Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00417
Entry Name
UniProt Accession
Theoretical PI
6.91
Molecular Weight
52296.47
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
55 kDa erythrocyte membrane protein
Protein Synonyms/Alias
p55; Membrane protein, palmitoylated 1;
Gene Name
MPP1
Gene Synonyms/Alias
DXS552E; EMP55;
Created Date
01-DEC-1992
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
242
Canonical
APSEAPSCSPFGKKK
[1]
S-Palmitoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Ciana A, Achilli C, Hannoush RN, Risso A, Balduini C, Minetti G. Freelyturning over palmitate in erythrocyte membrane proteins is not responsible forthe anchoring of lipid rafts to the spectrin skeleton: a study withbio-orthogonal chemical probes. Biochim Biophys Acta. 2013 Mar;1828(3):924-31.doi: 10.1016/j.bbamem.2012.11.029. Epub 2012 Dec 3.[PMID:23219804]
Functional Description
Essential regulator of neutrophil polarity. Regulates neutrophil polarization by regulating AKT1 phosphorylation through a mechanism that is independent of PIK3CG activity (By similarity).
Sequence Annotation
Domain: 71 152 PDZ.
Domain: 158 228 SH3.
Domain: 282 451 Guanylate kinase-like.
Region: 268 466 Interaction with MPP5.
Modified residue: 49 49 Phosphothreonine.
Modified residue: 57 57 Phosphoserine.
Modified residue: 110 110 Phosphoserine.
Modified residue: 243 243 Phosphoserine.
Protein Length
466 AA.
Protein Sequence
(Canonical)
MTLKASEGES GGSMHTALSD LYLEHLLQKR SRPEAVSHPL NTVTEDMYTN GSPAPGSPAQ  60
VKGQEVRKVR LIQFEKVTEE PMGITLKLNE KQSCTVARIL HGGMIHRQGS LHVGDEILEI  120
NGTNVTNHSV DQLQKAMKET KGMISLKVIP NQQSRLPALQ MFMRAQFDYD PKKDNLIPCK  180
EAGLKFATGD IIQIINKDDS NWWQGRVEGS SKESAGLIPS PELQEWRVAS MAQSAPSEAP  240
SCSPFGKKKK YKDKYLAKHS SIFDQLDVVS YEEVVRLPAF KRKTLVLIGA SGVGRSHIKN  300
ALLSQNPEKF VYPVPYTTRP PRKSEEDGKE YHFISTEEMT RNISANEFLE FGSYQGNMFG  360
TKFETVHQIH KQNKIAILDI EPQTLKIVRT AELSPFIVFI APTDQGTQTE ALQQLQKDSE  420
AIRSQYAHYF DLSLVNNGVD ETLKKLQEAF DQACSSPQWV PVSWVY                 466
FASTA
(Canonical)
>LipidDB-9606-00417|Q00013
MTLKASEGESGGSMHTALSDLYLEHLLQKRSRPEAVSHPLNTVTEDMYTNGSPAPGSPAQ
VKGQEVRKVRLIQFEKVTEEPMGITLKLNEKQSCTVARILHGGMIHRQGSLHVGDEILEI
NGTNVTNHSVDQLQKAMKETKGMISLKVIPNQQSRLPALQMFMRAQFDYDPKKDNLIPCK
EAGLKFATGDIIQIINKDDSNWWQGRVEGSSKESAGLIPSPELQEWRVASMAQSAPSEAP
SCSPFGKKKKYKDKYLAKHSSIFDQLDVVSYEEVVRLPAFKRKTLVLIGASGVGRSHIKN
ALLSQNPEKFVYPVPYTTRPPRKSEEDGKEYHFISTEEMTRNISANEFLEFGSYQGNMFG
TKFETVHQIHKQNKIAILDIEPQTLKIVRTAELSPFIVFIAPTDQGTQTEALQQLQKDSE
AIRSQYAHYFDLSLVNNGVDETLKKLQEAFDQACSSPQWVPVSWVY
Gene Ontology
GO:0042995; C:cell projection; IEA:UniProtKB-KW
GO:0030863; C:cortical cytoskeleton; IEA:Ensembl
GO:0005887; C:integral component of plasma membrane; TAS:ProtInc
GO:0005622; C:intracellular; IDA:LIFEdb
GO:0016020; C:membrane; IDA:UniProtKB
GO:0004385; F:guanylate kinase activity; TAS:ProtInc
GO:0046939; P:nucleotide phosphorylation; TAS:GOC
GO:0090022; P:regulation of neutrophil chemotaxis; ISS:UniProtKB
GO:0007165; P:signal transduction; TAS:ProtInc
Interpro
InterPro; IPR008145; GK/Ca_channel_bsu
InterPro; IPR008144; Guanylate_kin-like
InterPro; IPR020590; Guanylate_kinase_CS
InterPro; IPR027417; P-loop_NTPase
InterPro; IPR001478; PDZ
InterPro; IPR011511; SH3_2
InterPro; IPR001452; SH3_domain
Pfam
Pfam; PF00625; Guanylate_kin;
Pfam; PF00595; PDZ;
Pfam; PF07653; SH3_2;
SMART
SMART; SM00072; GuKc;
SMART; SM00228; PDZ;
SMART; SM00326; SH3;
PROSITE
PROSITE; PS00856; GUANYLATE_KINASE_1;
PROSITE; PS50052; GUANYLATE_KINASE_2;
PROSITE; PS50106; PDZ;
PROSITE; PS50002; SH3;
PRINTS