CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000720
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Band 4.1-like protein 2 
Protein Synonyms/Alias
 Generally expressed protein 4.1; 4.1G 
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
13GSVSEVKKDSSQLGTubiquitination[1]
28DATKEKPKEVAENQQubiquitination[1]
45SSDPEEEKGSQPPPAubiquitination[1]
83RFIPPWLKKQKSYTLubiquitination[2]
86PPWLKKQKSYTLVVAubiquitination[2, 3]
94SYTLVVAKDGGDKKEubiquitination[2]
99VAKDGGDKKEPTQAVubiquitination[1, 4]
100AKDGGDKKEPTQAVVubiquitination[1]
114VEEQVLDKEEPLPEEubiquitination[1, 4]
126PEEQRQAKGDAEEMAubiquitination[1]
135DAEEMAQKKQEIKVEubiquitination[1]
144QEIKVEVKEEKPSVSubiquitination[1]
160EEKPSVSKVEMQPTEubiquitination[4, 5, 6]
171QPTELVSKEREEKVKubiquitination[1]
176VSKEREEKVKETQEDacetylation[7]
178KEREEKVKETQEDKLubiquitination[1, 4]
184VKETQEDKLEGGAAKacetylation[7]
184VKETQEDKLEGGAAKubiquitination[1]
191KLEGGAAKRETKEVQacetylation[7]
195GAAKRETKEVQTNELubiquitination[1]
203EVQTNELKAEKASQKubiquitination[1, 3]
246KGQVLFDKVCEHLNLubiquitination[2, 5]
270FQESPEQKNWLDPAKubiquitination[1, 2, 4, 5, 6]
374QTKELEEKVAELHKTubiquitination[1, 3]
399SQFLENAKRLSMYGVubiquitination[2, 3, 5, 6]
444INRFAWPKILKISYKubiquitination[2, 5, 6]
474FESTIGFKLPNHRAAubiquitination[5, 6]
507PEQPPKAKFLTLGSKubiquitination[2]
514KFLTLGSKFRYSGRTacetylation[8]
514KFLTLGSKFRYSGRTubiquitination[2]
601REVRSPTKAPHLQLIubiquitination[4]
643KAQEDILKHQASISEubiquitination[2]
652QASISELKRNFMESTubiquitination[2]
712ITEEMNGKEISPGSGubiquitination[1]
827AQKIPGEKSVHEGALubiquitination[1]
892QRTEISTKEVPIVQTubiquitination[1]
946THITKTVKGGISETRubiquitination[2]
995VTRVVVHKETELAEEubiquitination[1, 3, 4]
Reference
 [1] 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]
 [2] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [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] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861] 
Functional Description
  
Sequence Annotation
 DOMAIN 218 499 FERM.
 REGION 502 610 Hydrophilic.
 REGION 611 676 Spectrin--actin-binding.
 REGION 855 1005 C-terminal (CTD).
 MOD_RES 2 2 N-acetylthreonine.
 MOD_RES 39 39 Phosphoserine.
 MOD_RES 87 87 Phosphoserine.
 MOD_RES 89 89 Phosphothreonine.
 MOD_RES 386 386 Phosphoserine.
 MOD_RES 499 499 Phosphoserine.
 MOD_RES 550 550 Phosphoserine.
 MOD_RES 598 598 Phosphoserine (By similarity).
 MOD_RES 614 614 Phosphoserine.
 MOD_RES 623 623 Phosphotyrosine (By similarity).
 MOD_RES 627 627 Phosphoserine (By similarity).
 MOD_RES 647 647 Phosphoserine (By similarity).
 MOD_RES 715 715 Phosphoserine.
 MOD_RES 718 718 Phosphoserine.
 MOD_RES 763 763 Phosphothreonine (By similarity).  
Keyword
 Acetylation; Actin-binding; Alternative splicing; Cell membrane; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; Membrane; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1005 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 KKNSLRVEGD NIYVRHSNLM LEELDKAQED ILKHQASISE LKRNFMESTP 660
EPRPNEWEKR RITPLSLQTQ GSSHETLNIV EEKKRAEVGK DERVITEEMN GKEISPGSGP 720
GEIRKVEPVT QKDSTSLSSE SSSSSSESEE EDVGEYRPHH RVTEGTIREE QEYEEEVEEE 780
PRPAAKVVER EEAVPEASPV TQAGASVITV ETVIQENVGA QKIPGEKSVH EGALKQDMGE 840
EAEEEPQKVN GEVSHVDIDV LPQIICCSEP PVVKTEMVTI SDASQRTEIS TKEVPIVQTE 900
TKTITYESPQ IDGGAGGDSG TLLTAQTITS ESVSTTTTTH ITKTVKGGIS ETRIEKRIVI 960
TGDGDIDHDQ ALAQAIREAR EQHPDMSVTR VVVHKETELA EEGED 1005 
Gene Ontology
 GO:0030054; C:cell junction; IDA:HPA.
 GO:0019898; C:extrinsic to membrane; IEA:InterPro.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0005886; C:plasma membrane; IDA:HPA.
 GO:0008091; C:spectrin; TAS:ProtInc.
 GO:0005198; F:structural molecule activity; IEA:InterPro.
 GO:0030866; P:cortical actin cytoskeleton organization; 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.
 IPR007477; SAB_dom. 
Pfam
 PF05902; 4_1_CTD
 PF08736; FA
 PF09380; FERM_C
 PF00373; FERM_M
 PF09379; FERM_N
 PF04382; SAB 
SMART
 SM00295; B41 
PROSITE
 PS00660; FERM_1
 PS00661; FERM_2
 PS50057; FERM_3 
PRINTS
 PR00935; BAND41.
 PR00661; ERMFAMILY.