMESLRARAARRQNDLEANVQFQQYLADLHEAETWIREKEPIVDNTNYGADEEAAGALLKKHEAFLLDLNSFGDSMKALRNQANACQQQQAAPVEGVAGEQRVMALYDFQARSPREVTMKKGDVLTLLSSINKDWWKVEAADHQGIVPAVYVRRLAHDEFPMLPQRRREEPGNITQRQEQIENQYRSLLDRAEERRRRLLQRYNEFLLAYEAGDMLEWIQEKKAENTGVELDDVWELQKKFDEFQKDLNTNEPRLRDINKVADDLLFEGLLTPEGAQIRQELNSRWGSLQRLADEQRQLLGSAHAVEVFHREADDTKEQIEKKCQALSAADPGSDLFSVQALQRRHEGFERDLVPLGDKVTILGETAERLSESHPDATEDLQRQKMELNEAWEDLQGRTKDRKESLNEAQKFYLFLSKARDLQNWISSIGGMVSSQELAEDLTGIEILLERHQEHRADMEAEAPTFQALEDFSAELIDSGHHASPEIEKKLQAVKLERDDLEKAWEKRKKILDQCLELQMFQGNCDQVESWMVARENSLRSDDKSSLDSLEALMKKRDDLDKAITAQEGKITDLEHFAESLIADEHYAKEEIATRLQRVLDRWKALKAQLIDERTKLGDYANLKQFYRDLEELEEWISEMLPTACDESYKDATNIQRKYLKHQTFAHEVDGRSEQVHGVINLGNSLIECSACDGNEEAMKEQLEQLKEHWDHLLERTNDKGKKLNEASRQQRFNTSIRDFEFWLSEAETLLAMKDQARDLASAGNLLKKHQLLEREMLAREDALKDLNTLAEDLLSSGTFNVDQIVKKKDNVNKRFLNVQELAAAHHEKLKEAYALFQFFQDLDDEESWIEEKLIRVSSQDYGRDLQGVQNLLKKHKRLEGELVAHEPAIQNVLDMAEKLKDKAAVGQEEIQLRLAQFVEHWEKLKELAKARGLKLEESLEYLQFMQNAEEEEAWINEKNALAVRGDCGDTLAATQSLLMKHEALENDFAVHETRVQNVCAQGEDILNKVLQEESQNKEISSKIEALNEKTPSLAKAIAAWKLQLEDDYAFQEFNWKADVVEAWIADKETSLKTNGNGADLGDFLTLLAKQDTLDASLQSFQQERLPEITDLKDKLISAQHNQSKAIEERYAALLKRWEQLLEASAVHRQKLLEKQLPLQKAEDLFVEFAHKASALNNWCEKMEENLSEPVHCVSLNEIRQLQKDHEDFLASLARAQADFKCLLELDQQIKALGVPSSPYTWLTVEVLERTWKHLSDIIEEREQELQKEEARQVKNFEMCQEFEQNASTFLQWILETRAYFLDGSLLKETGTLESQLEANKRKQKEIQAMKRQLTKIVDLGDNLEDALILDIKYSTIGLAQQWDQLYQLGLRMQHNLEQQIQAKDIKGVSEETLKEFSTIYKHFDENLTGRLTHKEFRSCLRGLNYYLPMVEEDEHEPKFEKFLDAVDPGRKGYVSLEDYTAFLIDKESENIKSSDEIENAFQALAEGKSYITKEDMKQALTPEQVSFCATHMQQYMDPRGRSHLSGYDYVGFTNSYFGN
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
8PhosphorylationMEQFPKETVVESSGP
CCCCCCCHHHCCCCC
35.6622468782
13PhosphorylationKETVVESSGPKVLET
CCHHHCCCCCHHHHH
45.6822468782
20PhosphorylationSGPKVLETAEEIQER
CCCHHHHHHHHHHHH
34.9022468782
35PhosphorylationRQEVLTRYQSFKERV
HHHHHHHHHHHHHHH
11.8529449344
37PhosphorylationEVLTRYQSFKERVAE
HHHHHHHHHHHHHHH
29.3828152594
59AcetylationSYHLQVFKRDADDLG
HHHEEEECCCHHHHH
50.9830592629
96PhosphorylationGKYQKHQSLEAEVQT
CCHHHHHCHHHHHHH
28.0927251275
109PhosphorylationQTKSRLMSELEKTRE
HHHHHHHHHHHHHHH
43.5523403867
261PhosphorylationLQRQKALSNAANLQR
HHHHHHHHHHHHHHH
29.3123025827
283AcetylationAIQWIKEKEPVLTSE
HHHHHHHHCCCCCCC
63.4220167786
299PhosphorylationYGKDLVASEGLFHSH
HCCCCHHCCCCCCCC
25.39-
317PhosphorylationERNLAVMSDKVKELC
HHHHHHHCHHHHHHH
27.9019664994
361PhosphorylationHIRALATSRYEKLQA
HHHHHHHHHHHHHHH
27.5325627689
370PhosphorylationYEKLQATYWYHRFSS
HHHHHHHHHHHHCCC
13.64-
421PhosphorylationQHKHEIDSYDDRFQS
HCCCCCCCCHHHHHC
35.8028270605
422PhosphorylationHKHEIDSYDDRFQSA
CCCCCCCCHHHHHCC
20.3628270605
428PhosphorylationSYDDRFQSADETGQD
CCHHHHHCCCHHCHH
34.6728270605
432PhosphorylationRFQSADETGQDLVNA
HHHCCCHHCHHHHHC
40.4628270605
507PhosphorylationENEDLGNSLGSAEAL
HCCHHHHCCCCHHHH
32.1023025827
510PhosphorylationDLGNSLGSAEALLQK
HHHHCCCCHHHHHHH
