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Q6WCQ1

- MPRIP_HUMAN

UniProt

Q6WCQ1 - MPRIP_HUMAN

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Protein

Myosin phosphatase Rho-interacting protein

Gene

MPRIP

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

Functioni

Targets myosin phosphatase to the actin cytoskeleton. Required for the regulation of the actin cytoskeleton by RhoA and ROCK1. Depletion leads to an increased number of stress fibers in smooth muscle cells through stabilization of actin fibers by phosphorylated myosin. Overexpression of MRIP as well as its F-actin-binding region leads to disassembly of stress fibers in neuronal cells.By similarity2 Publications

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Myosin phosphatase Rho-interacting protein
Short name:
M-RIP
Alternative name(s):
Rho-interacting protein 3
Short name:
RIP3
p116Rip
Gene namesi
Name:MPRIP
Synonyms:KIAA0864, MRIP, RHOIP3Imported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:30321. MPRIP.

Subcellular locationi

Cytoplasmcytoskeleton 2 Publications
Note: Colocalizes with F-actin.

GO - Cellular componenti

  1. actin cytoskeleton Source: HPA
  2. cytoplasm Source: HPA
  3. focal adhesion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162396092.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini2 – 10251024Myosin phosphatase Rho-interacting proteinPRO_0000223930Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei192 – 1921Phosphoserine1 Publication
Modified residuei220 – 2201Phosphoserine2 Publications
Modified residuei224 – 2241Phosphoserine1 Publication
Modified residuei226 – 2261Phosphoserine1 Publication
Modified residuei269 – 2691Phosphoserine1 Publication
Modified residuei289 – 2891Phosphoserine3 Publications
Modified residuei292 – 2921Phosphoserine1 Publication
Modified residuei295 – 2951Phosphothreonine1 Publication
Modified residuei362 – 3621Phosphoserine2 Publications
Modified residuei365 – 3651Phosphoserine2 Publications
Modified residuei619 – 6191Phosphoserine3 Publications
Modified residuei891 – 8911Phosphoserine2 Publications
Modified residuei977 – 9771Phosphoserine3 Publications
Modified residuei993 – 9931Phosphoserine1 Publication
Modified residuei1016 – 10161Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ6WCQ1.
PaxDbiQ6WCQ1.
PRIDEiQ6WCQ1.

PTM databases

PhosphoSiteiQ6WCQ1.

Expressioni

Gene expression databases

BgeeiQ6WCQ1.
CleanExiHS_MPRIP.
ExpressionAtlasiQ6WCQ1. baseline and differential.
GenevestigatoriQ6WCQ1.

Organism-specific databases

HPAiHPA022901.

Interactioni

Subunit structurei

Binds F-actin through its N-terminus. Interacts with MYZAP (By similarity). Binds RHOA, PPP1R12A/MBS and PPP1R12C/MBS85 through adjacent coiled coil domains.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Ppp1r12aQ107286EBI-1022605,EBI-918263From a different organism.

Protein-protein interaction databases

BioGridi116776. 36 interactions.
IntActiQ6WCQ1. 16 interactions.
MINTiMINT-1161017.
STRINGi9606.ENSP00000379156.

Structurei

3D structure databases

ProteinModelPortaliQ6WCQ1.
SMRiQ6WCQ1. Positions 390-482.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini43 – 150108PH 1PROSITE-ProRule annotationAdd
BLAST
Domaini387 – 48397PH 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 383383Interaction with F-actinBy similarityAdd
BLAST
Regioni546 – 824279Interaction with RHOAAdd
BLAST
Regioni824 – 87956Interaction with PPP1R12AAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili673 – 977305Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi179 – 25274Ser-richAdd
BLAST

Sequence similaritiesi

Contains 2 PH domains.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiNOG243797.
GeneTreeiENSGT00530000063678.
HOVERGENiHBG023864.
InParanoidiQ6WCQ1.
OrthoDBiEOG773XKP.
PhylomeDBiQ6WCQ1.
TreeFamiTF329258.

