Tag | Content |
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CPLM ID | CPLM-012206 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Spectrin alpha chain, non-erythrocytic 1 |
Protein Synonyms/Alias | Alpha-II spectrin; Fodrin alpha chain; Spectrin, non-erythroid alpha subunit |
Gene Name | SPTAN1 |
Gene Synonyms/Alias | NEAS; SPTA2 |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
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335 | SATQIQVKREELITN | ubiquitination | [1] | 825 | GVQNLLKKHQALQAE | ubiquitination | [1] | 1252 | TKEWIEEKNQALNTD | ubiquitination | [1] | 1288 | DLAALGDKVNSLGET | ubiquitination | [1] | 1369 | VSSDELAKDVTGAEA | ubiquitination | [1] | 1519 | IAAGHYAKGDISSRR | ubiquitination | [1] | 1580 | TASDESYKDPTNIQL | ubiquitination | [1] | 1589 | PTNIQLSKLLSKHQK | ubiquitination | [1] | 1651 | QWQFLVQKSAEKSQK | ubiquitination | [1] | 1843 | SDDNTIGKEEIQQRL | ubiquitination | [1] | 2057 | AAKHVQSKAIEARHA | ubiquitination | [1] |
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Reference | [1] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization. Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW. Nature. 2013 Apr 18;496(7445):372-6. [ PMID: 23503661] |
Functional Description | 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. |
Sequence Annotation | REPEAT 10 42 Spectrin 1. REPEAT 44 147 Spectrin 2. REPEAT 149 253 Spectrin 3. REPEAT 255 359 Spectrin 4. REPEAT 361 465 Spectrin 5. REPEAT 467 571 Spectrin 6. REPEAT 573 676 Spectrin 7. REPEAT 678 782 Spectrin 8. REPEAT 784 888 Spectrin 9. REPEAT 890 955 Spectrin 10. DOMAIN 967 1026 SH3. REPEAT 1062 1089 Spectrin 11. REPEAT 1091 1161 Spectrin 12. REPEAT 1208 1231 Spectrin 13. REPEAT 1233 1337 Spectrin 14. REPEAT 1339 1443 Spectrin 15. REPEAT 1445 1549 Spectrin 16. REPEAT 1551 1656 Spectrin 17. REPEAT 1658 1762 Spectrin 18. REPEAT 1764 1868 Spectrin 19. REPEAT 1870 1974 Spectrin 20. REPEAT 1976 2081 Spectrin 21. REPEAT 2091 2195 Spectrin 22. REPEAT 2205 2310 Spectrin 23. DOMAIN 2323 2358 EF-hand 1. DOMAIN 2366 2401 EF-hand 2. DOMAIN 2404 2439 EF-hand 3. MOD_RES 637 637 N6-acetyllysine. MOD_RES 667 667 Phosphothreonine (By similarity). MOD_RES 982 982 Phosphoserine. MOD_RES 999 999 Phosphoserine. MOD_RES 1029 1029 Phosphoserine (By similarity). MOD_RES 1041 1041 Phosphoserine. MOD_RES 1176 1176 Phosphotyrosine. MOD_RES 1217 1217 Phosphoserine. MOD_RES 1519 1519 N6-acetyllysine. MOD_RES 1647 1647 Phosphoserine. MOD_RES 2052 2052 N6-acetyllysine. MOD_RES 2421 2421 N6-acetyllysine. |
Keyword | 3D-structure; Acetylation; Actin capping; Actin-binding; Alternative splicing; Calcium; Calmodulin-binding; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; Disease mutation; Epilepsy; Mental retardation; Metal-binding; Phosphoprotein; Polymorphism; Reference proteome; Repeat; SH3 domain. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 2472 AA |
