Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

MAGUK p55 subfamily member 5

Gene

MPP5

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

Functioni

May play a role in tight junctions biogenesis and in the establishment of cell polarity in epithelial cells. May modulate SC6A1/GAT1-mediated GABA uptake by stabilizing the transporter. Required for localization of EZR to the apical membrane of parietal cells and may play a role in the dynamic remodeling of the apical cytoskeleton (By similarity).By similarity

GO - Molecular functioni

  1. protein domain specific binding Source: BHF-UCL

GO - Biological processi

  1. cell-cell junction organization Source: Reactome
  2. cell junction assembly Source: Reactome
  3. establishment of protein localization to plasma membrane Source: Ensembl
  4. morphogenesis of an epithelial sheet Source: UniProtKB
  5. myelin assembly Source: Ensembl
  6. peripheral nervous system myelin maintenance Source: Ensembl
  7. protein localization to myelin sheath abaxonal region Source: Ensembl
  8. tight junction assembly Source: Reactome
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_19373. Tight junction interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
MAGUK p55 subfamily member 5
Gene namesi
Name:MPP5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:18669. MPP5.

Subcellular locationi

  1. Cell membrane; Peripheral membrane protein
  2. Endomembrane system; Peripheral membrane protein
  3. Cell junctiontight junction

  4. Note: Localized to the tight junctions of epithelial cells and a subset of intracellular vesicles. In the retina, detected at the outer limiting membrane (OLM), apical to the adherens junction (AJ), where it colocalizes with CRB1. Colocalizes with MPP1 in the retina at the outer limiting membrane (OLM). Localized to the Purkinje cell body and axon.

GO - Cellular componenti

  1. cytoplasm Source: LIFEdb
  2. endomembrane system Source: UniProtKB-SubCell
  3. extracellular vesicular exosome Source: UniProtKB
  4. lateral loop Source: Ensembl
  5. myelin sheath adaxonal region Source: Ensembl
  6. nucleoplasm Source: HPA
  7. plasma membrane Source: HPA
  8. protein complex Source: Ensembl
  9. Schmidt-Lanterman incisure Source: Ensembl
  10. tight junction Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Tight junction

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA38631.

Polymorphism and mutation databases

BioMutaiMPP5.
DMDMi116242632.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 675675MAGUK p55 subfamily member 5PRO_0000094580Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei25 – 251Phosphoserine1 Publication
Modified residuei84 – 841Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8N3R9.
PaxDbiQ8N3R9.
PRIDEiQ8N3R9.

PTM databases

PhosphoSiteiQ8N3R9.

Expressioni

Tissue specificityi

Expressed in the retina (at protein level).2 Publications

Gene expression databases

BgeeiQ8N3R9.
CleanExiHS_MPP5.
ExpressionAtlasiQ8N3R9. baseline and differential.
GenevestigatoriQ8N3R9.

Organism-specific databases

HPAiHPA000993.

Interactioni

Subunit structurei

Interacts with CRB3, LIN7C and MPDZ. Interacts with INADL, PARD6B, SC6A1 and EZR (By similarity). Forms a complex with CRB1 and MPP4. Component of a complex whose core is composed of ARHGAP17, AMOT, MPP5/PALS1, INADL/PATJ and PARD3/PAR3. Heterodimer with MPP1. Interacts with MPP7.By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
INADLQ8NI354EBI-2513978,EBI-724390
LIN7AO149105EBI-2513978,EBI-2513988

Protein-protein interaction databases

BioGridi122155. 24 interactions.
IntActiQ8N3R9. 18 interactions.
MINTiMINT-1772982.
STRINGi9606.ENSP00000261681.

