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Protein

55 kDa erythrocyte membrane protein

Gene

MPP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Essential regulator of neutrophil polarity. Regulates neutrophil polarization by regulating AKT1 phosphorylation through a mechanism that is independent of PIK3CG activity (By similarity).By similarity

GO - Molecular functioni

  • guanylate kinase activity Source: ProtInc

GO - Biological processi

  • GDP metabolic process Source: GOC
  • GMP metabolic process Source: GOC
  • regulation of neutrophil chemotaxis Source: UniProtKB
  • signal transduction Source: ProtInc
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
55 kDa erythrocyte membrane protein
Short name:
p55
Alternative name(s):
Membrane protein, palmitoylated 1
Gene namesi
Name:MPP1
Synonyms:DXS552E, EMP55
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:7219. MPP1.

Subcellular locationi

  • Membrane; Lipid-anchor
  • Cell projectionstereocilium By similarity

  • Note: Colocalizes with WHRN at stereocilium tip during hair cell development (By similarity). Colocalizes with MPP5 in the retina, at the outer limiting membrane (OLM). Colocalizes with WHRN in the retina, at the outer limiting membrane (OLM), outer plexifirm layer (OPL), basal bodies and at the connecting cilium (CC). Colocalizes with NF2 in non-myelin-forming Schwann cells.By similarity

GO - Cellular componenti

  • cortical cytoskeleton Source: Ensembl
  • integral component of plasma membrane Source: ProtInc
  • intracellular Source: LIFEdb
  • membrane Source: UniProtKB
  • stereocilium Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30924.

Polymorphism and mutation databases

BioMutaiMPP1.
DMDMi1346575.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 46646555 kDa erythrocyte membrane proteinPRO_0000094565Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonineCombined sources
Modified residuei49 – 491PhosphothreonineCombined sources
Modified residuei52 – 521PhosphoserineBy similarity
Modified residuei57 – 571PhosphoserineCombined sources
Modified residuei110 – 1101PhosphoserineCombined sources
Modified residuei243 – 2431PhosphoserineCombined sources

Post-translational modificationi

Extensively palmitoylated by ZDHHC17, palmitoylation is essential for membrane organization and is crucial for proper erythrocytes morphology.2 Publications

Keywords - PTMi

Acetylation, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

EPDiQ00013.
PaxDbiQ00013.
PeptideAtlasiQ00013.
PRIDEiQ00013.

PTM databases

iPTMnetiQ00013.
PhosphoSiteiQ00013.
SwissPalmiQ00013.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiQ00013.
CleanExiHS_MPP1.
ExpressionAtlasiQ00013. baseline and differential.
GenevisibleiQ00013. HS.

Organism-specific databases

HPAiHPA000884.

Interactioni

Subunit structurei

Heterodimer with MPP5. Interacts with DLG5 and NF2. Interacts (via guanylate kinase-like domain) with WHRN (via third PDZ domain).2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DNPEPQ9ULA03EBI-711788,EBI-748356
KLHL12Q53G593EBI-711788,EBI-740929
OPTNQ96CV92EBI-711788,EBI-748974

Protein-protein interaction databases

BioGridi110494. 44 interactions.
IntActiQ00013. 39 interactions.
MINTiMINT-1402557.
STRINGi9606.ENSP00000358547.

Structurei

Secondary structure

1
466
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi70 – 767Combined sources
Beta strandi78 – 803Combined sources
Beta strandi83 – 886Combined sources
Beta strandi94 – 996Combined sources
Beta strandi101 – 1033Combined sources
Helixi104 – 1085Combined sources
Beta strandi116 – 1205Combined sources
Turni125 – 1273Combined sources
Helixi131 – 1399Combined sources
Beta strandi142 – 1498Combined sources
Beta strandi284 – 2885Combined sources
Helixi295 – 30511Combined sources
Turni307 – 3093Combined sources
Helixi336 – 3449Combined sources
Beta strandi348 – 3547Combined sources
Beta strandi357 – 3626Combined sources
Helixi363 – 3719Combined sources
Beta strandi375 – 3795Combined sources
Helixi382 – 3843Combined sources
Helixi385 – 3884Combined sources
Turni391 – 3933Combined sources
Beta strandi395 – 4028Combined sources
Beta strandi405 – 4073Combined sources
Helixi410 – 42617Combined sources
Helixi427 – 4293Combined sources
Beta strandi431 – 4377Combined sources
Helixi439 – 45214Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EJYNMR-A69-153[»]
2EV8NMR-A69-153[»]
3NEYX-ray2.26A/B/C/D/E/F282-460[»]
ProteinModelPortaliQ00013.
SMRiQ00013. Positions 57-465.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ00013.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini71 – 15282PDZPROSITE-ProRule annotationAdd
BLAST
Domaini158 – 22871SH3PROSITE-ProRule annotationAdd
BLAST
Domaini282 – 451170Guanylate kinase-likePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni268 – 466199Interaction with MPP5Add
BLAST