Family and domain databases

Gene3Di2.30.29.30. 2 hits.
InterProiIPR001849. PH_domain.
IPR011993. PH_like_dom.
[Graphical view]
PfamiPF00169. PH. 2 hits.
[Graphical view]
SMARTiSM00233. PH. 2 hits.
[Graphical view]
PROSITEiPS50003. PH_DOMAIN. 2 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 11 Publication (identifier: Q6WCQ1-1) [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
MSAAKENPCR KFQANIFNKS KCQNCFKPRE SHLLNDEDLT QAKPIYGGWL
60 70 80 90 100
LLAPDGTDFD NPVHRSRKWQ RRFFILYEHG LLRYALDEMP TTLPQGTINM
110 120 130 140 150
NQCTDVVDGE GRTGQKFSLC ILTPEKEHFI RAETKEIVSG WLEMLMVYPR
160 170 180 190 200
TNKQNQKKKR KVEPPTPQEP GPAKVAVTSS SSSSSSSSSI PSAEKVPTTK
210 220 230 240 250
STLWQEEMRT KDQPDGSSLS PAQSPSQSQP PAASSLREPG LESKEEESAM
260 270 280 290 300
SSDRMDCGRK VRVESGYFSL EKTKQDLKAE EQQLPPPLSP PSPSTPNHRR
310 320 330 340 350
SQVIEKFEAL DIEKAEHMET NAVGPSPSSD TRQGRSEKRA FPRKRDFTNE
360 370 380 390 400
APPAPLPDAS ASPLSPHRRA KSLDRRSTEP SVTPDLLNFK KGWLTKQYED
410 420 430 440 450
GQWKKHWFVL ADQSLRYYRD SVAEEAADLD GEIDLSACYD VTEYPVQRNY
460 470 480 490 500
GFQIHTKEGE FTLSAMTSGI RRNWIQTIMK HVHPTTAPDV TSSLPEEKNK
510 520 530 540 550
SSCSFETCPR PTEKQEAELG EPDPEQKRSR ARERRREGRS KTFDWAEFRP
560 570 580 590 600
IQQALAQERV GGVGPADTHE PLRPEAEPGE LERERARRRE ERRKRFGMLD
610 620 630 640 650
ATDGPGTEDA ALRMEVDRSP GLPMSDLKTH NVHVEIEQRW HQVETTPLRE
660 670 680 690 700
EKQVPIAPVH LSSEDGGDRL STHELTSLLE KELEQSQKEA SDLLEQNRLL
710 720 730 740 750
QDQLRVALGR EQSAREGYVL QATCERGFAA MEETHQKKIE DLQRQHQREL
760 770 780 790 800
EKLREEKDRL LAEETAATIS AIEAMKNAHR EEMERELEKS QRSQISSVNS
810 820 830 840 850
DVEALRRQYL EELQSVQREL EVLSEQYSQK CLENAHLAQA LEAERQALRQ
860 870 880 890 900
CQRENQELNA HNQELNNRLA AEITRLRTLL TGDGGGEATG SPLAQGKDAY
910 920 930 940 950
ELEVLLRVKE SEIQYLKQEI SSLKDELQTA LRDKKYASDK YKDIYTELSI
960 970 980 990 1000
AKAKADCDIS RLKEQLKAAT EALGEKSPDS ATVSGYDIMK SKSNPDFLKK
1010 1020
DRSCVTRQLR NIRSKSVIEQ VSWDT
Length:1,025
Mass (Da):116,533
Last modified:November 25, 2008 - v3
Checksum:i5B7A30CDB3685E4E
GO
Isoform 21 Publication (identifier: Q6WCQ1-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1017-1025: VIEQVSWDT → LKEGLTVQERLKLFESRDLKKD

Show »
Length:1,038
Mass (Da):118,103
Checksum:iEE674842C8133516
GO
Isoform 3Curated (identifier: Q6WCQ1-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     346-383: Missing.
     1017-1025: VIEQVSWDT → LKEGLTVQERLKLFESRDLKKD