Structurei

Secondary structure

1
675
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi124 – 13714Combined sources
Helixi141 – 15515Combined sources
Helixi157 – 17317Combined sources
Helixi186 – 19712Combined sources
Turni198 – 2003Combined sources
Helixi203 – 21311Combined sources
Helixi215 – 22915Combined sources
Beta strandi230 – 2323Combined sources
Beta strandi249 – 2513Combined sources
Beta strandi255 – 2617Combined sources
Beta strandi268 – 2747Combined sources
Beta strandi277 – 2837Combined sources
Helixi288 – 2925Combined sources
Beta strandi300 – 3045Combined sources
Helixi314 – 3229Combined sources
Beta strandi326 – 3338Combined sources
Beta strandi348 – 3525Combined sources
Helixi358 – 3603Combined sources
Helixi367 – 3693Combined sources
Beta strandi378 – 3836Combined sources
Beta strandi389 – 3946Combined sources
Beta strandi405 – 4084Combined sources
Beta strandi464 – 4729Combined sources
Beta strandi482 – 4865Combined sources
Turni488 – 4914Combined sources
Helixi492 – 50211Combined sources
Turni503 – 5064Combined sources
Turni524 – 5274Combined sources
Helixi533 – 5419Combined sources
Beta strandi545 – 5517Combined sources
Beta strandi554 – 5596Combined sources
Helixi560 – 5678Combined sources
Turni568 – 5703Combined sources
Beta strandi571 – 5766Combined sources
Helixi579 – 5813Combined sources
Helixi582 – 5865Combined sources
Beta strandi593 – 5986Combined sources
Helixi602 – 6087Combined sources
Helixi621 – 63111Combined sources
Helixi634 – 6363Combined sources
Beta strandi639 – 6446Combined sources
Helixi648 – 66013Combined sources
Turni661 – 6644Combined sources
Beta strandi667 – 6704Combined sources
Helixi671 – 6733Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Y76NMR-B/D118-177[»]
3UITX-ray2.05A/B/C/D119-232[»]
A/B/C/D260-326[»]
4UU5X-ray1.23A251-335[»]
4UU6X-ray1.80A251-335[»]
4WSIX-ray2.95A/B236-675[»]
ProteinModelPortaliQ8N3R9.
SMRiQ8N3R9. Positions 119-232, 236-335, 349-671.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8N3R9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini120 – 17758L27 1PROSITE-ProRule annotationAdd
BLAST
Domaini179 – 23557L27 2PROSITE-ProRule annotationAdd
BLAST
Domaini256 – 33681PDZPROSITE-ProRule annotationAdd
BLAST
Domaini345 – 41773SH3PROSITE-ProRule annotationAdd
BLAST
Domaini479 – 660182Guanylate kinase-likePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni21 – 140120Interaction with PARD6BBy similarityAdd
BLAST
Regioni181 – 24363Interaction with LIN7CBy similarityAdd
BLAST

Domaini

The L27 domain 1 functions in targeting to the tight junctions by binding to INADL.By similarity
The PDZ domain binds to the C-terminus of SC6A1.By similarity

Sequence similaritiesi

Belongs to the MAGUK family.Curated
Contains 1 guanylate kinase-like domain.PROSITE-ProRule annotation
Contains 2 L27 domains.PROSITE-ProRule annotation
Contains 1 PDZ (DHR) domain.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, SH3 domain

Phylogenomic databases

eggNOGiCOG0194.
GeneTreeiENSGT00760000118866.
HOGENOMiHOG000233034.
HOVERGENiHBG001858.
InParanoidiQ8N3R9.
KOiK06091.
OMAiVHQKEGQ.
OrthoDBiEOG79CXZ5.
PhylomeDBiQ8N3R9.
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.
IPR020590. Guanylate_kinase_CS.
IPR004172. L27.
IPR014775. L27_C.
IPR015145. L27_N.
IPR027417. P-loop_NTPase.
IPR001478. PDZ.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF00625. Guanylate_kin. 1 hit.
PF02828. L27. 1 hit.
PF09060. L27_N. 1 hit.
PF00595. PDZ. 1 hit.
PF07653. SH3_2. 1 hit.
[Graphical view]
SMARTiSM00072. GuKc. 1 hit.
SM00569. L27. 2 hits.
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.
PS51022. L27. 2 hits.
PS50106. PDZ. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8N3R9-1) [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
MTTSHMNGHV TEESDSEVKN VDLASPEEHQ KHREMAVDCP GDLGTRMMPI
60 70 80 90 100
RRSAQLERIR QQQEDMRRRR EEEGKKQELD LNSSMRLKKL AQIPPKTGID
110 120 130 140 150
NPMFDTEEGI VLESPHYAVK ILEIEDLFSS LKHIQHTLVD SQSQEDISLL
160 170 180 190 200
LQLVQNKDFQ NAFKIHNAIT VHMNKASPPF PLISNAQDLA QEVQTVLKPV
210 220 230 240 250
HHKEGQELTA LLNTPHIQAL LLAHDKVAEQ EMQLEPITDE RVYESIGQYG
260 270 280 290 300
GETVKIVRIE KARDIPLGAT VRNEMDSVII SRIVKGGAAE KSGLLHEGDE
310 320 330 340 350
VLEINGIEIR GKDVNEVFDL LSDMHGTLTF VLIPSQQIKP PPAKETVIHV
360 370 380 390 400
KAHFDYDPSD DPYVPCRELG LSFQKGDILH VISQEDPNWW QAYREGDEDN
410 420 430 440 450
QPLAGLVPGK SFQQQREAMK QTIEEDKEPE KSGKLWCAKK NKKKRKKVLY
460 470 480 490 500
NANKNDDYDN EEILTYEEMS LYHQPANRKR PIILIGPQNC GQNELRQRLM
510 520 530 540 550
NKEKDRFASA VPHTTRSRRD QEVAGRDYHF VSRQAFEADI AAGKFIEHGE
560 570 580 590 600
FEKNLYGTSI DSVRQVINSG KICLLSLRTQ SLKTLRNSDL KPYIIFIAPP
610 620 630 640 650
SQERLRALLA KEGKNPKPEE LREIIEKTRE MEQNNGHYFD TAIVNSDLDK
660 670
AYQELLRLIN KLDTEPQWVP STWLR
Length:675
Mass (Da):77,294
Last modified:October 17, 2006 - v3
Checksum:iA3B2CB594E0908CA
GO
Isoform 2 (identifier: Q8N3R9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-34: Missing.

