SPTB1_HUMAN - dbPTM
SPTB1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SPTB1_HUMAN
UniProt AC P11277
Protein Name Spectrin beta chain, erythrocytic
Gene Name SPTB
Organism Homo sapiens (Human).
Sequence Length 2137
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 MTSATEFENVGNQPPYSRINARWDAPDDELDNDNSSARLFERSRIKALADEREVVQKKTFTKWVNSHLARVSCRITDLYKDLRDGRMLIKLLEVLSGEMLPKPTKGKMRIHCLENVDKALQFLKEQRVHLENMGSHDIVDGNHRLVLGLIWTIILRFQIQDIVVQTQEGRETRSAKDALLLWCQMKTAGYPHVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDKLKDSNARHNLEHAFNVAERQLGIIPLLDPEDVFTENPDEKSIITYVVAFYHYFSKMKVLAVEGKRVGKVIDHAIETEKMIEKYSGLASDLLTWIEQTITVLNSRKFANSLTGVQQQLQAFSTYRTVEKPPKFQEKGNLEVLLFTIQSRMRANNQKVYTPHDGKLVSDINRAWESLEEAEYRRELALRNELIRQEKLEQLARRFDRKAAMRETWLSENQRLVAQDNFGYDLAAVEAAKKKHEAIETDTAAYEERVRALEDLAQELEKENYHDQKRITARKDNILRLWSYLQELLQSRRQRLETTLALQKLFQDMLHSIDWMDEIKAHLLSAEFGKHLLEVEDLLQKHKLMEADIAIQGDKVKAITAATLKFTEGKGYQPCDPQVIQDRISHLEQCFEELSNMAAGRKAQLEQSKRLWKFFWEMDEAESWIKEKEQIYSSLDYGKDLTSVLILQRKHKAFEDELRGLDAHLEQIFQEAHGMVARKQFGHPQIEARIKEVSAQWDQLKDLAAFCKKNLQDAENFFQFQGDADDLKAWLQDAHRLLSGEDVGQDEGATRALGKKHKDFLEELEESRGVMEHLEQQAQGFPEEFRDSPDVTHRLQALRELYQQVVAQADLRQQRLQEALDLYTVFGETDACELWMGEKEKWLAEMEMPDTLEDLEVVQHRFDILDQEMKTLMTQIDGVNLAANSLVESGHPRSREVKQYQDHLNTRWQAFQTLVSERREAVDSALRVHNYCVDCEETSKWITDKTKVVESTKDLGRDLAGIIAIQRKLSGLERDVAAIQARVDALERESQQLMDSHPEQKEDIGQRQKHLEELWQGLQQSLQGQEDLLGEVSQLQAFLQDLDDFQAWLSITQKAVASEDMPESLPEAEQLLQQHAGIKDEIDGHQDSYQRVKESGEKVIQGQTDPEYLLLGQRLEGLDTGWNALGRMWESRSHTLAQCLGFQEFQKDAKQAEAILSNQEYTLAHLEPPDSLEAAEAGIRKFEDFLGSMENNRDKVLSPVDSGNKLVAEGNLYSDKIKEKVQLIEDRHRKNNEKAQEASVLLRDNLELQNFLQNCQELTLWINDKLLTSQDVSYDEARNLHNKWLKHQAFVAELASHEGWLENIDAEGKQLMDEKPQFTALVSQKLEALHRLWDELQATTKEKTQHLSAARSSDLRLQTHADLNKWISAMEDQLRSDDPGKDLTSVNRMLAKLKRVEDQVNVRKEELGELFAQVPSMGEEGGDADLSIEKRFLDLLEPLGRRKKQLESSRAKLQISRDLEDETLWVEERLPLAQSADYGTNLQTVQLFMKKNQTLQNEILGHTPRVEDVLQRGQQLVEAAEIDCQDLEERLGHLQSSWDRLREAAAGRLQRLRDANEAQQYYLDADEAEAWIGEQELYVISDEIPKDEEGAIVMLKRHLRQQRAVEDYGRNIKQLASRAQGLLSAGHPEGEQIIRLQGQVDKHYAGLKDVAEERKRKLENMYHLFQLKRETDDLEQWISEKELVASSPEMGQDFDHVTLLRDKFRDFARETGAIGQERVDNVNAFIERLIDAGHSEAATIAEWKDGLNEMWADLLELIDTRMQLLAASYDLHRYFYTGAEILGLIDEKHRELPEDVGLDASTAESFHRVHTAFERELHLLGVQVQQFQDVATRLQTAYAGEKAEAIQNKEQEVSAAWQALLDACAGRRTQLVDTADKFRFFSMARDLLSWMESIIRQIETQERPRDVSSVELLMKYHQGINAEIETRSKNFSACLELGESLLQRQHQASEEIREKLQQVMSRRKEMNEKWEARWERLRMLLEVCQFSRDASVAEAWLIAQEPYLASGDFGHTVDSVEKLIKRHEAFEKSTASWAERFAALEKPTTLELKERQIAERPAEETGPQEEEGETAGEAPVSHHAATERTSPVSLWSRLSSSWESLQPEPSHPY
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------MTSATEFEN
------CCCCCCCCC
38.0728857561
3Phosphorylation-----MTSATEFENV
-----CCCCCCCCCC
45.0828857561
5Phosphorylation---MTSATEFENVGN
---CCCCCCCCCCCC
40.7628857561
35PhosphorylationDELDNDNSSARLFER
CCCCCCCHHHHHHHH
28.3928857561
35 (in isoform 2)Phosphorylation-28.3927251275