Show »
Length:1,000
Mass (Da):114,049
Checksum:iFCFDB3210A73EEF9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti31 – 311S → P in AAQ63176. (PubMed:14506264)Curated
Sequence conflicti184 – 1841S → R in BAD89507. (PubMed:15545284)Curated
Sequence conflicti188 – 1892Missing in BAD89507. (PubMed:15545284)Curated
Sequence conflicti188 – 1892Missing in AAH09982. (PubMed:15489334)Curated
Sequence conflicti189 – 1891Missing in AAQ63176. (PubMed:14506264)Curated
Sequence conflicti189 – 1891Missing in BAC78198. 1 PublicationCurated
Sequence conflicti189 – 1891Missing in CAD39169. (PubMed:17974005)Curated
Sequence conflicti235 – 2351S → F in BAD89507. (PubMed:15545284)Curated
Sequence conflicti352 – 3521P → S in BAD89507. (PubMed:15545284)Curated
Sequence conflicti528 – 5281R → T in AAQ63176. (PubMed:14506264)Curated
Sequence conflicti550 – 5501P → L in BAC78198. 1 PublicationCurated
Sequence conflicti550 – 5501P → L in CAD39169. (PubMed:17974005)Curated
Sequence conflicti578 – 5781P → S in AAQ63176. (PubMed:14506264)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti327 – 3271P → Q.2 Publications
Corresponds to variant rs3744137 [ dbSNP | Ensembl ].
VAR_051203

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei346 – 38338Missing in isoform 3. 1 PublicationVSP_051947Add
BLAST
Alternative sequencei1017 – 10259VIEQVSWDT → LKEGLTVQERLKLFESRDLK KD in isoform 2 and isoform 3. 3 PublicationsVSP_051948

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY296247 mRNA. Translation: AAQ63176.1.
AB189741 mRNA. Translation: BAD89507.1.
AB098507 mRNA. Translation: BAC78198.1.
AC079111 Genomic DNA. No translation available.
AC055811 Genomic DNA. No translation available.
AL834513 mRNA. Translation: CAD39169.1.
BC009982 mRNA. Translation: AAH09982.2.
BC075847 mRNA. Translation: AAH75847.1.
BC105987 mRNA. Translation: AAI05988.1.
CCDSiCCDS32578.1. [Q6WCQ1-1]
CCDS42268.1. [Q6WCQ1-2]
RefSeqiNP_055949.2. NM_015134.3. [Q6WCQ1-2]
NP_958431.2. NM_201274.3. [Q6WCQ1-1]
UniGeneiHs.462341.

Genome annotation databases

EnsembliENST00000341712; ENSP00000342379; ENSG00000133030. [Q6WCQ1-1]
ENST00000395811; ENSP00000379156; ENSG00000133030. [Q6WCQ1-2]
GeneIDi23164.
KEGGihsa:23164.
UCSCiuc002gqu.2. human. [Q6WCQ1-1]
uc002gqv.2. human. [Q6WCQ1-2]

Polymorphism databases

DMDMi215274136.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY296247 mRNA. Translation: AAQ63176.1 .
AB189741 mRNA. Translation: BAD89507.1 .
AB098507 mRNA. Translation: BAC78198.1 .
AC079111 Genomic DNA. No translation available.
AC055811 Genomic DNA. No translation available.
AL834513 mRNA. Translation: CAD39169.1 .
BC009982 mRNA. Translation: AAH09982.2 .
BC075847 mRNA. Translation: AAH75847.1 .
BC105987 mRNA. Translation: AAI05988.1 .
CCDSi CCDS32578.1. [Q6WCQ1-1 ]
CCDS42268.1. [Q6WCQ1-2 ]
RefSeqi NP_055949.2. NM_015134.3. [Q6WCQ1-2 ]
NP_958431.2. NM_201274.3. [Q6WCQ1-1 ]
UniGenei Hs.462341.

3D structure databases

ProteinModelPortali Q6WCQ1.
SMRi Q6WCQ1. Positions 390-482.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116776. 36 interactions.
IntActi Q6WCQ1. 16 interactions.
MINTi MINT-1161017.
STRINGi 9606.ENSP00000379156.

