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Q8N3R9

- MPP5_HUMAN

UniProt

Q8N3R9 - MPP5_HUMAN

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Protein

MAGUK p55 subfamily member 5

Gene

MPP5

Organism
Homo sapiens (Human)
Status
Reviewed - 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: UniProt
  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: Chromosome 14

Organism-specific databases

HGNCiHGNC:18669. MPP5.

Subcellular locationi

Cell membrane; Peripheral membrane protein. Endomembrane system; Peripheral membrane protein. Cell junctiontight junction
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. extracellular vesicular exosome Source: UniProtKB
  3. lateral loop Source: Ensembl
  4. myelin sheath adaxonal region Source: Ensembl
  5. nucleus Source: HPA
  6. plasma membrane Source: HPA
  7. protein complex Source: Ensembl
  8. Schmidt-Lanterman incisure Source: Ensembl
  9. tight junction Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Tight junction

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA38631.

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

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

Protein-protein interaction databases

BioGridi122155. 16 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
Helixi264 – 27613Combined sources
Helixi279 – 2857Combined sources
Helixi294 – 30310Combined sources
Helixi305 – 32016Combined 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[»]
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. Align

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. Reason: 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 databases

DMDMi116242632.

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 .
CCDSi CCDS58325.1. [Q8N3R9-2 ]
CCDS9779.1. [Q8N3R9-1 ]
RefSeqi NP_001243479.1. NM_001256550.1. [Q8N3R9-2 ]
NP_071919.2. NM_022474.3. [Q8N3R9-1 ]
XP_005268060.1. XM_005268003.1. [Q8N3R9-2 ]
UniGenei Hs.652312.
Hs.740524.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1Y76 NMR - B/D 118-177 [» ]
3UIT X-ray 2.05 A/B/C/D 119-232 [» ]
ProteinModelPortali Q8N3R9.
SMRi Q8N3R9. Positions 119-232, 236-335, 349-671.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 122155. 16 interactions.
IntActi Q8N3R9. 18 interactions.
MINTi MINT-1772982.
STRINGi 9606.ENSP00000261681.

PTM databases

PhosphoSitei Q8N3R9.

Polymorphism databases

DMDMi 116242632.

Proteomic databases

MaxQBi Q8N3R9.
PaxDbi Q8N3R9.
PRIDEi Q8N3R9.

Protocols and materials databases

DNASUi 64398.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000261681 ; ENSP00000261681 ; ENSG00000072415 . [Q8N3R9-1 ]
ENST00000555925 ; ENSP00000451488 ; ENSG00000072415 . [Q8N3R9-2 ]
GeneIDi 64398.
KEGGi hsa:64398.
UCSCi uc001xjc.4. human. [Q8N3R9-1 ]

Organism-specific databases

CTDi 64398.
GeneCardsi GC14P067708.
HGNCi HGNC:18669. MPP5.
HPAi HPA000993.
MIMi 606958. gene.
neXtProti NX_Q8N3R9.
PharmGKBi PA38631.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0194.
GeneTreei ENSGT00760000118866.
HOGENOMi HOG000233034.
HOVERGENi HBG001858.
InParanoidi Q8N3R9.
KOi K06091.
OMAi VHQKEGQ.
OrthoDBi EOG79CXZ5.
PhylomeDBi Q8N3R9.
TreeFami TF314263.

Enzyme and pathway databases

Reactomei REACT_19373. Tight junction interactions.

Miscellaneous databases

ChiTaRSi MPP5. human.
EvolutionaryTracei Q8N3R9.
GeneWikii MPP5.
GenomeRNAii 64398.
NextBioi 66338.
PROi Q8N3R9.
SOURCEi Search...

Gene expression databases

Bgeei Q8N3R9.
CleanExi HS_MPP5.
ExpressionAtlasi Q8N3R9. baseline and differential.
Genevestigatori Q8N3R9.

Family and domain databases

Gene3Di 2.30.42.10. 1 hit.
3.40.50.300. 2 hits.
InterProi IPR008145. 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 ]
Pfami PF00625. Guanylate_kin. 1 hit.
PF02828. L27. 1 hit.
PF09060. L27_N. 1 hit.
PF00595. PDZ. 1 hit.
PF07653. SH3_2. 1 hit.
[Graphical view ]
SMARTi SM00072. GuKc. 1 hit.
SM00569. L27. 2 hits.
SM00228. PDZ. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 1 hit.
SSF50156. SSF50156. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEi PS00856. 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 ]
ProtoNeti Search...

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. "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.
  12. 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: November 26, 2014
This is version 135 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