CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004412
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 
Gene Name
 Sptan1 
Gene Synonyms/Alias
 Spna2; Spta2 
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
73VASDENYKDPTNLQGubiquitination[1]
150IKLLQAQKLVQYLREubiquitination[2]
441ASDEVREKLSILSEEubiquitination[1]
633SRIDALEKAGQKLIDubiquitination[1]
814AASTNRGKDLIGVQNubiquitination[2]
909AESWMREKEPIVGSTubiquitination[1]
981ALYDYQEKSPREVTMubiquitination[1]
990PREVTMKKGDILTLLubiquitination[1]
1057DNQTRITKEAGSVSLubiquitination[1]
1419ASPEIKEKLDILDQEubiquitination[1]
2052AAKHIQSKAIEARHAubiquitination[1]
2426EGKPYVTKEELYQNLubiquitination[2]
Reference
 [1] Synaptic protein ubiquitination in rat brain revealed by antibody-based ubiquitome analysis.
 Na CH, Jones DR, Yang Y, Wang X, Xu Y, Peng J.
 J Proteome Res. 2012 Sep 7;11(9):4722-32. [PMID: 22871113]
 [2] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965] 
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 (By similarity). 
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 (By similarity).
 MOD_RES 667 667 Phosphothreonine (By similarity).
 MOD_RES 982 982 Phosphoserine (By similarity).
 MOD_RES 999 999 Phosphoserine (By similarity).
 MOD_RES 1029 1029 Phosphoserine (By similarity).
 MOD_RES 1041 1041 Phosphoserine (By similarity).
 MOD_RES 1176 1176 Phosphotyrosine.
 MOD_RES 1217 1217 Phosphoserine.
 MOD_RES 1519 1519 N6-acetyllysine (By similarity).
 MOD_RES 1647 1647 Phosphoserine (By similarity).
 MOD_RES 2052 2052 N6-acetyllysine (By similarity).
 MOD_RES 2421 2421 N6-acetyllysine (By similarity).  
Keyword
 3D-structure; Acetylation; Actin capping; Actin-binding; Calcium; Calmodulin-binding; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; Metal-binding; Phosphoprotein; 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
QEKLQVASDE NYKDPTNLQG KLQKHQAFEA EVQANSGAIV KLDETGNLMI SEGHFASETI 120
RTRLMELHRQ WELLLEKMRE KGIKLLQAQK LVQYLRECED VMDWINDKEA IVTSEELGQD 180
LEHVEVLQKK FEEFQTDLAA HEERVNEVNQ FAAKLIQEQH PEEELIKTKQ EEVNAAWQRL 240
KGLALQRQGK LFGAAEVQRF NRDVDETIGW IKEKEQLMAS DDFGRDLASV QALLRKHEGL 300
ERDLAALEDK VKALCAEADR LQQSHPLSAN QIQVKREELI TNWEQIRTLA AERHARLDDS 360
YRLQRFLADF RDLTSWVTEM KALINADELA NDVAGAEALL DRHQEHKGEI DAHEDSFKSA 420
DESGQALLAA GHYASDEVRE KLSILSEERA ALLELWELRR QQYEQCMDLQ LFYRDTEQVD 480
NWMSKQEAFL LNEDLGDSLD SVEALLKKHE DFEKSLSAQE EKITALDEFA TKLIQNNHYA 540
MEDVATRRDA LLSRRNALHE RAMHRRAQLA DSFHLQQFFR DSDELKSWVN EKMKTATDEA 600
YKDPSNLQGK VQKHQAFEAE LSANQSRIDA LEKAGQKLID VNHYAKEEVA ARMNEVISLW 660
KKLLEATELK GVKLREANQQ QQFNRNVEDI ELWLYEVEGH LASDDYGKDL TNVQNLQKKH 720
ALLEADVAAH QDRIDGITIQ ARQFQDAGHF DAENIKKKQE ALVARYEALK EPMVARKQKL 780
ADSLRLQQLF RDVEDEETWI REKEPIAAST NRGKDLIGVQ NLLKKHQALQ AEIAGHEPRI 840
