Overview
| Uniprot ID | G3V6S0 |
| Protein Name | Spectrin beta chain |
| Gene Name | Sptbn1 |
| Organism | Rattus norvegicus |
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 105 |
ERLPKPTKGRMRIHC |
| 1120 |
NYEEDYQKMRDMGEM |
| 1210 |
GAEAAIKKQEDFMTT |
| 124 |
DKALQFLKEQRVHLE |
| 1312 |
EARNLHSKWLKHQAF |
| 1352 |
PETEAVVKEKLTGLH |
| 1354 |
TEAVVKEKLTGLHKM |
| 1620 |
LYMMSEEKAKDEQSA |
| 170 |
SVETEDNKEKKSAKD |
| 1989 |
HYASEEIKEKLLQLT |
| 1991 |
ASEEIKEKLLQLTEK |
| 2174 |
PSPTSDRKAKSALPA |
| 224 |
PDLIDFDKLKKSNAH |
| 2354 |
DKEKDKEKRFSLFGK |
| 281 |
YHYFSKMKALAVEGK |
| 379 |
KMRANNQKVYMPREG |
| 401 |
KAWERLEKAEHEREL |
| 419 |
NELIRQEKLEQLARR |
| 463 |
AVEAATKKHEAIETD |
| 497 |
AESYHDIKRITARKD |
| 659 |
GWIREKEKILSSDDY |
| 668 |
LSSDDYGKDLTSVMR |
| 842 |
AELTRLRKQALQDTL |
Function
Fodrin, which seems to be involved in secretion, interacts with calmodulin in a calcium-dependent manner and is thus candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Plays a critical role in central nervous system development and function
Protein Sequence
10
MTTTVATDYD
20
NIEIQQQYSD
30
VNNRWDVDDW
40
DNENSSARLF
50
ERSRIKALAD
60
EREAVQKKTF
70
TKWVNSHLAR
80
VSCRITDLYT
90
DLRDGRMLIK
100
LLEVLSGERL
110
PKPTKGRMRI
120
HCLENVDKAL
130
QFLKEQRVHL
140
ENMGSHDIVD
150
GNHRLTLGLI
160
WTIILRFQIQ
170
DISVETEDNK
180
EKKSAKDALL
190
LWCQMKTAGY
200
PNVNIHNFTT
210
SWRDGMAFNA
220
LIHKHRPDLI
230
DFDKLKKSNA
240
HYNLQNAFNL
250
AEQHLGLTKL
260
LDPEDISVDH
270
PDEKSIITYV
280
VTYYHYFSKM
290
KALAVEGKRI
300
GKVLDNAIET
310
EKMIEKYESL
320
ASDLLEWIEQ
330
TIIILNNRKF
340
ANSLVGVQQQ
350
LQAFNTYRTV
360
EKPPKFTEKG
370
NLEVLLFTIQ
380
SKMRANNQKV
390
YMPREGKLIS
400
DINKAWERLE
410
KAEHERELAL
420
RNELIRQEKL
430
EQLARRFDRK
440
AAMRETWLSE
450
NQRLVSQDNF
460
GFDLPAVEAA
470
TKKHEAIETD
480
IAAYEERVQA
490
VVAVARELEA
500
ESYHDIKRIT
510
ARKDNVIRLW
520
EYLLELLRAR
530
RQRLEMNLGL
540
QKIFQEMLYI
550
MDWMDEMKVL
560
LLSQDYGKHL
570
LGVEDLLQKH
580
ALVEADIAIQ
590
AERVRGVNAS
600
AQKFATDGEG
610
YKPCDPQVIR
620
DRVAHMEFCY
630
QELCQLAAER
640
RARLEESRRL
650
WKFFWEMAEE
660
EGWIREKEKI
670
LSSDDYGKDL
680
TSVMRLLSKH
690
RAFEDEMSGR
700
SGHFEQAIKE
710
GEDMIAEEHF
720
GSEKIRERIS
730
YIREQWANLE
740
QLSAIRKKRL
750
EEASLLHQFQ
760
ADADDIDAWM
770
LDILKIVSSN
780
DVGHDEYSTQ
790
SLVKKHKDVA
800
EEISNYRPTI
810
DTLHEQAGAL
820
PQAHAESPDV
830
KGRLAGIEER
840
YKEVAELTRL
850
RKQALQDTLA
860
LYKMFSEADA
870
CELWIDEKEQ
880
WLNNMQIPEK
890
LEDLEVIQHR
900
FESLEPEMNN
910
QASRVAVVNQ
920
IARQLMHSGH
930
PSEKEIRAQQ
940
DKLNTRWSQF
950
RELVDRKKDA
960
LLSALSIQNY
970
HLECNETKSW
980
IREKTKVIES
990
TQDLGNDLAG
1000
VMALQRKLTG
1010
MERDLVAIEA