36PhosphorylationELDNDNSSARLFERS
CCCCCCHHHHHHHHH
24.5421082442
36 (in isoform 2)Phosphorylation-24.54-
57UbiquitinationDEREVVQKKTFTKWV
CHHHHHHHHHHHHHH
42.0223000965
58UbiquitinationEREVVQKKTFTKWVN
HHHHHHHHHHHHHHH
31.6023000965
62UbiquitinationVQKKTFTKWVNSHLA
HHHHHHHHHHHHHHH
44.9821890473
62 (in isoform 1)Ubiquitination-44.9821890473
62 (in isoform 2)Ubiquitination-44.9821890473
62 (in isoform 3)Ubiquitination-44.9821890473
66PhosphorylationTFTKWVNSHLARVSC
HHHHHHHHHHHHHHH
15.4028857561
76PhosphorylationARVSCRITDLYKDLR
HHHHHHHHHHHHHHH
10.70-
80AcetylationCRITDLYKDLRDGRM
HHHHHHHHHHHCCHH
58.5519813157
90AcetylationRDGRMLIKLLEVLSG
HCCHHHHHHHHHHCC
42.9526051181
96PhosphorylationIKLLEVLSGEMLPKP
HHHHHHHCCCCCCCC
37.5718452278
96 (in isoform 2)Phosphorylation-37.57-
102UbiquitinationLSGEMLPKPTKGKMR
HCCCCCCCCCCCCCC
62.45-
104PhosphorylationGEMLPKPTKGKMRIH
CCCCCCCCCCCCCCC
59.5623186163
107UbiquitinationLPKPTKGKMRIHCLE
CCCCCCCCCCCCHHC
26.93-
118AcetylationHCLENVDKALQFLKE
CHHCCHHHHHHHHHH
46.8754421449
118UbiquitinationHCLENVDKALQFLKE
CHHCCHHHHHHHHHH
46.8730230243
124AcetylationDKALQFLKEQRVHLE
HHHHHHHHHCCCCHH
53.7626051181
124UbiquitinationDKALQFLKEQRVHLE
HHHHHHHHHCCCCHH
53.7633845483
133SulfoxidationQRVHLENMGSHDIVD
CCCCHHHCCCCCCCC
4.2028183972
152PhosphorylationLVLGLIWTIILRFQI
HHHHHHHHHHHHHHH
7.37-
224AcetylationPDLIDFDKLKDSNAR
CCCCCHHHHCCCCHH
58.3825953088
224UbiquitinationPDLIDFDKLKDSNAR
CCCCCHHHHCCCCHH
58.3829967540
307PhosphorylationTEKMIEKYSGLASDL
HHHHHHHHHCHHHHH
8.6521951684
316PhosphorylationGLASDLLTWIEQTIT
CHHHHHHHHHHHHHH
31.52-
355AcetylationRTVEKPPKFQEKGNL
CCCCCCCCCCCCCCE
69.117932607
379AcetylationRMRANNQKVYTPHDG
HHHHCCCCCCCCCCC
39.057932619
390PhosphorylationPHDGKLVSDINRAWE
CCCCCCHHHHHHHHH
43.1223312004
398PhosphorylationDINRAWESLEEAEYR
HHHHHHHHHHHHHHH
30.3128258704
404PhosphorylationESLEEAEYRRELALR
HHHHHHHHHHHHHHH
23.2428258704
419UbiquitinationNELIRQEKLEQLARR
HHHHHHHHHHHHHHH
49.32-
439PhosphorylationAMRETWLSENQRLVA
HHHHHHHCHHHHHHH
26.5125867546
461AcetylationLAAVEAAKKKHEAIE
HHHHHHHHHHHHHCC
70.2030705433
462GlycationAAVEAAKKKHEAIET
HHHHHHHHHHHHCCC
55.42-
474PhosphorylationIETDTAAYEERVRAL
CCCCHHHHHHHHHHH
18.8321951684
493PhosphorylationQELEKENYHDQKRIT
HHHHHCCCCCHHCHH
14.0921951684
497AcetylationKENYHDQKRITARKD
HCCCCCHHCHHHCHH
52.4030705439
519PhosphorylationYLQELLQSRRQRLET
HHHHHHHHHHHHHHH
29.42-
637AcetylationKAQLEQSKRLWKFFW
HHHHHHHHHHHHHHH
51.7230578653
660PhosphorylationIKEKEQIYSSLDYGK
HHHHHHHHHHCCCCC
7.6021951684
670PhosphorylationLDYGKDLTSVLILQR
CCCCCCHHHHHHHHH
27.2429083192
671O-linked_GlycosylationDYGKDLTSVLILQRK
CCCCCHHHHHHHHHH
23.4028411811
671PhosphorylationDYGKDLTSVLILQRK
CCCCCHHHHHHHHHH
23.4029083192
767O-linked_GlycosylationQDAHRLLSGEDVGQD
HHHHHHHCCCCCCCC
44.7312556401
