Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00804
Entry Name
UniProt Accession
Theoretical PI
8.39
Molecular Weight
77009.14
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Erythrocyte membrane protein band 4.2
Protein Synonyms/Alias
Erythrocyte protein 4.2; P4.2;
Gene Name
EPB42
Gene Synonyms/Alias
E42P;
Created Date
01-AUG-1990
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
2
Canonical
******MGQALGIKS
[1]
N-Myristoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Risinger MA, Dotimas EM, Cohen CM. Human erythrocyte protein 4.2, a high copy number membrane protein, is N-myristylated. J Biol Chem. 1992 Mar15;267(8):5680-5.[PMID:1544941]
Functional Description
Probably plays an important role in the regulation of erythrocyte shape and mechanical properties.
Sequence Annotation
Region: 31 39 Band 3 binding.
Modified residue: 248 248 Phosphoserine; by PKA.
Protein Length
691 AA.
Protein Sequence
(Canonical)
MGQALGIKSC DFQAARNNEE HHTKALSSRR LFVRRGQPFT IILYFRAPVR AFLPALKKVA  60
LTAQTGEQPS KINRTQATFP ISSLGDRKWW SAVVEERDAQ SWTISVTTPA DAVIGHYSLL  120
LQVSGRKQLL LGQFTLLFNP WNREDAVFLK NEAQRMEYLL NQNGLIYLGT ADCIQAESWD  180
FGQFEGDVID LSLRLLSKDK QVEKWSQPVH VARVLGALLH FLKEQRVLPT PQTQATQEGA  240
LLNKRRGSVP ILRQWLTGRG RPVYDGQAWV LAAVACTVLR CLGIPARVVT TFASAQGTGG  300
RLLIDEYYNE EGLQNGEGQR GRIWIFQTST ECWMTRPALP QGYDGWQILH PSAPNGGGVL  360
GSCDLVPVRA VKEGTLGLTP AVSDLFAAIN ASCVVWKCCE DGTLELTDSN TKYVGNNIST  420
KGVGSDRCED ITQNYKYPEG SLQEKEVLER VEKEKMEREK DNGIRPPSLE TASPLYLLLK  480
APSSLPLRGD AQISVTLVNH SEQEKAVQLA IGVQAVHYNG VLAAKLWRKK LHLTLSANLE  540
KIITIGLFFS NFERNPPENT FLRLTAMATH SESNLSCFAQ EDIAICRPHL AIKMPEKAEQ  600
YQPLTASVSL QNSLDAPMED CVISILGRGL IHRERSYRFR SVWPENTMCA KFQFTPTHVG  660
LQRLTVEVDC NMFQNLTNYK SVTVVAPELS A                                 691
FASTA
(Canonical)
>LipidDB-9606-00804|P16452
MGQALGIKSCDFQAARNNEEHHTKALSSRRLFVRRGQPFTIILYFRAPVRAFLPALKKVA
LTAQTGEQPSKINRTQATFPISSLGDRKWWSAVVEERDAQSWTISVTTPADAVIGHYSLL
LQVSGRKQLLLGQFTLLFNPWNREDAVFLKNEAQRMEYLLNQNGLIYLGTADCIQAESWD
FGQFEGDVIDLSLRLLSKDKQVEKWSQPVHVARVLGALLHFLKEQRVLPTPQTQATQEGA
LLNKRRGSVPILRQWLTGRGRPVYDGQAWVLAAVACTVLRCLGIPARVVTTFASAQGTGG
RLLIDEYYNEEGLQNGEGQRGRIWIFQTSTECWMTRPALPQGYDGWQILHPSAPNGGGVL
GSCDLVPVRAVKEGTLGLTPAVSDLFAAINASCVVWKCCEDGTLELTDSNTKYVGNNIST
KGVGSDRCEDITQNYKYPEGSLQEKEVLERVEKEKMEREKDNGIRPPSLETASPLYLLLK
APSSLPLRGDAQISVTLVNHSEQEKAVQLAIGVQAVHYNGVLAAKLWRKKLHLTLSANLE
KIITIGLFFSNFERNPPENTFLRLTAMATHSESNLSCFAQEDIAICRPHLAIKMPEKAEQ
YQPLTASVSLQNSLDAPMEDCVISILGRGLIHRERSYRFRSVWPENTMCAKFQFTPTHVG
LQRLTVEVDCNMFQNLTNYKSVTVVAPELSA
Gene Ontology
GO:0030863; C:cortical cytoskeleton; IEA:Ensembl
GO:0005856; C:cytoskeleton; TAS:ProtInc
GO:0005886; C:plasma membrane; TAS:ProtInc
GO:0005524; F:ATP binding; TAS:ProtInc
GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; IEA:InterPro
GO:0005200; F:structural constituent of cytoskeleton; TAS:ProtInc
GO:0000902; P:cell morphogenesis; IEA:Ensembl
GO:0043249; P:erythrocyte maturation; IEA:UniProtKB-KW
GO:0020027; P:hemoglobin metabolic process; IEA:Ensembl
GO:0055072; P:iron ion homeostasis; IEA:Ensembl
GO:0018149; P:peptide cross-linking; IEA:InterPro
GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW
GO:0048536; P:spleen development; IEA:Ensembl
Interpro
InterPro; IPR023608; Gln_gamma-glutamylTfrase_euk
InterPro; IPR013783; Ig-like_fold
InterPro; IPR014756; Ig_E-set
InterPro; IPR002931; Transglutaminase-like
InterPro; IPR008958; Transglutaminase_C
InterPro; IPR013808; Transglutaminase_CS
InterPro; IPR001102; Transglutaminase_N
Pfam
Pfam; PF00927; Transglut_C;
Pfam; PF01841; Transglut_core;
Pfam; PF00868; Transglut_N;
SMART
SMART; SM00460; TGc;
PROSITE
PROSITE; PS00547; TRANSGLUTAMINASES;
PRINTS