CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-017646
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Structural maintenance of chromosomes protein 1B 
Protein Synonyms/Alias
 SMC protein 1B; SMC-1-beta; SMC-1B 
Gene Name
 SMC1B 
Gene Synonyms/Alias
 SMC1L2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
38IGPNGSGKSNVMDALubiquitination[1]
92VEESGEEKTFARIIRubiquitination[1]
177EKKRKLQKAEEDAQFubiquitination[1]
188DAQFNFNKKKNIAAEubiquitination[1]
190QFNFNKKKNIAAERRubiquitination[1]
234QLYHNEKKIHLLNTKacetylation[2]
234QLYHNEKKIHLLNTKubiquitination[1]
241KIHLLNTKLEHVNRDacetylation[2]
252VNRDLSVKRESLSHHacetylation[2]
294VETLLNQKRPQYIKAubiquitination[1]
395TMTQQLEKLQWEQKTubiquitination[1]
495GIDTHEGKRQQKRAEubiquitination[1]
508AEVLEHLKRLYPDSVubiquitination[1]
529LCHPIHKKYQLAVTKubiquitination[1, 3]
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] 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]
 [3] 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] 
Functional Description
 Meiosis-specific component of cohesin complex. Required for the maintenance of meiotic cohesion, but not, or only to a minor extent, for its establishment. Contributes to axial element (AE) formation and the organization of chromatin loops along the AE. Plays a key role in synapsis, recombination and chromosome movements. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. The meiosis-specific cohesin complex probably replaces mitosis specific cohesin complex when it dissociates from chromatin during prophase I (By similarity). 
Sequence Annotation
 NP_BIND 32 39 ATP (Potential).
 REGION 491 665 Flexible hinge.  
Keyword
 Alternative splicing; ATP-binding; Cell cycle; Centromere; Chromosome; Coiled coil; Complete proteome; Meiosis; Nucleotide-binding; Nucleus; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1235 AA 
Protein Sequence
MAHLELLLVE NFKSWRGRQV IGPFRRFTCI IGPNGSGKSN VMDALSFVMG EKIANLRVKN 60
IQELIHGAHI GKPISSSASV KIIYVEESGE EKTFARIIRG GCSEFRFNDN LVSRSVYIAE 120
LEKIGIIVKA QNCLVFQGTV ESISVKKPKE RTQFFEEIST SGELIGEYEE KKRKLQKAEE 180
DAQFNFNKKK NIAAERRQAK LEKEEAERYQ SLLEELKMNK IQLQLFQLYH NEKKIHLLNT 240
KLEHVNRDLS VKRESLSHHE NIVKARKKEH GMLTRQLQQT EKELKSVETL LNQKRPQYIK 300
AKENTSHHLK KLDVAKKSIK DSEKQCSKQE DDIKALETEL ADLDAAWRSF EKQIEEEILH 360
KKRDIELEAS QLDRYKELKE QVRKKVATMT QQLEKLQWEQ KTDEERLAFE KRRHGEVQGN 420
LKQIKEQIED HKKRIEKLEE YTKTCMDCLK EKKQQEETLV DEIEKTKSRM SEFNEELNLI 480
RSELQNAGID THEGKRQQKR AEVLEHLKRL YPDSVFGRLF DLCHPIHKKY QLAVTKVFGR 540
FITAIVVASE KVAKDCIRFL KEERAEPETF LALDYLDIKP INERLRELKG CKMVIDVIKT 600
QFPQLKKVIQ FVCGNGLVCE TMEEARHIAL SGPERQKTVA LDGTLFLKSG VISGGSSDLK 660
YKARCWDEKE LKNLRDRRSQ KIQELKGLMK TLRKETDLKQ IQTLIQGTQT RLKYSQNELE 720
MIKKKHLVAF YQEQSQLQSE LLNIESQCIM LSEGIKERQR RIKEFQEKID KVEDDIFQHF 780
CEEIGVENIR EFENKHVKRQ QEIDQKRYFY KKMLTRLNVQ LEYSRSHLKK KLNKINTLKE 840
TIQKGSEDID HLKKAEENCL QTVNELMAKQ QQLKDIRVTQ NSSAEKVQTQ IEEERKKFLA 900
VDREVGKLQK EVVSIQTSLE QKRLEKHNLL LDCKVQDIEI ILLSGSLDDI IEVEMGTEAE 960
STQATIDIYE KEEAFEIDYS SLKEDLKALQ SDQEIEAHLR LLLQQVASQE DILLKTAAPN 1020
LRALENLKTV RDKFQESTDA FEASRKEARL CRQEFEQVKK RRYDLFTQCF EHVSISIDQI 1080
YKKLCRNNSA QAFLSPENPE EPYLEGISYN CVAPGKRFMP MDNLSGGEKC VAALALLFAV 1140
HSFRPAPFFV LDEVDAALDN TNIGKVSSYI KEQTQDQFQM IVISLKEEFY SRADALIGIY 1200
PEYDDCMFSR VLTLDLSQYP DTEGQESSKR HGESR 1235 
Gene Ontology
 GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
 GO:0000800; C:lateral element; IEA:Compara.
 GO:0030893; C:meiotic cohesin complex; IDA:UniProtKB.
 GO:0034991; C:nuclear meiotic cohesin complex; IEA:Compara.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0003677; F:DNA binding; IEA:Compara.
 GO:0030261; P:chromosome condensation; IEA:InterPro.
 GO:0006310; P:DNA recombination; IEA:InterPro.
 GO:0006281; P:DNA repair; IEA:InterPro.
 GO:0007126; P:meiosis; IEA:UniProtKB-KW.
 GO:0007062; P:sister chromatid cohesion; IEA:Compara. 
Interpro
 IPR027417; P-loop_NTPase.
 IPR003395; RecF/RecN/SMC.
 IPR024704; SMC.
 IPR010935; SMC_hinge. 
Pfam
 PF06470; SMC_hinge
 PF02463; SMC_N 
SMART
 SM00968; SMC_hinge 
PROSITE
  
PRINTS