Sequence similaritiesi

Belongs to the MAGUK family.Curated
Contains 1 guanylate kinase-like domain.PROSITE-ProRule annotation
Contains 1 PDZ (DHR) domain.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

SH3 domain

Phylogenomic databases

eggNOGiKOG0609. Eukaryota.
COG0194. LUCA.
GeneTreeiENSGT00760000118866.
HOGENOMiHOG000233034.
HOVERGENiHBG001858.
InParanoidiQ00013.
OMAiIPNQQSR.
PhylomeDBiQ00013.
TreeFamiTF314263.

Family and domain databases

Gene3Di2.30.42.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR008145. GK/Ca_channel_bsu.
IPR008144. Guanylate_kin-like_dom.
IPR020590. Guanylate_kinase_CS.
IPR027417. P-loop_NTPase.
IPR001478. PDZ.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF00625. Guanylate_kin. 1 hit.
PF00595. PDZ. 1 hit.
PF07653. SH3_2. 1 hit.
[Graphical view]
SMARTiSM00072. GuKc. 1 hit.
SM00228. PDZ. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF50156. SSF50156. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS00856. GUANYLATE_KINASE_1. 1 hit.
PS50052. GUANYLATE_KINASE_2. 1 hit.
PS50106. PDZ. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q00013-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MTLKASEGES GGSMHTALSD LYLEHLLQKR SRPEAVSHPL NTVTEDMYTN
60 70 80 90 100
GSPAPGSPAQ VKGQEVRKVR LIQFEKVTEE PMGITLKLNE KQSCTVARIL
110 120 130 140 150
HGGMIHRQGS LHVGDEILEI NGTNVTNHSV DQLQKAMKET KGMISLKVIP
160 170 180 190 200
NQQSRLPALQ MFMRAQFDYD PKKDNLIPCK EAGLKFATGD IIQIINKDDS
210 220 230 240 250
NWWQGRVEGS SKESAGLIPS PELQEWRVAS MAQSAPSEAP SCSPFGKKKK
260 270 280 290 300
YKDKYLAKHS SIFDQLDVVS YEEVVRLPAF KRKTLVLIGA SGVGRSHIKN
310 320 330 340 350
ALLSQNPEKF VYPVPYTTRP PRKSEEDGKE YHFISTEEMT RNISANEFLE
360 370 380 390 400
FGSYQGNMFG TKFETVHQIH KQNKIAILDI EPQTLKIVRT AELSPFIVFI
410 420 430 440 450
APTDQGTQTE ALQQLQKDSE AIRSQYAHYF DLSLVNNGVD ETLKKLQEAF
460
DQACSSPQWV PVSWVY
Length:466
Mass (Da):52,296
Last modified:February 1, 1996 - v2
Checksum:iDC68AA68EF48A26E
GO
Isoform 2 (identifier: Q00013-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-34: MTLKASEGESGGSMHTALSDLYLEHLLQKRSRPE → MESW

Note: No experimental confirmation available.
Show »
Length:436
Mass (Da):49,075
Checksum:iD70881879A5C497A
GO
Isoform 3 (identifier: Q00013-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     161-180: Missing.

