CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-028958
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Spectrin alpha chain, non-erythrocytic 1 
Protein Synonyms/Alias
  
Gene Name
 Sptan1 
Gene Synonyms/Alias
 Spna2 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
190HVEVLQKKFEEFQTDacetylation[1]
441ASDEVREKLSILSEEubiquitination[2]
514KKHEDFEKSLSAQEEubiquitination[2]
532ALDEFATKLIQNNHYacetylation[1]
602TATDEAYKDPSNLQGacetylation[1]
613NLQGKVQKHQAFEAEacetylation[1]
633SRIDALEKAGQKLIDubiquitination[2]
646IDVNHYAKEEVAARMacetylation[1]
718TNVQNLQKKHALLEAubiquitination[2]
719NVQNLQKKHALLEADacetylation[1]
803EETWIREKEPIAASTacetylation[3]
803EETWIREKEPIAASTubiquitination[2]
814AASTNRGKDLIGVQNubiquitination[2]
824IGVQNLLKKHQALQAubiquitination[2]
825GVQNLLKKHQALQAEacetylation[1]
909AESWMREKEPIVGSTubiquitination[2]
920VGSTDYGKDEDSAEAubiquitination[2]
969PMDDETGKELVLALYubiquitination[2]
981ALYDYQEKSPREVTMubiquitination[2]
990PREVTMKKGDILTLLubiquitination[2]
1022FVPAAYVKKLDPAQSubiquitination[2]
1118KKFDDFQKDLKANESubiquitination[2]
1132SRLKDINKVAEDLESubiquitination[2]
1167PRDEADSKTASPWKSubiquitination[2]
1268DLAALGDKVNSLGETubiquitination[2]
1349VSSDELAKDVTGAEAubiquitination[2]
1399ASPEIKEKLDILDQEubiquitination[2]
1453AFLNTEDKGDSLDSVubiquitination[2]
1526QMIEKRSKLGESQTLubiquitination[2]
1560TASDESYKDPTNIQLubiquitination[2]
1615AGSEDAVKARLAALAubiquitination[2]
1631QWQFLVQKSAEKSQKubiquitination[2]
1684SVNNLLKKHQLLEADacetylation[1]
1700SAHEDRLKDLNSQADubiquitination[2]
1814GVLDTGKKLSDDNTIubiquitination[2]
1838AQFVEHWKELKQLAAacetylation[1]
1896AIQGLLKKHEAFETDacetylation[1]
1980VESWIGEKENSLKTDubiquitination[2]
2032KDQLLAAKHIQSKAIubiquitination[2]
2037AAKHIQSKAIEARHAubiquitination[2]
2063NSATRKKKLLEAQSHacetylation[1]
2073EAQSHFRKVEDLFLTubiquitination[2]
2112CNSLEEIKALREAHDubiquitination[2]
2318KEFSMMFKHFDKDKSacetylation[1]
2334RLNHQEFKSCLRSLGacetylation[1]
2389SRETENVKSSEEIESubiquitination[2]
2406RALSSEGKPYVTKEEacetylation[1]
2411EGKPYVTKEELYQNLacetylation[1]
2411EGKPYVTKEELYQNLubiquitination[2]
2431DYCVSHMKPYVDGKGacetylation[1]
2431DYCVSHMKPYVDGKGubiquitination[2]
2437MKPYVDGKGRELPTAubiquitination[2]
Reference
 [1] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [2] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [3] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337] 
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2457 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 HEERVNEVSQ FAAKLIQEQH PEEELIKTKQ DEVNAAWQRL 240