KAVTQKGNAM VEEGHFAAED VKAKLSELNQ KWEALKAKAS QRRQDLEDSL QAQQYFADAN 900
EAESWMREKE PIVGSTDYGK DEDSAEALLK KHEALMSDLS AYGSSIQALR EQAQSCRQQV 960
APMDDETGKE LVLALYDYQE KSPREVTMKK GDILTLLNST NKDWWKVEVN DRQGFVPAAY 1020
VKKLDPAQSA SRENLLEEQG SIALRQGQID NQTRITKEAG SVSLRMKQVE ELYQSLLELG 1080
EKRKGMLEKS CKKFMLFREA NELQQWINEK EAALTSEEVG ADLEQVEVLQ KKFDDFQKDL 1140
KANESRLKDI NKVAEDLESE GLMAEEVQAV QQQEVYGMMP RDEADSKTAS PWKSARLMVH 1200
TVATFNSIKE LNERWRSLQQ LAEERSQLLG SAHEVQRFHR DADETKEWIE EKNQALNTDN 1260
YGHDLASVQA LQRKHEGFER DLAALGDKVN SLGETAQRLI QSHPESAEDL KEKCTELNQA 1320
WTSLGKRADQ RKAKLGDSHD LQRFLSDFRD LMSWINGIRG LVSSDELAKD VTGAEALLER 1380
HQEHRTEIDA RAGTFQAFEQ FGQQLLAHGH YASPEIKEKL DILDQERTDL EKAWVQRRMM 1440
LDHCLELQLF HRDCEQAENW MAAREAFLNT EDKGDSLDSV EALIKKHEDF DKAINVQEEK 1500
IAALQAFADQ LIAVDHYAKG DIANRRNEVL DRWRRLKAQM IEKRSKLGES QTLQQFSRDV 1560
DEIEAWISEK LQTASDESYK DPTNIQSKHQ KHQAFEAELH ANADRIRGVI DMGNSLIERG 1620
ACAGSEDAVK ARLAALADQW QFLVQKSAEK SQKLKEANKQ QNFNTGIKDF DFWLSEVEAL 1680
LASEDYGKDL ASVNNLLKKH QLLEADISAH EDRLKDLNSQ ADSLMTSSAF DTSQVKEKRD 1740
TINGRFQKIK SMATSRRAKL SESHRLHQFF RDMDDEESWI KEKKLLVSSE DYGRDLTGVQ 1800
NLRKKHKRLE AELAAHEPAI QGVLDTGKKL SDDNTIGQEE IQQRLAQFVE HWKELKQLAA 1860
ARGQRLEESL EYQQFVANVE EEEAWINEKM TLVASEDYGD TLAAIQGLLK KHEAFETDFT 1920
VHKDRVNDVC TNGQDLIKKN NHHEENISSK MKGLNGKVSD LEKAAAQRKA KLDENSAFLQ 1980
FNWKADVVES WIGEKENSLK TDDYGRDLSS VQTLLTKQET FDAGLQAFQQ EGIANITALK 2040
DQLLAAKHIQ SKAIEARHAS LMKRWTQLLA NSATRKKKLL EAQSHFRKVE DLFLTFAKKA 2100
SAFNSWFENA EEDLTDPVRC NSLEEIKALR EAHDAFRSSL SSAQADFNQL AELDRQIKSF 2160
RVASNPYTWF TMEALEETWR NLQKIIKERE LELQKEQRRQ EENDKLRQEF AQHANAFHQW 2220
IQETRTYLLD GSCMVEESGT LESQLEATKR KHQEIRAMRS QLKKIEDLGA AMEEALILDN 2280
KYTEHSTVGL AQQWDQLDQL GMRMQHNLEQ QIQARNTTGV TEEALKEFSM MFKHFDKDKS 2340
GRLNHQEFKS CLRSLGYDLP MVEEGEPDPE FEAILDTVDP NRDGHVSLQE YMAFMISRET 2400
ENVKSSEEIE SAFRALSSEG KPYVTKEELY QNLTREQADY CVSHMKPYVD GKGRELPTAF 2460
DYVEFTRSLF VN 2472 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005886; C:plasma membrane; IDA:RGD.
 GO:0043234; C:protein complex; IDA:RGD.
 GO:0008091; C:spectrin; TAS:RGD.
 GO:0005509; F:calcium ion binding; IEA:InterPro.
 GO:0031532; P:actin cytoskeleton reorganization; IMP:RGD.
 GO:0051693; P:actin filament capping; IEA:UniProtKB-KW. 
Interpro
 IPR011992; EF-hand-like_dom.
 IPR014837; EF-hand_Ca_insen.
 IPR018247; EF_Hand_1_Ca_BS.
 IPR002048; EF_hand_dom.
 IPR001452; SH3_domain.
 IPR018159; Spectrin/alpha-actinin.
 IPR013315; Spectrin_alpha_SH3.
 IPR002017; Spectrin_repeat. 
Pfam
 PF00036; efhand
 PF08726; efhand_Ca_insen
 PF00018; SH3_1
 PF00435; Spectrin 
SMART
 SM00054; EFh
 SM00326; SH3
 SM00150; SPEC 
PROSITE
 PS00018; EF_HAND_1
 PS50222; EF_HAND_2
 PS50002; SH3 
PRINTS
 PR00452; SH3DOMAIN.
 PR01887; SPECTRNALPHA.