PTM databases

PhosphoSitei Q6WCQ1.

Polymorphism databases

DMDMi 215274136.

Proteomic databases

MaxQBi Q6WCQ1.
PaxDbi Q6WCQ1.
PRIDEi Q6WCQ1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000341712 ; ENSP00000342379 ; ENSG00000133030 . [Q6WCQ1-1 ]
ENST00000395811 ; ENSP00000379156 ; ENSG00000133030 . [Q6WCQ1-2 ]
GeneIDi 23164.
KEGGi hsa:23164.
UCSCi uc002gqu.2. human. [Q6WCQ1-1 ]
uc002gqv.2. human. [Q6WCQ1-2 ]

Organism-specific databases

CTDi 23164.
GeneCardsi GC17P016946.
HGNCi HGNC:30321. MPRIP.
HPAi HPA022901.
MIMi 612935. gene.
neXtProti NX_Q6WCQ1.
PharmGKBi PA162396092.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG243797.
GeneTreei ENSGT00530000063678.
HOVERGENi HBG023864.
InParanoidi Q6WCQ1.
OrthoDBi EOG773XKP.
PhylomeDBi Q6WCQ1.
TreeFami TF329258.

Miscellaneous databases

ChiTaRSi MPRIP. human.
GeneWikii M-RIP.
GenomeRNAii 23164.
NextBioi 44551.
PROi Q6WCQ1.
SOURCEi Search...

Gene expression databases

Bgeei Q6WCQ1.
CleanExi HS_MPRIP.
ExpressionAtlasi Q6WCQ1. baseline and differential.
Genevestigatori Q6WCQ1.

Family and domain databases

Gene3Di 2.30.29.30. 2 hits.
InterProi IPR001849. PH_domain.
IPR011993. PH_like_dom.
[Graphical view ]
Pfami PF00169. PH. 2 hits.
[Graphical view ]
SMARTi SM00233. PH. 2 hits.
[Graphical view ]
PROSITEi PS50003. PH_DOMAIN. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Myosin phosphatase-Rho interacting protein. A new member of the myosin phosphatase complex that directly binds RhoA."
    Surks H.K., Richards C.T., Mendelsohn M.E.
    J. Biol. Chem. 278:51484-51493(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, INTERACTION WITH PPP1R12A AND RHOA.
    Tissue: AortaImported.
  2. "p116Rip decreases myosin II phosphorylation by activating myosin light chain phosphatase and by inactivating RhoA."
    Koga Y., Ikebe M.
    J. Biol. Chem. 280:4983-4991(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH PPP1R12A.
  3. "Cloning of human orthologue RHOIP3 of Mus Rhoip3."
    Inazawa J., Imoto I.
    Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT GLN-327.
  4. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 38-1025 (ISOFORM 1), VARIANT GLN-327.
    Tissue: Melanoma.
  6. "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] OF 157-1025 (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 194-1025 (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 377-1025 (ISOFORM 2).
    Tissue: BrainImported, LymphImported and MuscleImported.
  7. "M-RIP targets myosin phosphatase to stress fibers to regulate myosin light chain phosphorylation in vascular smooth muscle cells."
    Surks H.K., Riddick N., Ohtani K.
    J. Biol. Chem. 280:42543-42551(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PPP1R12A AND F-ACTIN.
  8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-619, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192; SER-220; SER-224; SER-226; SER-289; SER-292; THR-295; SER-362; SER-365; SER-619; SER-891 AND SER-977, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  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-220; SER-269; SER-289; SER-362; SER-365; SER-619; SER-891 AND SER-977, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-977; SER-993 AND SER-1016, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMPRIP_HUMAN
AccessioniPrimary (citable) accession number: Q6WCQ1
Secondary accession number(s): Q3KQZ5
, Q5FB94, Q6DHW2, Q7Z5Y2, Q8N390, Q96G40
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2006
Last sequence update: November 25, 2008
Last modified: October 29, 2014
This is version 97 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3