28.3823025827
548PhosphorylationKLIGDDHYDSENIKA
HHHCCCCCCHHHHHH
28.3220206558
588PhosphorylationSLLLQKLYEDSDDLK
HHHHHHHHCCCHHHH
25.40-
635PhosphorylationKELAVNKTQLENIQK
HHHCCCHHHHHHHHH
32.9319664994
762UbiquitinationEIGHPDSKDIRARQE
HHCCCCHHHHHHHHH
65.6330230243
812PhosphorylationEEAWIQETEPSATST
HHHHHHCCCCCCCHH
36.50-
818PhosphorylationETEPSATSTYLGKDL
CCCCCCCHHCCCHHH
18.12-
844O-linked_GlycosylationVILENIASHEPRIQE
HHHHHHHHCCHHHHH
25.2930379171
876PhosphorylationDVASRVKSLNQNMES
HHHHHHHHHHHHHHH
29.6923898821
986PhosphorylationEQRVMALYDFQARSP
HHHHHHHHEECCCCC
12.7423917254
992PhosphorylationLYDFQARSPREVTMK
HHEECCCCCCEECCC
31.1823025827
1064PhosphorylationQEQIENQYRSLLDRA
HHHHHHHHHHHHHHH
17.47-
1151PhosphorylationLLFEGLLTPEGAQIR
HHHCCCCCCCHHHHH
25.0823025827
1167PhosphorylationELNSRWGSLQRLADE
HHHHCHHHHHHHHHH
17.8623025827
1250O-linked_GlycosylationGETAERLSESHPDAT
HHHHHHHHHHCCCHH
43.1830379171
1250PhosphorylationGETAERLSESHPDAT
HHHHHHHHHHCCCHH
43.18-
1257PhosphorylationSESHPDATEDLQRQK
HHHCCCHHHHHHHHH
37.09-
1278PhosphorylationWEDLQGRTKDRKESL
HHHHCCCCCCHHHHH
44.0922199227
1284PhosphorylationRTKDRKESLNEAQKF
CCCCHHHHHHHHHHH
39.2623025827
1296PhosphorylationQKFYLFLSKARDLQN
HHHHHHHHHHHHHHH
19.5523025827
1344PhosphorylationDMEAEAPTFQALEDF
CCCCCCCHHHHHHHH
35.1128270605
1352PhosphorylationFQALEDFSAELIDSG
HHHHHHHHHHHHHCC
32.9128270605
1358PhosphorylationFSAELIDSGHHASPE
HHHHHHHCCCCCCHH
32.7928270605
1363PhosphorylationIDSGHHASPEIEKKL
HHCCCCCCHHHHHHH
20.7828270605
1424PhosphorylationSLRSDDKSSLDSLEA
CCCCCCCCHHHHHHH
43.03-
1425PhosphorylationLRSDDKSSLDSLEAL
CCCCCCCHHHHHHHH
41.77-
1428PhosphorylationDDKSSLDSLEALMKK
CCCCHHHHHHHHHHC
33.1423186163
1486UbiquitinationLDRWKALKAQLIDER
HHHHHHHHHHHHCHH
38.6629967540
1499PhosphorylationERTKLGDYANLKQFY
HHHHHCCHHCHHHHH
8.8020206558
1538PhosphorylationATNIQRKYLKHQTFA
CHHHHHHHHHHCCCE
24.1518083107
1579AcetylationDGNEEAMKEQLEQLK
CCCHHHHHHHHHHHH
49.7311922443
1586AcetylationKEQLEQLKEHWDHLL
HHHHHHHHHHHHHHH
47.4211922455
1710UbiquitinationAAHHEKLKEAYALFQ
HHCHHHHHHHHHHHH
51.9011165260
1738O-linked_GlycosylationEKLIRVSSQDYGRDL
HHHHHHHCCHHCCCH
24.9830379171
1803 (in isoform 1)Ubiquitination-60.7221890473
1803UbiquitinationQFVEHWEKLKELAKA
HHHHHHHHHHHHHHH
60.7222817900
1803 (in isoform 2)Ubiquitination-60.7221890473
1803AcetylationQFVEHWEKLKELAKA
HHHHHHHHHHHHHHH
60.7225953088
1805UbiquitinationVEHWEKLKELAKARG
HHHHHHHHHHHHHCC
62.8522817900
1901PhosphorylationSQNKEISSKIEALNE
HCCHHHHHHHHHHHC
43.23-
1909AcetylationKIEALNEKTPSLAKA
HHHHHHCCCHHHHHH
65.7419413330
1910PhosphorylationIEALNEKTPSLAKAI
HHHHHCCCHHHHHHH
16.36-
1912PhosphorylationALNEKTPSLAKAIAA
HHHCCCHHHHHHHHH
46.31-
1976PhosphorylationKQDTLDASLQSFQQE
HCCCHHHHHHHHHHH
26.978018926
2051AcetylationLFVEFAHKASALNNW
HHHHHHHHHHHHHHH
40.3830592617
2184PhosphorylationRAYFLDGSLLKETGT
HHHHCCCCHHHHCCC
30.1424719451