Note: No experimental confirmation available.
Show »
Length:446
Mass (Da):49,854
Checksum:iC935FBFA6E563CE1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti204 – 2041Q → R in AAV35469 (Ref. 5) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti448 – 4481E → Q.
Corresponds to variant rs14092 [ dbSNP | Ensembl ].
VAR_011914

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3434MTLKA…RSRPE → MESW in isoform 2. 1 PublicationVSP_042675Add
BLAST
Alternative sequencei161 – 18020Missing in isoform 3. 1 PublicationVSP_044634Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64925 mRNA. Translation: AAA60059.1.
M87059 Genomic DNA. Translation: AAA60060.1.
U39611 Genomic DNA. Translation: AAD14835.1.
AY423731 mRNA. Translation: AAS00494.1.
AK290246 mRNA. Translation: BAF82935.1.
AK303111 mRNA. Translation: BAG64217.1.
AK312296 mRNA. Translation: BAG35223.1.
AK315957 mRNA. Translation: BAH14328.1.
AY634686 mRNA. Translation: AAV35469.1.
AC109993 Genomic DNA. No translation available.
CH471172 Genomic DNA. Translation: EAW72655.1.
CH471172 Genomic DNA. Translation: EAW72656.1.
CH471172 Genomic DNA. Translation: EAW72660.1.
BC002392 mRNA. Translation: AAH02392.1.
CCDSiCCDS14762.1. [Q00013-1]
CCDS55544.1. [Q00013-2]
CCDS55545.1. [Q00013-3]
PIRiA39599.
RefSeqiNP_001159932.1. NM_001166460.1.
NP_001159933.1. NM_001166461.1. [Q00013-3]
NP_001159934.1. NM_001166462.1. [Q00013-2]
NP_002427.1. NM_002436.3. [Q00013-1]
UniGeneiHs.496984.

Genome annotation databases

EnsembliENST00000369534; ENSP00000358547; ENSG00000130830. [Q00013-1]
ENST00000393531; ENSP00000377165; ENSG00000130830. [Q00013-3]
ENST00000413259; ENSP00000400155; ENSG00000130830. [Q00013-2]
GeneIDi4354.
KEGGihsa:4354.
UCSCiuc004fmp.3. human. [Q00013-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64925 mRNA. Translation: AAA60059.1.
M87059 Genomic DNA. Translation: AAA60060.1.
U39611 Genomic DNA. Translation: AAD14835.1.
AY423731 mRNA. Translation: AAS00494.1.
AK290246 mRNA. Translation: BAF82935.1.
AK303111 mRNA. Translation: BAG64217.1.
AK312296 mRNA. Translation: BAG35223.1.
AK315957 mRNA. Translation: BAH14328.1.
AY634686 mRNA. Translation: AAV35469.1.
AC109993 Genomic DNA. No translation available.
CH471172 Genomic DNA. Translation: EAW72655.1.
CH471172 Genomic DNA. Translation: EAW72656.1.
CH471172 Genomic DNA. Translation: EAW72660.1.
BC002392 mRNA. Translation: AAH02392.1.
CCDSiCCDS14762.1. [Q00013-1]
CCDS55544.1. [Q00013-2]
CCDS55545.1. [Q00013-3]
PIRiA39599.
RefSeqiNP_001159932.1. NM_001166460.1.
NP_001159933.1. NM_001166461.1. [Q00013-3]
NP_001159934.1. NM_001166462.1. [Q00013-2]
NP_002427.1. NM_002436.3. [Q00013-1]
UniGeneiHs.496984.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EJYNMR-A69-153[»]
2EV8NMR-A69-153[»]
3NEYX-ray2.26A/B/C/D/E/F282-460[»]
ProteinModelPortaliQ00013.
SMRiQ00013. Positions 57-465.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110494. 44 interactions.
IntActiQ00013. 39 interactions.
MINTiMINT-1402557.
STRINGi9606.ENSP00000358547.

PTM databases

iPTMnetiQ00013.
PhosphoSiteiQ00013.
SwissPalmiQ00013.

Polymorphism and mutation databases

BioMutaiMPP1.
DMDMi1346575.

Proteomic databases

EPDiQ00013.
PaxDbiQ00013.
PeptideAtlasiQ00013.
PRIDEiQ00013.