1020
KLSDLQKEAE
1030
KLESEHPDQA
1040
QAILSRLAEI
1050
SDVWEEMKTT
1060
LKNREASLGE
1070
ASKLQQFLRD
1080
LDDFQSWLSR
1090
TQTAIASEDM
1100
PNTLTEAEKL
1110
LTQHENIKNE
1120
IDNYEEDYQK
1130
MRDMGEMVTQ
1140
GQTDAQYMFL
1150
RQRLQALDTG
1160
WNELHKMWEN
1170
RQNLLSQSHA
1180
YQQFLRDTKQ
1190
AEAFLNNQEY
1200
VLAHTEMPTT
1210
LEGAEAAIKK
1220
QEDFMTTMDA
1230
NEEKINAVVE
1240
TGRRLVSDGN
1250
INSDRIQEKV
1260
DSIDDRHRKN
1270
REAASELLMR
1280
LKDNRDLQKF
1290
LQDCQELSLW
1300
INEKMLTAQD
1310
MSYDEARNLH
1320
SKWLKHQAFM
1330
AELASNKEWL
1340
DKIEKEGMQL
1350
ISEKPETEAV
1360
VKEKLTGLHK
1370
MWEVLESTTQ
1380
TKAQRLFDAN
1390
KAELFTQSCA
1400
DLDKWLHGLE
1410
SQIQSDDYGK
1420
DLTSVNILLK
1430
KQQMLENQME
1440
VRKKEIEELQ
1450
SQAQALSQEG
1460
KSTDEVDSKR
1470
LTVQTKFMEL
1480
LEPLNERKHN
1490
LLASKEIHQF
1500
NRDVEDEILW
1510
VGERMPLATS
1520
TDHGHNLQTV
1530
QLLIKKNQTL
1540
QKEIQGHQPR
1550
IDDIFERSQN
1560
IITDSSSLNA
1570
EAIRQRLADL
1580
KQLWGLLIEE
1590
TEKRHRRLEE
1600
AHKAQQYYFD
1610
AAEAEAWMSE
1620
QELYMMSEEK
1630
AKDEQSAVSM
1640
LKKHQILEQA
1650
VEDYAETVHQ
1660
LSKTSRALVA
1670
DSHPESERIS
1680
MRQSKVDKLY
1690
AGLKDLAEER
1700
RGKLDERHRL
1710
FQLNREVDDL
1720
EQWIAEREVV
1730
AGSHELGQDY
1740
EHVTMLQERF
1750
REFARDTGNI
1760
GQERVDTVNH
1770
MADDLINSGH
1780
SDAATIAEWK
1790
DGLNEAWADL
1800
LELIDTRTQI
1810
LAASYELHKF
1820
YHDAKEIFGR
1830
IQDKHKKLPE
1840
ELGRDQNTVE
1850
TLQRMHTTFE
1860
HDIQALGTQV
1870
RQLQEDAARL
1880
QAAYAGDKAD
1890
DIQKRENEVL
1900
EAWKSLLDAC
1910
EGRRVRLVDT
1920
GDKFRFFSMV
1930
RDLMLWMEDV
1940
IRQIEAQEKP
1950
RDVSSVELLM
1960
NNHQGIKAEI
1970
DARNDSFTAC
1980
IELGKALLAR
1990
KHYASEEIKE
2000
KLLQLTEKRK
2010
EMIDKWEDRW
2020
EWLRLILEVH
2030
QFSRDASVAE
2040
AWLLGQEPYL
2050
SSREIGQSVD
2060
EVEKLIKRHE
2070
AFEKSAATWD
2080
ERFSALERLT
2090
TLELLEVRRQ
2100
QEEEERKRRP
2110
PSPEPSAKVS
2120
EEAESQQWDT
2130
SKGDQVSQNG
2140
LPAEQGSPRM
2150
AGTMETSEMV
2160
NGAAEQRTSS
2170
KESSPVPSPT
2180
SDRKAKSALP
2190
AQSAATLPAR
2200
TLETPAAQME
2210
GFLNRKHEWE
2220
AHNKKASSRS
2230
WHNVYCVINN
2240
QEMGFYKDAK
2250
SAASGVPYHS
2260
EVPVSLKEAI
2270
CEVALDYKKK
2280
KHVFKLRLSD
2290
GNEYLFQAKD
2300
DDEMNTWIQA
2310
ITSAISSDKH
2320
DTSASTQSTP
2330
ASSRAQTLPT
2340
SVVTITSESS
2350
PGKREKDKEK
2360
DKEKRFSLFG
KKK
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0030673 |
axolemma |
| Cellular Component |
GO:0031430 |
M band |
| Cellular Component |
GO:0016020 |
membrane |
| Cellular Component |
GO:0005730 |
nucleolus |
| Cellular Component |
GO:0005634 |
nucleus |
| Cellular Component |
GO:0005886 |
plasma membrane |
| Cellular Component |
GO:0098794 |
postsynapse |
| Cellular Component |
GO:0014069 |