2200AcetylationESQLEANKRKQKEIQ
HHHHHHHHHHHHHHH
68.9430592623
2269PhosphorylationAKDIKGVSEETLKEF
HHCCCCCCHHHHHHH
38.0823025827
2272PhosphorylationIKGVSEETLKEFSTI
CCCCCHHHHHHHHHH
38.7923025827
2277PhosphorylationEETLKEFSTIYKHFD
HHHHHHHHHHHHHCC
18.2623403867
2278PhosphorylationETLKEFSTIYKHFDE
HHHHHHHHHHHHCCC
33.3823403867
2280PhosphorylationLKEFSTIYKHFDENL
HHHHHHHHHHCCCCC
9.8623403867
2288PhosphorylationKHFDENLTGRLTHKE
HHCCCCCCCCCCHHH
31.6623312004
2333PhosphorylationVDPGRKGYVSLEDYT
CCCCCCCEECHHHHH
7.0119060867
2335PhosphorylationPGRKGYVSLEDYTAF
CCCCCEECHHHHHEE
19.9827251275
2381PhosphorylationEDMKQALTPEQVSFC
HHHHHCCCHHHHHHH
28.0028450419
2386PhosphorylationALTPEQVSFCATHMQ
CCCHHHHHHHHHHHH
17.8228450419
2390PhosphorylationEQVSFCATHMQQYMD
HHHHHHHHHHHHHCC
21.0428450419
2395PhosphorylationCATHMQQYMDPRGRS
HHHHHHHHCCCCCCC
6.1328450419
2405PhosphorylationPRGRSHLSGYDYVGF
CCCCCCCCCCCCCCC
29.86-
2407PhosphorylationGRSHLSGYDYVGFTN
CCCCCCCCCCCCCCC
10.75-

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 SPTA1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SPTA1_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 SPTA1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FANCA_HUMANFANCAphysical
12571280
XPF_HUMANERCC4physical
12571280
ANK1_HUMANANK1physical
2971657
SPTB1_HUMANSPTBphysical
1634521
ANK1_HUMANANK1physical
15929114
SPTA1_HUMANSPTA1physical
12672815
SMCA4_HUMANSMARCA4physical
16889989
ROA2_HUMANHNRNPA2B1physical
16889989
SMCA2_HUMANSMARCA2physical
16889989
ERCC5_HUMANERCC5physical
16889989
ERCC6_HUMANERCC6physical
16889989
FANCA_HUMANFANCAphysical
16889989
FACD2_HUMANFANCD2physical
16889989
RAD50_HUMANRAD50physical
16889989
FANCJ_HUMANBRIP1physical
16889989
XPF_HUMANERCC4physical
16889989
ERCC3_HUMANERCC3physical
16889989
MRE11_HUMANMRE11Aphysical
16889989
XRCC5_HUMANXRCC5physical
16889989
ERCC2_HUMANERCC2physical
16889989
SPTN4_HUMANSPTBN4physical
16889989
XRCC6_HUMANXRCC6physical
16889989
RFA1_HUMANRPA1physical
16889989
LMNA_HUMANLMNAphysical
16889989
PML_HUMANPMLphysical
16889989
FANCG_HUMANFANCGphysical
16889989
FANCC_HUMANFANCCphysical
16889989
RD23B_HUMANRAD23Bphysical
16889989
FANCF_HUMANFANCFphysical
16889989
XPA_HUMANXPAphysical
16889989
RSSA_HUMANRPSAphysical
16889989
RAD51_HUMANRAD51physical
16889989
ERCC1_HUMANERCC1physical
16889989
EMD_HUMANEMDphysical
16889989
XRCC2_HUMANXRCC2physical
16889989
RFA2_HUMANRPA2physical
16889989
E41L3_HUMANEPB41L3physical
16889989
ACTS_HUMANACTA1physical
16889989

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
130600Elliptocytosis 2 (EL2)
266140Hereditary pyropoikilocytosis (HPP)
270970Spherocytosis 3 (SPH3)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SPTA1_HUMAN

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Related Literatures of Post-Translational Modification

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