Protocols and materials databases

DNASUi4354.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000369534; ENSP00000358547; ENSG00000130830. [Q00013-1]
ENST00000393531; ENSP00000377165; ENSG00000130830. [Q00013-3]
ENST00000413259; ENSP00000400155; ENSG00000130830. [Q00013-2]
GeneIDi4354.
KEGGihsa:4354.
UCSCiuc004fmp.3. human. [Q00013-1]

Organism-specific databases

CTDi4354.
GeneCardsiMPP1.
HGNCiHGNC:7219. MPP1.
HPAiHPA000884.
MIMi305360. gene.
neXtProtiNX_Q00013.
PharmGKBiPA30924.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0609. Eukaryota.
COG0194. LUCA.
GeneTreeiENSGT00760000118866.
HOGENOMiHOG000233034.
HOVERGENiHBG001858.
InParanoidiQ00013.
OMAiIPNQQSR.
PhylomeDBiQ00013.
TreeFamiTF314263.

Miscellaneous databases

ChiTaRSiMPP1. human.
EvolutionaryTraceiQ00013.
GeneWikiiMPP1.
GenomeRNAii4354.
PROiQ00013.
SOURCEiSearch...

Gene expression databases

BgeeiQ00013.
CleanExiHS_MPP1.
ExpressionAtlasiQ00013. baseline and differential.
GenevisibleiQ00013. HS.

Family and domain databases

Gene3Di2.30.42.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR008145. GK/Ca_channel_bsu.
IPR008144. Guanylate_kin-like_dom.
IPR020590. Guanylate_kinase_CS.
IPR027417. P-loop_NTPase.
IPR001478. PDZ.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF00625. Guanylate_kin. 1 hit.
PF00595. PDZ. 1 hit.
PF07653. SH3_2. 1 hit.
[Graphical view]
SMARTiSM00072. GuKc. 1 hit.
SM00228. PDZ. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF50156. SSF50156. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS00856. GUANYLATE_KINASE_1. 1 hit.
PS50052. GUANYLATE_KINASE_2. 1 hit.
PS50106. PDZ. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular identification of a major palmitoylated erythrocyte membrane protein containing the src homology 3 motif."
    Ruff P., Speicher D.W., Husain-Chishti A.
    Proc. Natl. Acad. Sci. U.S.A. 88:6595-6599(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, PALMITOYLATION.
    Tissue: Reticulocyte.
  2. "The gene encoding the palmitoylated erythrocyte membrane protein, p55, originates at the CpG island 3' to the factor VIII gene."
    Metzenberg A.B., Gitschier J.
    Hum. Mol. Genet. 1:97-101(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Identification of a human migration-related gene."
    Kim J.W.
    Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Lung cancer.
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Amygdala, Cerebellum, Cervix and Thymus.
  5. "Identification of a human aging-related gene."
    Kim J.W.
    Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Umbilical cord.
  6. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Lung.
  9. Cited for: SUBUNIT, SUBCELLULAR LOCATION, INTERACTION WITH MPP5 AND WHRN, TISSUE SPECIFICITY.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-49; SER-57 AND SER-243, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Identification of erythrocyte p55/MPP1 as a binding partner of NF2 tumor suppressor protein/Merlin."
    Seo P.-S., Quinn B.J., Khan A.A., Zeng L., Takoudis C.G., Hanada T., Bolis A., Bolino A., Chishti A.H.
    Exp. Biol. Med. 234:255-262(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NF2, SUBCELLULAR LOCATION.
  12. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Palmitoylation of MPP1 (membrane-palmitoylated protein 1)/p55 is crucial for lateral membrane organization in erythroid cells."
    Lach A., Grzybek M., Heger E., Korycka J., Wolny M., Kubiak J., Kolondra A., Boguslawska D.M., Augoff K., Majkowski M., Podkalicka J., Kaczor J., Stefanko A., Kuliczkowski K., Sikorski A.F.
    J. Biol. Chem. 287:18974-18984(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PALMITOYLATION BY ZDHHC17, SUBCELLULAR LOCATION.
  15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Solution structure of human erythroid p55 PDZ domain."
    Kusunoki H., Kohno T.
    Proteins 64:804-807(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 69-153.

Entry informationi

Entry nameiEM55_HUMAN
AccessioniPrimary (citable) accession number: Q00013
Secondary accession number(s): B4DZV5
, G3XAI1, Q2TSB6, Q5J7V5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: February 1, 1996
Last modified: June 8, 2016
This is version 170 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.