CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-037491
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Band 4.1-like protein 2 
Protein Synonyms/Alias
  
Gene Name
 EPB41L2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
12VGSVSEVKKDSSQLGubiquitination[1]
13GSVSEVKKDSSQLGTubiquitination[2]
28DATKEKPKEVAENQQubiquitination[2]
45SSDPEEEKGSQPPPAubiquitination[2]
86PPWLKKQKSYTLVVAubiquitination[3]
99VAKDGGDKKEPTQAVubiquitination[2, 4, 5]
100AKDGGDKKEPTQAVVubiquitination[2, 4]
114VEEQVLDKEEPLPEEubiquitination[2, 5]
126PEEQRQAKGDAEEMAubiquitination[2]
135DAEEMAQKKQEIKVEubiquitination[2]
144QEIKVEVKEEKPSVSubiquitination[2]
160EEKPSVSKVEMQPTEubiquitination[5, 6]
171QPTELVSKEREEKVKubiquitination[2]
178KEREEKVKETQEDKLubiquitination[2, 5]
184VKETQEDKLEGGAAKubiquitination[2]
195GAAKRETKEVQTNELubiquitination[2]
203EVQTNELKAEKASQKubiquitination[2, 3]
246KGQVLFDKVCEHLNLubiquitination[3, 6]
270FQESPEQKNWLDPAKubiquitination[2, 4, 5, 6]
374QTKELEEKVAELHKTacetylation[7]
374QTKELEEKVAELHKTubiquitination[1, 2, 3]
399SQFLENAKRLSMYGVubiquitination[3, 6]
444INRFAWPKILKISYKubiquitination[6]
474FESTIGFKLPNHRAAubiquitination[6]
507PEQPPKAKFLTLGSKubiquitination[6]
514KFLTLGSKFRYSGRTacetylation[8]
514KFLTLGSKFRYSGRTubiquitination[3, 6]
601REVRSPTKAPHLQLIubiquitination[5]
623TLNIVEEKKRAEVGKubiquitination[2]
642ITEEMNGKEISPGSGubiquitination[2]
757AQKIPGEKSVHEGALubiquitination[2]
822QRTEISTKEVPIVQTubiquitination[2]
925VTRVVVHKETELAEEubiquitination[2, 3, 5]
Reference
 [1] 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]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [3] 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]
 [4] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [5] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [6] 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]
 [7] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [8] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 935 AA 
Protein Sequence
MTTEVGSVSE VKKDSSQLGT DATKEKPKEV AENQQNQSSD PEEEKGSQPP PAAESQSSLR 60
RQKREKETSE SRGISRFIPP WLKKQKSYTL VVAKDGGDKK EPTQAVVEEQ VLDKEEPLPE 120
EQRQAKGDAE EMAQKKQEIK VEVKEEKPSV SKEEKPSVSK VEMQPTELVS KEREEKVKET 180
QEDKLEGGAA KRETKEVQTN ELKAEKASQK VTKKTKTVQC KVTLLDGTEY SCDLEKHAKG 240
QVLFDKVCEH LNLLEKDYFG LLFQESPEQK NWLDPAKEIK RQLRNLPWLF TFNVKFYPPD 300
PSQLTEDITR YFLCLQLRQD IASGRLPCSF VTHALLGSYT LQAELGDYDP EEHGSIDLSE 360
FQFAPTQTKE LEEKVAELHK THRGLSPAQA DSQFLENAKR LSMYGVDLHH AKDSEGVDIK 420
LGVCANGLLI YKDRLRINRF AWPKILKISY KRSNFYIKVR PAELEQFEST IGFKLPNHRA 480
AKRLWKVCVE HHTFYRLVSP EQPPKAKFLT LGSKFRYSGR TQAQTRQAST LIDRPAPHFE 540
RTSSKRVSRS LDGAPIGVMD QSLMKDFPGA AGEISAYGPG LVSIAVVQDG DGRREVRSPT 600
KAPHLQLIEG KSSHETLNIV EEKKRAEVGK DERVITEEMN GKEISPGSGP GEIRKVEPVT 660
QKDSTSLSSE SSSSSSESEE EDVGEYRPHH RVTEGTIREE QEYEEEVEEE PRPAAKVVER 720
EEAVPEASPV TQAGASVITV ETVIQENVGA QKIPGEKSVH EGALKQDMGE EAEEEPQKVN 780
GEVSHVDIDV LPQIICCSEP PVVKTEMVTI SDASQRTEIS TKEVPIVQTE TKTITYESPQ 840
IDGGAGGDSG TLLTAQTITS ESVSTTTTTH ITKTVKGGIS ETRIEKRIVI TGDGDIDHDQ 900
ALAQAIREAR EQHPDMSVTR VVVHKETELA EEGED 935 
Gene Ontology
 GO:0030054; C:cell junction; IDA:HPA.
 GO:0005737; C:cytoplasm; IEA:InterPro.
 GO:0005856; C:cytoskeleton; IEA:InterPro.
 GO:0019898; C:extrinsic to membrane; IEA:InterPro.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0005886; C:plasma membrane; IDA:HPA.
 GO:0005198; F:structural molecule activity; IEA:InterPro. 
Interpro
 IPR008379; Band_4.1_C.
 IPR019749; Band_41_domain.
 IPR019750; Band_41_fam.
 IPR021187; Band_41_protein.
 IPR000798; Ez/rad/moesin_like.
 IPR014847; FERM-adjacent.
 IPR014352; FERM/acyl-CoA-bd_prot_3-hlx.
 IPR019748; FERM_central.
 IPR019747; FERM_CS.
 IPR000299; FERM_domain.
 IPR018979; FERM_N.
 IPR018980; FERM_PH-like_C.
 IPR011993; PH_like_dom. 
Pfam
 PF05902; 4_1_CTD
 PF08736; FA
 PF09380; FERM_C
 PF00373; FERM_M
 PF09379; FERM_N 
SMART
 SM00295; B41 
PROSITE
 PS00660; FERM_1
 PS00661; FERM_2
 PS50057; FERM_3 
PRINTS
 PR00935; BAND41.
 PR00661; ERMFAMILY.