CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015996
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Schlafen family member 11 
Protein Synonyms/Alias
  
Gene Name
 SLFN11 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
97LQAFFETKQQGRCFYubiquitination[1]
153REAFCFLKTKRKPKIacetylation[2]
153REAFCFLKTKRKPKIubiquitination[1]
168LEEGPFHKIHKGVYQubiquitination[1]
171GPFHKIHKGVYQELPubiquitination[1]
221EFKQFSTKHFQEYVKubiquitination[1]
228KHFQEYVKRTIPEYVubiquitination[1]
253LFIGVDDKSREVLGCubiquitination[1]
262REVLGCAKENVDPDSubiquitination[1]
273DPDSLRRKIEQAIYKubiquitination[1]
391KKGLEHKKELQQLLFubiquitination[3]
429GLEELINKQMQPFFRubiquitination[1, 4]
495TRTAFTLKQKLVNMGubiquitination[1]
497TAFTLKQKLVNMGGYubiquitination[1]
507NMGGYTGKVCVRAKVubiquitination[1]
605HGLPGSGKTIMAMKIubiquitination[1]
685GDWYGKAKSITRRAKubiquitination[1]
739RNADPIAKYLQKEMQubiquitination[1, 2]
743PIAKYLQKEMQVIRSubiquitination[1, 2, 3, 4]
807FDRGYSPKDVAVLVSubiquitination[1, 2, 3]
817AVLVSTAKEVEHYKYubiquitination[1]
823AKEVEHYKYELLKAMubiquitination[1, 2, 3]
890ICLASRAKQHLYIFPubiquitination[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] 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]
 [3] 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]
 [4] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724] 
Functional Description
 Interferon (IFN)-induced antiviral protein which acts as an inhibitor of retrovirus protein synthesis. Specifically abrogates the production of retroviruses such as human immunodeficiency virus 1 (HIV-1) by acting as a specific inhibitor of the synthesis of retroviruses encoded proteins in a codon- usage-dependent manner. Binds to tRNAs and exploits the unique viral codon bias towards A/T nucleotides. The exact inhibition mechanism is unclear: may either sequesters tRNAs, prevents their maturation via post-transcriptional processing or accelerates their deacylation. Does not inhibit reverse transcription, integration or production and nuclear export of viral RNA. May play a role in cell cycle arrest and/or induction of apoptosis in response to exogenously induced DNA damage. 
Sequence Annotation
 NP_BIND 599 606 ATP (Potential).  
Keyword
 Antiviral defense; ATP-binding; Complete proteome; Immunity; Nucleotide-binding; Nucleus; Polymorphism; Reference proteome; RNA-binding; tRNA-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 901 AA 
Protein Sequence
MEANQCPLVV EPSYPDLVIN VGEVTLGEEN RKKLQKIQRD QEKERVMRAA CALLNSGGGV 60
IRMAKKVEHP VEMGLDLEQS LRELIQSSDL QAFFETKQQG RCFYIFVKSW SSGPFPEDRS 120
VKPRLCSLSS SLYRRSETSV RSMDSREAFC FLKTKRKPKI LEEGPFHKIH KGVYQELPNS 180
DPADPNSDPA DLIFQKDYLE YGEILPFPES QLVEFKQFST KHFQEYVKRT IPEYVPAFAN 240
TGGGYLFIGV DDKSREVLGC AKENVDPDSL RRKIEQAIYK LPCVHFCQPQ RPITFTLKIV 300
NVLKRGELYG YACMIRVNPF CCAVFSEAPN SWIVEDKYVC SLTTEKWVGM MTDTDPDLLQ 360
LSEDFECQLS LSSGPPLSRP VYSKKGLEHK KELQQLLFSV PPGYLRYTPE SLWRDLISEH 420
RGLEELINKQ MQPFFRGILI FSRSWAVDLN LQEKPGVICD ALLIAQNSTP ILYTILREQD 480
AEGQDYCTRT AFTLKQKLVN MGGYTGKVCV RAKVLCLSPE SSAEALEAAV SPMDYPASYS 540
LAGTQHMEAL LQSLVIVLLG FRSLLSDQLG CEVLNLLTAQ QYEIFSRSLR KNRELFVHGL 600
PGSGKTIMAM KIMEKIRNVF HCEAHRILYV CENQPLRNFI SDRNICRAET RKTFLRENFE 660
HIQHIVIDEA QNFRTEDGDW YGKAKSITRR AKGGPGILWI FLDYFQTSHL DCSGLPPLSD 720
QYPREELTRI VRNADPIAKY LQKEMQVIRS NPSFNIPTGC LEVFPEAEWS QGVQGTLRIK 780
KYLTVEQIMT CVADTCRRFF DRGYSPKDVA VLVSTAKEVE HYKYELLKAM RKKRVVQLSD 840
ACDMLGDHIV LDSVRRFSGL ERSIVFGIHP RTADPAILPN VLICLASRAK QHLYIFPWGG 900
H 901 
Gene Ontology
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0000049; F:tRNA binding; IDA:UniProtKB.
 GO:0051607; P:defense response to virus; IMP:UniProtKB.
 GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IMP:UniProtKB. 
Interpro
 IPR007421; ATPase_AAA-4.
 IPR018647; DUF2075.
 IPR027417; P-loop_NTPase. 
Pfam
 PF04326; AAA_4
 PF09848; DUF2075 
SMART
  
PROSITE
  
PRINTS