KGLALQRQGK LFGAAEVQRF NRDVDETIGW IKEKEQLMAS DDFGRDLASV QALLRKHEGL 300
ERDLAALEDK VKALCAEADR LQQSHPLSAS QIQVKREELI TNWEQIRTLA AERHARLDDS 360
YRLQRFLADF RDLTSWVTEM KALINADELA NDVAGAEALL DRHQEHKGEI DAHEDSFKSA 420
DESGQALLAA SHYASDEVRE KLSILSEERT 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 GIKLREANQQ 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 NQYQSLLELG EKRKGMLEKS CKKFMLFREA 1080
NELQQWITEK EAALTNEEVG ADLEQVEVLQ KKFDDFQKDL KANESRLKDI NKVAEDLESE 1140
GLMAEEVQAV QQQEVYGAMP RDEADSKTAS PWKSARLMVH TVATFNSIKE LNERWRSLQQ 1200
LAEERSQLLG SAHEVQRFHR DADETKEWIE EKNQALNTDN YGHDLASVQA LQRKHEGFER 1260
DLAALGDKVN SLGETAQRLI QSHPESAEDL KEKCTELNQA WTSLGKRADQ RKAKLGDSHD 1320
LQRFLSDFRD LMSWINGIRG LVSSDELAKD VTGAEALLER HQEHRTEIDA RAGTFQAFEQ 1380
FGQQLLAHGH YASPEIKEKL DILDQERTDL EKAWVQRRMM LDHCLELQLF HRDCEQAENW 1440
MAAREAFLNT EDKGDSLDSV EALIKKHEDF DKAINVQEEK IAALQAFADQ LIAVDHYAKG 1500
DIANRRNEVL DRWRRLKAQM IEKRSKLGES QTLQQFSRDV DEIEAWISEK LQTASDESYK 1560
DPTNIQLSKL LSKHQKHQAF EAELHANADR IRGVIDMGNS LIERGACAGS EDAVKARLAA 1620
LADQWQFLVQ KSAEKSQKLK EANKQQNFNT GIKDFDFWLS EVEALLASED YGKDLASVNN 1680
LLKKHQLLEA DISAHEDRLK DLNSQADSLM TSSAFDTSQV KEKRDTINGR FQKIKSMATS 1740
RRAKLSESHR LHQFFRDMDD EESWIKEKKL LVSSEDYGRD LTGVQNLRKK HKRLEAELAA 1800
HEPAIQGVLD TGKKLSDDNT IGQEEIQQRL AQFVEHWKEL KQLAAARGQR LEESLEYQQF 1860
VANVEEEEAW INEKMTLVAS EDYGDTLAAI QGLLKKHEAF ETDFTVHKDR VNDVCTNGQD 1920
LIKKNNHHEE NISSKMKGLN GKVSDLEKAA AQRKAKLDEN SAFLQFNWKA DVVESWIGEK 1980
ENSLKTDDYG RDLSSVQTLL TKQETFDAGL QAFQQEGIAN ITALKDQLLA AKHIQSKAIE 2040
ARHASLMKRW TQLLANSATR KKKLLEAQSH FRKVEDLFLT FAKKASAFNS WFENAEEDLT 2100
DPVRCNSLEE IKALREAHDA FRSSLSSAQA DFNQLAELDR QIKSFRVASN PYTWFTMEAL 2160
EETWRNLQKI IKERELELQK EQRRQEENDK LRQEFAQHAN AFHQWIQETR TYLLDGSCMV 2220
EESGTLESQL EATKRKHQEI RAMRSQLKKI EDLGAAMEEA LILDNKYTEH STVGLAQQWD 2280
QLDQLGMRMQ HNLEQQIQAR NTTGVTEEAL KEFSMMFKHF DKDKSGRLNH QEFKSCLRSL 2340
GYDLPMVEEG EPDPEFEAIL DTVDPNRDGH VSLQEYMAFM ISRETENVKS SEEIESAFRA 2400
LSSEGKPYVT KEELYQNLTR EQADYCVSHM KPYVDGKGRE LPTAFDYVEF TRSLFVN 2457 
Gene Ontology
 GO:0032437; C:cuticular plate; IDA:MGI.
 GO:0005916; C:fascia adherens; IDA:MGI.
 GO:0016328; C:lateral plasma membrane; IDA:MGI.
 GO:0030018; C:Z disc; IDA:MGI.
 GO:0005509; F:calcium ion binding; IEA:InterPro.
 GO:0046982; F:protein heterodimerization activity; IDA:MGI.
 GO:0030507; F:spectrin binding; IDA:MGI. 
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
 PF13499; EF_hand_5
 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.