979PhosphorylationDKTKVVESTKDLGRD
CCHHHHHCCHHHCHH
29.19-
998PhosphorylationIAIQRKLSGLERDVA
HHHHHHHCCCHHHHH
53.0323025827
998 (in isoform 2)Phosphorylation-53.0327251275
1018PhosphorylationVDALERESQQLMDSH
HHHHHHHHHHHHHCC
29.4624719451
1024PhosphorylationESQQLMDSHPEQKED
HHHHHHHCCHHHHHH
27.2929759185
1226PhosphorylationNNRDKVLSPVDSGNK
CCCCCCCCCCCCCCC
26.3523025827
1226 (in isoform 2)Phosphorylation-26.3527251275
1242PhosphorylationVAEGNLYSDKIKEKV
EEECCCCCHHHHHHH
35.28-
1258AcetylationLIEDRHRKNNEKAQE
HHHHHHHHCCHHHHH
58.9888185
1262AcetylationRHRKNNEKAQEASVL
HHHHCCHHHHHHHHH
58.4588189
1296PhosphorylationWINDKLLTSQDVSYD
HHCCCCCCCCCCCHH
34.4823025827
1297O-linked_GlycosylationINDKLLTSQDVSYDE
HCCCCCCCCCCCHHH
25.0928411811
1297PhosphorylationINDKLLTSQDVSYDE
HCCCCCCCCCCCHHH
25.09-
1301PhosphorylationLLTSQDVSYDEARNL
CCCCCCCCHHHHHHH
34.8523025827
1302PhosphorylationLTSQDVSYDEARNLH
CCCCCCCHHHHHHHH
20.0423025827
1372PhosphorylationQATTKEKTQHLSAAR
HHHCHHHHHHHHHHH
23.4726437602
1376PhosphorylationKEKTQHLSAARSSDL
HHHHHHHHHHHHCCC
20.1226437602
1396PhosphorylationADLNKWISAMEDQLR
HHHHHHHHHHHHHHH
22.0523025827
1444PhosphorylationELFAQVPSMGEEGGD
HHHHCCCCCCCCCCC
40.3323025827
1455PhosphorylationEGGDADLSIEKRFLD
CCCCCCCCHHHHHHH
29.2823025827
1476PhosphorylationRRKKQLESSRAKLQI
HHHHHHHHHHHHHHH
33.4429083192
1477PhosphorylationRKKQLESSRAKLQIS
HHHHHHHHHHHHHHC
27.2129083192
1590PhosphorylationANEAQQYYLDADEAE
CHHHHHHHCCHHHHH
8.1821951684
1652O-linked_GlycosylationSRAQGLLSAGHPEGE
HHHHHHHHCCCCCHH
36.9312556403
1672PhosphorylationQGQVDKHYAGLKDVA
ECCCCHHHCCHHHHH
14.22-
1796PhosphorylationRMQLLAASYDLHRYF
HHHHHHHHHCHHHHH
17.3621406692
1797PhosphorylationMQLLAASYDLHRYFY
HHHHHHHHCHHHHHH
20.1421406692
1829PhosphorylationEDVGLDASTAESFHR
CCCCCCHHHHHHHHH
28.0228060719
1830PhosphorylationDVGLDASTAESFHRV
CCCCCHHHHHHHHHH
35.8428060719
1833PhosphorylationLDASTAESFHRVHTA
CCHHHHHHHHHHHHH
24.7228060719
1928O-linked_GlycosylationSIIRQIETQERPRDV
HHHHHHHCCCCCCCC
37.0430379171
1936O-linked_GlycosylationQERPRDVSSVELLMK
CCCCCCCCHHHHHHH
32.7112556407
1960PhosphorylationETRSKNFSACLELGE
HHCCCCHHHHHHHHH
27.7127251275
1989PhosphorylationEKLQQVMSRRKEMNE
HHHHHHHHHHHHHHH
30.0330108239
2031PhosphorylationWLIAQEPYLASGDFG
HHHHCCCCCCCCCCC
17.7228270605
2034PhosphorylationAQEPYLASGDFGHTV
HCCCCCCCCCCCCCH
35.9828270605
2040PhosphorylationASGDFGHTVDSVEKL
CCCCCCCCHHHHHHH
26.7928270605
2043PhosphorylationDFGHTVDSVEKLIKR
CCCCCHHHHHHHHHH
28.0423025827
2043 (in isoform 2)Phosphorylation-28.0427251275
2057PhosphorylationRHEAFEKSTASWAER
HHHHHHHHHHHHHHH
23.2326437602
2058PhosphorylationHEAFEKSTASWAERF
HHHHHHHHHHHHHHH
35.4622673903
2060PhosphorylationAFEKSTASWAERFAA
HHHHHHHHHHHHHHH
27.2323025827
2060 (in isoform 2)Phosphorylation-27.2327251275
2072PhosphorylationFAALEKPTTLELKER
HHHHCCCCCHHHHHH