Show »
Length:641
Mass (Da):73,421
Checksum:iAD604D26B3580FDB
GO

Sequence cautioni

The sequence AAH53366.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated
The sequence BAB14172.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti100 – 1001D → G in CAD38620 (PubMed:17974005).Curated
Sequence conflicti141 – 1411S → Y in CAD89937 (PubMed:17974005).Curated
Sequence conflicti161 – 1611N → S in BAC05295 (PubMed:14702039).Curated
Sequence conflicti324 – 3241M → L in BAC05295 (PubMed:14702039).Curated
Sequence conflicti401 – 4011Q → H in CAD89937 (PubMed:17974005).Curated
Sequence conflicti460 – 4601N → H in CAD89937 (PubMed:17974005).Curated
Sequence conflicti490 – 4901C → F in BAB14172 (PubMed:14702039).Curated
Sequence conflicti613 – 6131G → V in CAD38620 (PubMed:17974005).Curated
Sequence conflicti634 – 6341N → S in CAD38620 (PubMed:17974005).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3434Missing in isoform 2. 1 PublicationVSP_014002Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL832326 mRNA. Translation: CAD38620.1.
AL832578 mRNA. Translation: CAD89937.1.
CH471061 Genomic DNA. Translation: EAW80930.1.
BC053366 mRNA. Translation: AAH53366.1. Sequence problems.
BC129933 mRNA. Translation: AAI29934.1.
AK022677 mRNA. Translation: BAB14172.1. Different initiation.
AK098373 mRNA. Translation: BAC05295.1.
CCDSiCCDS58325.1. [Q8N3R9-2]
CCDS9779.1. [Q8N3R9-1]
RefSeqiNP_001243479.1. NM_001256550.1. [Q8N3R9-2]
NP_071919.2. NM_022474.3. [Q8N3R9-1]
XP_005268060.1. XM_005268003.1. [Q8N3R9-2]
UniGeneiHs.652312.
Hs.740524.

Genome annotation databases

EnsembliENST00000261681; ENSP00000261681; ENSG00000072415. [Q8N3R9-1]
ENST00000555925; ENSP00000451488; ENSG00000072415. [Q8N3R9-2]
GeneIDi64398.
KEGGihsa:64398.
UCSCiuc001xjc.4. human. [Q8N3R9-1]

Polymorphism and mutation databases

BioMutaiMPP5.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL832326 mRNA. Translation: CAD38620.1.
AL832578 mRNA. Translation: CAD89937.1.
CH471061 Genomic DNA. Translation: EAW80930.1.
BC053366 mRNA. Translation: AAH53366.1. Sequence problems.
BC129933 mRNA. Translation: AAI29934.1.
AK022677 mRNA. Translation: BAB14172.1. Different initiation.
AK098373 mRNA. Translation: BAC05295.1.
CCDSiCCDS58325.1. [Q8N3R9-2]
CCDS9779.1. [Q8N3R9-1]
RefSeqiNP_001243479.1. NM_001256550.1. [Q8N3R9-2]
NP_071919.2. NM_022474.3. [Q8N3R9-1]
XP_005268060.1. XM_005268003.1. [Q8N3R9-2]
UniGeneiHs.652312.
Hs.740524.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Y76NMR-B/D118-177[»]
3UITX-ray2.05A/B/C/D119-232[»]
A/B/C/D260-326[»]
4UU5X-ray1.23A251-335[»]
4UU6X-ray1.80A251-335[»]
4WSIX-ray2.95A/B236-675[»]
ProteinModelPortaliQ8N3R9.
SMRiQ8N3R9. Positions 119-232, 236-335, 349-671.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122155. 24 interactions.
IntActiQ8N3R9. 18 interactions.
MINTiMINT-1772982.
STRINGi9606.ENSP00000261681.

