Search Results
Overview
| Uniprot ID | A0A287BDN2 |
|---|---|
| Protein Name | Spectrin beta chain |
| Gene Name | SPTBN1 |
| Organism | Sus scrofa |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 1332 | SNKEWLDKIEKEGMQ |
| 1460 | STDEVDSKRLTVQTK |
| 1685 | DKLYAGLKDLAEERR |
| 1810 | AASYELHKFYHDAKE |
| 1816 | HKFYHDAKEIFGRIQ |
| 1879 | QAAYAGDKADDIQKR |
| 1885 | DKADDIQKRENEVLE |
| 1914 | RLVDTGDKFRFFSMV |
| 1982 | GKSLLARKHYASEEI |
| 1992 | ASEEIKEKLLQLTDK |
| 224 | PDLIDFDKLKKSNAH |
| 288 | KALAVEGKRIGKVLD |
| 46 | LFERSRIKALADERE |
| 463 | AVEAATKKHEAIETD |
| 659 | GWIREKEKILSSDDY |
| 832 | AGIEERYKEVAELTR |
| 842 | AELTRLRKQALQDTL |
| 932 | EIKAQQDKLNTRWSQ |
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
ENYHDIKRIT
510
ARKDNVIRLW
520
EYLLELLRAR
530
RQRLEMNLGL
540
QKIFQEMLYI
550
MDWMDEMKVL
560
LLSQDYGKHL
570
LGVEDLLQKH
580
ALVEADIGIQ
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
GSEKIRERIA
730
YIREQWAHLE
740
QLSAIRKKRL
750
EEASLLHQFQ
760
ADADDIDAWM
770
LDILKIVSSN
780
DVGHDEYSTQ
790
SLVKKHKDVA
800
EEIANYRPTI
810
DSLHEQAGAL
820
PQEHAESPDV
830
RGRLAGIEER
840
YKEVAELTRL
850
RKQALQDTLA
860
LYKMFSEADA
870
CELWIDEKEQ
880
WLNNMQIPEK
890
LEDLEVIQHR
900
FESLEPEMNN
910
QASRVAVVNQ
920
IARQLMHSGH
930
PSEKEIKAQQ
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
LRNREASLGE
1070
ASKLQQFLRD
1080
LDDFQSWLSR
1090
TQTAIASEDM
1100
PNTLTEAEKL
1110
LTQHENIKNE
1120
IDNYEEDYQK
1130
MRDMGEMVTQ
1140
GQTDAQYMFL
1150
RQRLQALDTG
1160
WNELHKMWEN
1170
RQNLLSQSHA
1180
HQQFLRDTKQ
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
KQQAMLENQM
1440
EVRKKEIEEL
1450
QSQAQALSQE
1460
GKSTDEVDSK
1470
RLTVQTKFME
1480
LLEPLNERKQ
1490
NLLASKEIHQ
1500
FNRDVEDEIL
1510
WVGERMPLAT
1520
STDHGHNLQT
1530
VQLLIKKNQT
1540
LQKEIQGHQP
1550
RIDDIFERSQ
1560
NIVADSSSLS
1570
AEAIRQRLAD
1580
LKQLWGQLIE
1590
ETEKRHRRLE
1600
EAHRAQQYYF
1610
DAAEAEAWMS
1620
EQELYMMSEE
1630
KAKDEQSAVS
1640
MLKKHQILEQ
1650
AVEDYAETVH
1660
QLSKTSRALV
1670
ADSHPESERI
1680
SMRQSKVDKL
1690
YAGLKDLAEE
1700
RRGKLDERHR
1710
LFQLNREVDD
1720
LEQWIAEREV
1730
VAGSHELGQD
1740
YEHVTMLQER
1750
FREFARDTGN
1760
IGQERVDTVN
1770
HMADELINSG
1780
HSDAATIAEW
1790
KDGLNEAWAD
1800
LLELIDTRTQ
1810
ILAASYELHK
1820
FYHDAKEIFG
1830
RIQDKHKKLP
1840
EELGRDQNTV
1850
ETLQRMHTTF
1860
EHDIQALGTQ
1870
VRQLQEDAAR
1880
LQAAYAGDKA
1890
DDIQKRENEV
1900
LEAWKALLDA
1910
CEGRRVRLVD
1920
TGDKFRFFSM
1930
VRDLMLWMED
1940
VIRQIEAQEK
1950
PRDVSSVELL
1960
MNNHQGIKAE
1970
IDARNDSFTT
1980
CIELGKSLLA
1990
RKHYASEEIK
2000
EKLLQLTDKR
2010
KEMIDKWEDR
2020
WEWLRLILEV
2030
HQFSRDASVA
2040
EAWLLGQEPY
2050
LSSREIGQSV
2060
DEVEKLIKRH
2070
EAFEKSAATW
2080
DERFSALERL
2090
TTLELLEVRR
2100
QQEEEERKRR
2110
PPSPEPSTKV
2120
SEETESQQQW
2130
DTSKGEQVSQ
2140
NGLPTEQGSP
2150
RMAETVDTSE
2160
MVNGAAEQRT
2170
SSKESSPIPS
2180
PTSDRKAKTS
2190
LPAQSAATLP
2200
ARTQETPSAQ
2210
MEGFLNRKHE
2220
WEAHNKKASS
2230
RSWHNVYCVI
2240
NNQEMGFYKD
2250
AKTAASGIPY
2260
HSEVPVSLKE
2270
AICEVALDYK
2280
KKKHVFKLRL
2290
NDGNEYLFQA
2300
KDDEEMNTWI
2310
QAISSAISSD
2320
KHEVSASTQS
2330
TPASSRAQTL
2340
PTSAVTITSE
2350
SSPGKREKDK
2360
EKDKEKRFSL
FGKKK
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0030673 | axolemma |
| Cellular Component | GO:0030054 | cell junction |
| Cellular Component | GO:0042995 | cell projection |
| Cellular Component | GO:0030864 | cortical actin cytoskeleton |
| Cellular Component | GO:0032437 | cuticular plate |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0031430 | M band |
| Cellular Component | GO:0005730 | nucleolus |
| Cellular Component | GO:0005886 | plasma membrane |
| Cellular Component | GO:0014069 | postsynaptic density |
| Cellular Component | GO:0008091 | spectrin |
| Molecular Function | GO:0051015 | actin filament binding |
| Molecular Function | GO:0030506 | ankyrin binding |
| Molecular Function | GO:0005516 | calmodulin binding |
| Molecular Function | GO:0051020 | GTPase binding |
| Molecular Function | GO:0005543 | phospholipid 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: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 |
Reference
[1] Fan S, Zhou R, Wen H, Ye H, Ma S et al.. Global profiling of protein lactylome in porcine granulosa cells.. J Ovarian Res 18(1):177. 2025 Aug 8. PMID: 40781717.