55.8928060719
2073PhosphorylationAALEKPTTLELKERQ
HHHCCCCCHHHHHHH
27.1128060719
2098PhosphorylationPQEEEGETAGEAPVS
CCHHCCCCCCCCCCC
51.3123186163
2105PhosphorylationTAGEAPVSHHAATER
CCCCCCCCCCCCCCC
14.4323186163
2110PhosphorylationPVSHHAATERTSPVS
CCCCCCCCCCCCCHH
27.1215065869
2113PhosphorylationHHAATERTSPVSLWS
CCCCCCCCCCHHHHH
31.0223025827
2113 (in isoform 2)Phosphorylation-31.0228270605
2114PhosphorylationHAATERTSPVSLWSR
CCCCCCCCCHHHHHH
29.5330266825
2114 (in isoform 2)Phosphorylation-29.5328270605
2117PhosphorylationTERTSPVSLWSRLSS
CCCCCCHHHHHHHHC
27.7530266825
2120PhosphorylationTSPVSLWSRLSSSWE
CCCHHHHHHHHCCHH
28.7423186163
2123PhosphorylationVSLWSRLSSSWESLQ
HHHHHHHHCCHHHCC
22.6330266825
2124PhosphorylationSLWSRLSSSWESLQP
HHHHHHHCCHHHCCC
44.0230266825
2125PhosphorylationLWSRLSSSWESLQPE
HHHHHHCCHHHCCCC
31.3330266825
2128PhosphorylationRLSSSWESLQPEPSH
HHHCCHHHCCCCCCC
26.5030266825
2134PhosphorylationESLQPEPSHPY----
HHCCCCCCCCC----
35.1229691806
2137PhosphorylationQPEPSHPY-------
CCCCCCCC-------
26.2629691806
2158 (in isoform 2)Phosphorylation-24076635
2161 (in isoform 2)Phosphorylation-24076635
2168 (in isoform 2)Phosphorylation-28270605
2178 (in isoform 2)Phosphorylation--
2184 (in isoform 2)Phosphorylation--
2213 (in isoform 2)Phosphorylation--
2216 (in isoform 2)Phosphorylation--
2257Ubiquitination-------------------------------------------------------------------------------------------------------------------------------
-------------------------------------------------------------------------------------------------------------------------------
32015554
2299 (in isoform 2)Phosphorylation-23285258
2322 (in isoform 2)Phosphorylation-26437602

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 SPTB1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
2110TPhosphorylation

15065869
2114SPhosphorylation

15065869
2117SPhosphorylation

15065869
2123SPhosphorylation

15065869
2125SPhosphorylation

15065869
2128SPhosphorylation

15065869

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 SPTB1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ANK1_HUMANANK1physical
2141335
41_HUMANEPB41physical
7673158

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
182870Elliptocytosis 3 (EL3)
182870Spherocytosis 2 (SPH2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SPTB1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"In vivo phosphorylation of human erythrocyte spectrin occurs in asequential manner.";
Tang H.Y., Speicher D.W.;
Biochemistry 43:4251-4262(2004).
Cited for: PHOSPHORYLATION AT THR-2110; SER-2114; SER-2117; SER-2123; SER-2125AND SER-2128.
"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 THR-2073, AND MASSSPECTROMETRY.

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