CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019575
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Sperm-associated antigen 5 
Protein Synonyms/Alias
 Astrin; Deepest; Mitotic spindle-associated protein p126; MAP126 
Gene Name
 SPAG5 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
41GALTNSGKRSPACSSubiquitination[1]
74PVDFVNNKRTDLSSEubiquitination[1]
396TPSAPQEKSTNTSQTubiquitination[1]
409QTGLVGTKHSTSETEubiquitination[1]
483SHSGITNKLQHLKESubiquitination[2, 3, 4]
488TNKLQHLKESHEMGQubiquitination[1, 2, 3]
552CCFDLLKKLRAKLQSubiquitination[1]
578EEMALRGKDAAEIVLubiquitination[1, 4]
614REFRGLLKDAQTQLVubiquitination[1, 4]
668RSRQLTEKLTVKSQQubiquitination[1]
672LTEKLTVKSQQALQEubiquitination[1]
687RDVAIEEKQEVSRVLubiquitination[1]
794QQQAVLAKEVRDLKEubiquitination[1]
866NQEQDLEKTRQYSQKubiquitination[1]
1021EQHQEVQKAKEADIEubiquitination[1]
1023HQEVQKAKEADIEKLacetylation[5]
1023HQEVQKAKEADIEKLubiquitination[1]
1029AKEADIEKLNQALCLacetylation[5]
1121WLSQEVDKLRVMFLEubiquitination[1]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [3] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [4] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [5] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786] 
Functional Description
 Essential component of the mitotic spindle required for normal chromosome segregation and progression into anaphase. Required for chromosome alignment, normal timing of sister chromatid segregation, and maintenance of spindle pole architecture. The astrin (SPAG5)-kinastrin (SKAP) complex promotes stable microtubule-kinetochore attachments. 
Sequence Annotation
 REGION 482 850 Interaction with KNSTRN.
 MOD_RES 12 12 Phosphoserine (By similarity).
 MOD_RES 14 14 Phosphoserine (By similarity).
 MOD_RES 43 43 Phosphoserine.
 MOD_RES 62 62 Phosphoserine.
 MOD_RES 66 66 Phosphoserine.
 MOD_RES 135 135 Phosphoserine.
 MOD_RES 334 334 Phosphoserine.
 MOD_RES 336 336 Phosphothreonine.
 MOD_RES 341 341 Phosphoserine.
 MOD_RES 362 362 Phosphoserine.  
Keyword
 Cell cycle; Cell division; Centromere; Chromosome; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Kinetochore; Microtubule; Mitosis; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1193 AA 
Protein Sequence
MWRVKKLSLS LSPSPQTGKP SMRTPLRELT LQPGALTNSG KRSPACSSLT PSLCKLGLQE 60
GSNNSSPVDF VNNKRTDLSS EHFSHSSKWL ETCQHESDEQ PLDPIPQISS TPKTSEEAVD 120
PLGNYMVKTI VLVPSPLGQQ QDMIFEARLD TMAETNSISL NGPLRTDDLV REEVAPCMGD 180
RFSEVAAVSE KPIFQESPSH LLEESPPNPC SEQLHCSKES LSSRTEAVRE DLVPSESNAF 240
LPSSVLWLSP STALAADFRV NHVDPEEEIV EHGAMEEREM RFPTHPKESE TEDQALVSSV 300
EDILSTCLTP NLVEMESQEA PGPAVEDVGR ILGSDTESWM SPLAWLEKGV NTSVMLENLR 360
QSLSLPSMLR DAAIGTTPFS TCSVGTWFTP SAPQEKSTNT SQTGLVGTKH STSETEQLLC 420
GRPPDLTALS RHDLEDNLLS SLVILEVLSR QLRDWKSQLA VPHPETQDSS TQTDTSHSGI 480
TNKLQHLKES HEMGQALQQA RNVMQSWVLI SKELISLLHL SLLHLEEDKT TVSQESRRAE 540
TLVCCCFDLL KKLRAKLQSL KAEREEARHR EEMALRGKDA AEIVLEAFCA HASQRISQLE 600
QDLASMREFR GLLKDAQTQL VGLHAKQEEL VQQTVSLTST LQQDWRSMQL DYTTWTALLS 660
RSRQLTEKLT VKSQQALQER DVAIEEKQEV SRVLEQVSAQ LEECKGQTEQ LELENSRLAT 720
DLRAQLQILA NMDSQLKELQ SQHTHCAQDL AMKDELLCQL TQSNEEQAAQ WQKEEMALKH 780
MQAELQQQQA VLAKEVRDLK ETLEFADQEN QVAHLELGQV ECQLKTTLEV LRERSLQCEN 840
LKDTVENLTA KLASTIADNQ EQDLEKTRQY SQKLGLLTEQ LQSLTLFLQT KLKEKTEQET 900
LLLSTACPPT QEHPLPNDRT FLGSILTAVA DEEPESTPVP LLGSDKSAFT RVASMVSLQP 960
AETPGMEESL AEMSIMTTEL QSLCSLLQES KEEAIRTLQR KICELQARLQ AQEEQHQEVQ 1020
KAKEADIEKL NQALCLRYKN EKELQEVIQQ QNEKILEQID KSGELISLRE EVTHLTRSLR 1080
RAETETKVLQ EALAGQLDSN CQPMATNWIQ EKVWLSQEVD KLRVMFLEMK NEKEKLMIKF 1140
QSHRNILEEN LRRSDKELEK LDDIVQHIYK TLLSIPEVVR GCKELQGLLE FLS 1193 
Gene Ontology
 GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0000776; C:kinetochore; IDA:UniProtKB.
 GO:0035371; C:microtubule plus end; IDA:UniProtKB.
 GO:0072686; C:mitotic spindle; IDA:UniProtKB.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0005876; C:spindle microtubule; IEA:Compara.
 GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0000090; P:mitotic anaphase; IMP:UniProtKB.
 GO:0000070; P:mitotic sister chromatid segregation; IMP:UniProtKB.
 GO:0048015; P:phosphatidylinositol-mediated signaling; NAS:UniProtKB.
 GO:0051988; P:regulation of attachment of spindle microtubules to kinetochore; IMP:UniProtKB.
 GO:0007051; P:spindle organization; IMP:UniProtKB. 
Interpro
  
Pfam
  
SMART
  
PROSITE
  
PRINTS