PTM databases

PhosphoSiteiQ8N3R9.

Polymorphism and mutation databases

BioMutaiMPP5.
DMDMi116242632.

Proteomic databases

MaxQBiQ8N3R9.
PaxDbiQ8N3R9.
PRIDEiQ8N3R9.

Protocols and materials databases

DNASUi64398.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000261681; ENSP00000261681; ENSG00000072415. [Q8N3R9-1]
ENST00000555925; ENSP00000451488; ENSG00000072415. [Q8N3R9-2]
GeneIDi64398.
KEGGihsa:64398.
UCSCiuc001xjc.4. human. [Q8N3R9-1]

Organism-specific databases

CTDi64398.
GeneCardsiGC14P067708.
HGNCiHGNC:18669. MPP5.
HPAiHPA000993.
MIMi606958. gene.
neXtProtiNX_Q8N3R9.
PharmGKBiPA38631.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0194.
GeneTreeiENSGT00760000118866.
HOGENOMiHOG000233034.
HOVERGENiHBG001858.
InParanoidiQ8N3R9.
KOiK06091.
OMAiVHQKEGQ.
OrthoDBiEOG79CXZ5.
PhylomeDBiQ8N3R9.
TreeFamiTF314263.

Enzyme and pathway databases

ReactomeiREACT_19373. Tight junction interactions.

Miscellaneous databases

ChiTaRSiMPP5. human.
EvolutionaryTraceiQ8N3R9.
GeneWikiiMPP5.
GenomeRNAii64398.
NextBioi66338.
PROiQ8N3R9.
SOURCEiSearch...

Gene expression databases

BgeeiQ8N3R9.
CleanExiHS_MPP5.
ExpressionAtlasiQ8N3R9. baseline and differential.
GenevestigatoriQ8N3R9.

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.
IPR020590. Guanylate_kinase_CS.
IPR004172. L27.
IPR014775. L27_C.
IPR015145. L27_N.
IPR027417. P-loop_NTPase.
IPR001478. PDZ.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF00625. Guanylate_kin. 1 hit.
PF02828. L27. 1 hit.
PF09060. L27_N. 1 hit.
PF00595. PDZ. 1 hit.
PF07653. SH3_2. 1 hit.
[Graphical view]
SMARTiSM00072. GuKc. 1 hit.
SM00569. L27. 2 hits.
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.
PS51022. L27. 2 hits.
PS50106. PDZ. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Skeletal muscle and Spinal cord.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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: Eye.
  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] OF 1-441 (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 155-675.
    Tissue: Brain.
  5. Cited for: COMPLEX FORMATION WITH CRB1 AND MPP4, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  6. "Membrane-associated guanylate kinase proteins MPP4 and MPP5 associate with Veli3 at distinct intercellular junctions of the neurosensory retina."
    Stoehr H., Molday L.L., Molday R.S., Weber B.H.F., Biedermann B., Reichenbach A., Kraemer F.
    J. Comp. Neurol. 481:31-41(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  7. "A Rich1/Amot complex regulates the Cdc42 GTPase and apical-polarity proteins in epithelial cells."
    Wells C.D., Fawcett J.P., Traweger A., Yamanaka Y., Goudreault M., Elder K., Kulkarni S., Gish G., Virag C., Lim C., Colwill K., Starostine A., Metalnikov P., Pawson T.
    Cell 125:535-548(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN A COMPLEX WITH ARHGAP17; AMOT; INADL AND PARD3, INTERACTION WITH MPP7.
  8. "The MAGUK protein MPP7 binds to the polarity protein hDlg1 and facilitates epithelial tight junction formation."
    Stucke V.M., Timmerman E., Vandekerckhove J., Gevaert K., Hall A.
    Mol. Biol. Cell 18:1744-1755(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MPP7.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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-25, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-84, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  12. "A unified assembly mode revealed by the structures of tetrameric L27 domain complexes formed by mLin-2/mLin-7 and Patj/Pals1 scaffold proteins."
    Feng W., Long J.-F., Zhang M.
    Proc. Natl. Acad. Sci. U.S.A. 102:6861-6866(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 118-177, INTERACTION WITH MPDZ.
  13. Cited for: INTERACTION WITH MPP1, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiMPP5_HUMAN
AccessioniPrimary (citable) accession number: Q8N3R9
Secondary accession number(s): A1L380
, Q7Z631, Q86T98, Q8N7I5, Q9H9Q0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2003
Last sequence update: October 17, 2006
Last modified: April 29, 2015
This is version 140 of the entry and version 3 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, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.