postsynaptic density |
| Cellular Component |
GO:0032991 |
protein-containing complex |
| Cellular Component |
GO:0008091 |
spectrin |
| Molecular Function |
GO:0051015 |
actin filament binding |
| Molecular Function |
GO:0030506 |
ankyrin binding |
| Molecular Function |
GO:0051020 |
GTPase binding |
| Molecular Function |
GO:0005543 |
phospholipid binding |
| Molecular Function |
GO:0044877 |
protein-containing complex binding |
| Molecular Function |
GO:0005200 |
structural constituent of cytoskeleton |
| Biological Process |
GO:0030036 |
actin cytoskeleton organization |
| Biological Process |
GO:0051693 |
actin filament capping |
| Biological Process |
GO:0007417 |
central nervous system development |
| Biological Process |
GO:0021556 |
central nervous system formation |
| Biological Process |
GO:0043001 |
Golgi to plasma membrane protein transport |
| Biological Process |
GO:0071709 |
membrane assembly |
| Biological Process |
GO:0000281 |
mitotic cytokinesis |
| Biological Process |
GO:0007009 |
plasma membrane organization |
| Biological Process |
GO:0032743 |
positive regulation of interleukin-2 production |
| Biological Process |
GO:1903078 |
positive regulation of protein localization to plasma membrane |
| Biological Process |
GO:0072659 |
protein localization to plasma membrane |
| Biological Process |
GO:1903076 |
regulation of protein localization to plasma membrane |
| Biological Process |
GO:0060390 |
regulation of SMAD protein signal transduction |
| Cellular Component |
GO:0030054 |
cell junction |
| Cellular Component |
GO:0042995 |
cell projection |
| Cellular Component |
GO:0030864 |
cortical actin cytoskeleton |
| Cellular Component |
GO:0030863 |
cortical cytoskeleton |
| Cellular Component |
GO:0032437 |
cuticular plate |
| Cellular Component |
GO:0005737 |
cytoplasm |
| Cellular Component |
GO:0005829 |
cytosol |
| Cellular Component |
GO:0098978 |
glutamatergic synapse |
Reference
[1] Yao Y, Bade R, Li G, Zhang A, Zhao H et al.. Global-Scale Profiling of Differential Expressed Lysine-Lactylated Proteins in the Cerebral Endothelium of Cerebral Ischemia-Reperfusion Injury Rats.. Cell Mol Neurobiol 43(5):1989-2004. 2023 Jul. PMID: 36030297.
[2] Sheng L, Xu H, Wang Y, Ni J, Xiang T et al.. Systematic analysis of lysine lactylation in nucleus pulposus cells.. iScience 27(11):111157. 2024 Nov 15. PMID: 39524337.
[3] Chen Y, Sun W, Sun Z, Zhao H, Wu T et al.. Effect of electroacupuncture on hippocampal protein lactylation in a rat model of vascular dementia.. Front Neurol 16:1629474. 2025. PMID: 40963935.