Protein Sequence | MDPSGVKVLE TAEDIQERRQ QVLDRYHRFK ELSTLRRQKL EDSYRFQFFQ RDAEELEKWI 60 QEKLQIASDE NYKDPTNLQG KLQKHQAFEA EVQANSGAIV KLDETGNLMI SEGHFASETI 120 RTRLMELHRQ WELLLEKMRE KGIKLLQAQK LVQYLRECED VMDWINDKEA IVTSEELGQD 180 LEHVEVLQKK FEEFQTDMAA HEERVNEVNQ FAAKLIQEQH PEEELIKTKQ DEVNAAWQRL 240 KGLALQRQGK LFGAAEVQRF NRDVDETISW IKEKEQLMAS DDFGRDLASV QALLRKHEGL 300 ERDLAALEDK VKALCAEADR LQQSHPLSAT QIQVKREELI TNWEQIRTLA AERHARLNDS 360 YRLQRFLADF RDLTSWVTEM KALINADELA SDVAGAEALL DRHQEHKGEI DAHEDSFKSA 420 DESGQALLAA GHYASDEVRE KLTVLSEERA ALLELWELRR QQYEQCMDLQ LFYRDTEQVD 480 NWMSKQEAFL LNEDLGDSLD SVEALLKKHE DFEKSLSAQE EKITALDEFA TKLIQNNHYA 540 MEDVATRRDA LLSRRNALHE RAMRRRAQLA DSFHLQQFFR DSDELKSWVN EKMKTATDEA 600 YKDPSNLQGK VQKHQAFEAE LSANQSRIDA LEKAGQKLID VNHYAKDEVA ARMNEVISLW 660 KKLLEATELK GIKLREANQQ QQFNRNVEDI ELWLYEVEGH LASDDYGKDL TNVQNLQKKH 720 ALLEADVAAH QDRIDGITIQ ARQFQDAGHF DAENIKKKQE ALVARYEALK EPMVARKQKL 780 ADSLRLQQLF RDVEDEETWI REKEPIAAST NRGKDLIGVQ NLLKKHQALQ AEIAGHEPRI 840 KAVTQKGNAM VEEGHFAAED VKAKLHELNQ KWEALKAKAS QRRQDLEDSL QAQQYFADAN 900 EAESWMREKE PIVGSTDYGK DEDSAEALLK KHEALMSDLS AYGSSIQALR EQAQSCRQQV 960 APTDDETGKE LVLALYDYQE KSPREVTMKK GDILTLLNST NKDWWKVEVN DRQGFVPAAY 1020 VKKLDPAQSA SRENLLEEQG SIALRQEQID NQTRITKEAG SVSLRMKQVE ELYHSLLELG 1080 EKRKGMLEKS CKKFMLFREA NELQQWINEK EAALTSEEVG ADLEQVEVLQ KKFDDFQKDL 1140 KANESRLKDI NKVAEDLESE GLMAEEVQAV QQQEVYGMMP RDETDSKTAS PWKSARLMVH 1200 TVATFNSIKE LNERWRSLQQ LAEERSQLLG SAHEVQRFHR DADETKEWIE EKNQALNTDN 1260 YGHDLASVQA LQRKHEGFER DLAALGDKVN SLGETAERLI QSHPESAEDL QEKCTELNQA 1320 WSSLGKRADQ RKAKLGDSHD LQRFLSDFRD LMSWINGIRG LVSSDELAKD VTGAEALLER 1380 HQEHRTEIDA RAGTFQAFEQ FGQQLLAHGH YASPEIKQKL DILDQERADL EKAWVQRRMM 1440 LDQCLELQLF HRDCEQAENW MAAREAFLNT EDKGDSLDSV EALIKKHEDF DKAINVQEEK 1500 IAALQAFADQ LIAAGHYAKG DISSRRNEVL DRWRRLKAQM IEKRSKLGES QTLQQFSRDV 1560 DEIEAWISEK LQTASDESYK DPTNIQLSKL LSKHQKHQAF EAELHANADR IRGVIDMGNS 1620 LIERGACAGS EDAVKARLAA LADQWQFLVQ KSAEKSQKLK EANKQQNFNT GIKDFDFWLS 1680 EVEALLASED YGKDLASVNN LLKKHQLLEA DISAHEDRLK DLNSQADSLM TSSAFDTSQV 1740 KDKRDTINGR FQKIKSMAAS RRAKLNESHR LHQFFRDMDD EESWIKEKKL LVGSEDYGRD 1800 LTGVQNLRKK HKRLEAELAA HEPAIQGVLD TGKKLSDDNT IGKEEIQQRL AQFVEHWKEL 1860 KQLAAARGQR LEESLEYQQF VANVEEEEAW INEKMTLVAS EDYGDTLAAI QGLLKKHEAF 1920 ETDFTVHKDR VNDVCTNGQD LIKKNNHHEE NISSKMKGLN GKVSDLEKAA AQRKAKLDEN 1980 SAFLQFNWKA DVVESWIGEK ENSLKTDDYG RDLSSVQTLL TKQETFDAGL QAFQQEGIAN 2040 ITALKDQLLA AKHVQSKAIE ARHASLMKRW SQLLANSAAR KKKLLEAQSH FRKVEDLFLT 2100 FAKKASAFNS WFENAEEDLT DPVRCNSLEE IKALREAHDA FRSSLSSAQA DFNQLAELDR 2160 QIKSFRVASN PYTWFTMEAL EETWRNLQKI IKERELELQK EQRRQEENDK LRQEFAQHAN 2220 AFHQWIQETR TYLLDGSCMV EESGTLESQL EATKRKHQEI RAMRSQLKKI EDLGAAMEEA 2280 LILDNKYTEH STVGLAQQWD QLDQLGMRMQ HNLEQQIQAR NTTGVTEEAL KEFSMMFKHF 2340 DKDKSGRLNH QEFKSCLRSL GYDLPMVEEG EPDPEFEAIL DTVDPNRDGH VSLQEYMAFM 2400 ISRETENVKS SEEIESAFRA LSSEGKPYVT KEELYQNLTR EQADYCVSHM KPYVDGKGRE 2460 LPTAFDYVEF TRSLFVN 2477 |
Gene Ontology | GO:0032437; C:cuticular plate; IEA:Compara. GO:0005829; C:cytosol; TAS:Reactome. GO:0005916; C:fascia adherens; IEA:Compara. GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. GO:0016328; C:lateral plasma membrane; IEA:Compara. GO:0016020; C:membrane; TAS:ProtInc. GO:0015630; C:microtubule cytoskeleton; IDA:HPA. GO:0008091; C:spectrin; TAS:ProtInc. GO:0030018; C:Z disc; IEA:Compara. GO:0003779; F:actin binding; TAS:ProtInc. GO:0005509; F:calcium ion binding; IEA:InterPro. GO:0005200; F:structural constituent of cytoskeleton; TAS:ProtInc. GO:0051693; P:actin filament capping; IEA:UniProtKB-KW. GO:0007411; P:axon guidance; TAS:Reactome. GO:0006921; P:cellular component disassembly involved in execution phase of apoptosis; TAS:Reactome. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |