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Protein

Mitotic interactor and substrate of PLK1

Gene

MISP

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

Functioni

Plays a role in mitotic spindle orientation and mitotic progression. Regulates the distribution of dynactin at the cell cortex in a PLK1-dependent manner, thus stabilizing cortical and astral microtubule attachments required for proper mitotic spindle positioning. May link microtubules to the actin cytospkeleton and focal adhesions. May be required for directed cell migration and centrosome orientation. May also be necessary for proper stacking of the Golgi apparatus.2 Publications

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Mitotic interactor and substrate of PLK1
Alternative name(s):
Mitotic spindle positioning protein
Gene namesi
Name:MISP
Synonyms:C19orf21
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:27000. MISP.

Subcellular locationi

  • Cell junctionfocal adhesion
  • Cytoplasmcytoskeleton
  • Cytoplasmcell cortex

  • Note: Predominantly localizes to cortical actin structures during interphase and mitosis. Present in retraction fibers, which are formed at former adhesion sites during mitosis, and at spicular membrane protrusions in re-attaching cytokinetic cells. Partially colocalizes with cytoplasmic F-actin. Not detected at microtubules at interphase, nor at spindle during mitosis.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Cytoskeleton

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi78 – 781S → A: Almost complete loss of CDK1 phosphorylation in vitro, loss of PLK1-binding, no effect on cortical localization; when associated with A-164; A-172; A-214; A-224; A-284; A-287; A-377 and A-575. 1 Publication
Mutagenesisi164 – 1641T → A: Almost complete loss of CDK1 phosphorylation in vitro, loss of PLK1-binding, no effect on cortical localization; when associated with A-78; A-172; A-214; A-224; A-284; A-287; A-377 and A-575. 1 Publication
Mutagenesisi172 – 1721T → A: Almost complete loss of CDK1 phosphorylation in vitro, loss of PLK1-binding, no effect on cortical localization; when associated with A-78; A-164; A-214; A-224; A-284; A-287; A-377 and A-575. 1 Publication
Mutagenesisi214 – 2141S → A: Almost complete loss of CDK1 phosphorylation in vitro, loss of PLK1-binding, no effect on cortical localization; when associated with A-78; A-164; A-172; A-224; A-284; A-287; A-377 and A-575. 1 Publication
Mutagenesisi224 – 2241T → A: Almost complete loss of CDK1 phosphorylation in vitro, loss of PLK1-binding, no effect on cortical localization; when associated with A-78; A-164; A-172; A-214; A-284; A-287; A-377 and A-575. 1 Publication
Mutagenesisi284 – 2841S → A: Almost complete loss of CDK1 phosphorylation in vitro, loss of PLK1-binding, no effect on cortical localization; when associated with A-78; A-164; A-172; A-214; A-224; A-287; A-377 and A-575. 1 Publication
Mutagenesisi287 – 2871T → A: Almost complete loss of CDK1 phosphorylation in vitro, loss of PLK1-binding, no effect on cortical localization; when associated with A-78; A-164; A-172; A-214; A-224; A-284; A-377 and A-575. 1 Publication
Mutagenesisi377 – 3771T → A: Almost complete loss of CDK1 phosphorylation in vitro, loss of PLK1-binding, no effect on cortical localization; when associated with A-78; A-164; A-172; A-214; A-224; A-284; A-287 and A-575. 1 Publication
Mutagenesisi382 – 3821S → A: Almost complete loss of CDK1 phosphorylation in vitro, loss of PLK1-binding, no effect on cortical localization; when associated with A-394; A-395; A-397; A-471; A-582 and A-586. 1 Publication
Mutagenesisi394 – 3941S → A: Drastic reduction in PLK1 phosphorylation in vitro, no effect on cortical localization; when associated with A-382; A-395; A-397; A-471; A-582 and A-586. 1 Publication
Mutagenesisi394 – 3941S → D: No effect on cortical localization; when associated with D-395; D-397; D-471; D-582 and D-586. 1 Publication
Mutagenesisi395 – 3951S → A: Drastic reduction in PLK1 phosphorylation in vitro, no effect on cortical localization; when associated with A-382; A-394; A-397; A-471; A-582 and A-586. 1 Publication
Mutagenesisi395 – 3951S → D: No effect on cortical localization; when associated with D-394; D-397; D-471; D-582 and D-586. 1 Publication
Mutagenesisi397 – 3971S → A: Drastic reduction in PLK1 phosphorylation in vitro, no effect on cortical localization; when associated with A-382; A-394; A-395; A-471; A-582 and A-586. 1 Publication
Mutagenesisi397 – 3971S → D: No effect on cortical localization; when associated with D-394; D-395; D-471; D-582 and D-586. 1 Publication
Mutagenesisi471 – 4711S → A: Drastic reduction in PLK1 phosphorylation in vitro, no effect on cortical localization; when associated with A-382; A-394; A-395; A-397; A-582 and A-586. 1 Publication
Mutagenesisi471 – 4711S → D: No effect on cortical localization; when associated with D-394; D-395; D-397; D-582 and D-586. 1 Publication
Mutagenesisi575 – 5751S → A: Almost complete loss of CDK1 phosphorylation in vitro, loss of PLK1-binding, no effect on cortical localization; when associated with A-78; A-164; A-172; A-214; A-224; A-284; A-287 and A-377. 1 Publication
Mutagenesisi582 – 5821S → A: Drastic reduction in PLK1 phosphorylation in vitro, no effect on cortical localization; when associated with A-382; A-394; A-395; A-397; A-471 and A-586. 1 Publication
Mutagenesisi582 – 5821S → D: No effect on cortical localization; when associated with D-394; D-395; D-397; D-471 and D-586. 1 Publication
Mutagenesisi586 – 5861S → A: Drastic reduction in PLK1 phosphorylation in vitro, no effect on cortical localization; when associated with A-382; A-394; A-395; A-397; A-471 and A-582. 1 Publication
Mutagenesisi586 – 5861S → D: No effect on cortical localization; when associated with D-394; D-395; D-397; D-471 and D-582. 1 Publication

Organism-specific databases

PharmGKBiPA134861073.

Polymorphism and mutation databases

BioMutaiMISP.
DMDMi73620663.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 679679Mitotic interactor and substrate of PLK1PRO_0000079381Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei78 – 781Phosphoserine; by CDK1; in vitroCombined sources1 Publication
Modified residuei164 – 1641Phosphothreonine; by CDK1; in vitroCombined sources1 Publication
Modified residuei172 – 1721Phosphothreonine; by CDK1; in vitroCombined sources1 Publication
Modified residuei214 – 2141Phosphoserine; by CDK1; in vitroCombined sources1 Publication
Modified residuei219 – 2191PhosphothreonineCombined sources
Modified residuei224 – 2241Phosphothreonine; by CDK1; in vitroCombined sources1 Publication
Modified residuei284 – 2841Phosphoserine; by CDK1; in vitroCombined sources1 Publication
Modified residuei287 – 2871Phosphothreonine; by CDK1; in vitroCombined sources1 Publication
Modified residuei377 – 3771Phosphothreonine; by CDK1; in vitroCombined sources1 Publication
Modified residuei382 – 3821Phosphoserine; by CDK1; in vitro1 Publication
Modified residuei394 – 3941Phosphoserine; by PLK1; in vitroCombined sources1 Publication
Modified residuei395 – 3951Phosphoserine; by PLK1; in vitroCombined sources1 Publication
Modified residuei397 – 3971Phosphoserine; by PLK1; in vitroCombined sources1 Publication
Modified residuei400 – 4001PhosphoserineCombined sources
Modified residuei430 – 4301PhosphoserineCombined sources
Modified residuei471 – 4711Phosphoserine; by PLK1; in vitroCombined sources
Modified residuei541 – 5411PhosphoserineCombined sources
Modified residuei543 – 5431PhosphoserineCombined sources
Modified residuei575 – 5751Phosphoserine; by CDK1; in vitroCombined sources1 Publication
Modified residuei577 – 5771PhosphothreonineCombined sources
Modified residuei582 – 5821Phosphoserine; by PLK1; in vitroCombined sources1 Publication
Modified residuei586 – 5861Phosphoserine; by PLK1; in vitro1 Publication
Modified residuei675 – 6751PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated by CDK1 and PLK1. CDK1 is the priming kinase for PLK1 phosphorylation. Phosphorylation by PLK1 is required for proper spindle orientation at metaphase.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8IVT2.
MaxQBiQ8IVT2.
PaxDbiQ8IVT2.
PRIDEiQ8IVT2.

PTM databases

iPTMnetiQ8IVT2.
PhosphoSiteiQ8IVT2.

Expressioni

Developmental stagei

Regulated in a cell-cycle dependent manner. Weakly expressed in G1 and S phases. Expression increases in G2/M phases and persisting until the end of mitosis (at protein level).1 Publication

Gene expression databases

BgeeiQ8IVT2.
CleanExiHS_C19orf21.
GenevisibleiQ8IVT2. HS.

Organism-specific databases

HPAiHPA049511.
HPA062232.

Interactioni

Subunit structurei

Associates with F-actin. Interacts with DCTN1; this interaction regulates DCTN1 distribution at the cell cortex. Interacts with PTK2/FAK and MAPRE1.2 Publications

Protein-protein interaction databases

BioGridi125982. 56 interactions.
IntActiQ8IVT2. 43 interactions.
MINTiMINT-4992628.
STRINGi9606.ENSP00000215582.

Structurei

3D structure databases

ProteinModelPortaliQ8IVT2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili545 – 56925Sequence analysisAdd
BLAST

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IP6Q. Eukaryota.
ENOG41127B9. LUCA.
GeneTreeiENSGT00510000049581.
HOGENOMiHOG000111983.
HOVERGENiHBG081352.
InParanoidiQ8IVT2.
OMAiPQTHHAT.
OrthoDBiEOG7CCBSC.
PhylomeDBiQ8IVT2.
TreeFamiTF334067.

Family and domain databases

InterProiIPR029304. AKAP2_C.
[Graphical view]
PfamiPF15304. AKAP2_C. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8IVT2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDRVTRYPIL GIPQAHRGTG LVLDGDTSYT YHLVCMGPEA SGWGQDEPQT
60 70 80 90 100
WPTDHRAQQG VQRQGVSYSV HAYTGQPSPR GLHSENREDE GWQVYRLGAR
110 120 130 140 150
DAHQGRPTWA LRPEDGEDKE MKTYRLDAGD ADPRRLCDLE RERWAVIQGQ
160 170 180 190 200
AVRKSSTVAT LQGTPDHGDP RTPGPPRSTP LEENVVDREQ IDFLAARQQF
210 220 230 240 250
LSLEQANKGA PHSSPARGTP AGTTPGASQA PKAFNKPHLA NGHVVPIKPQ
260 270 280 290 300
VKGVVREENK VRAVPTWASV QVVDDPGSLA SVESPGTPKE TPIEREIRLA
310 320 330 340 350
QEREADLREQ RGLRQATDHQ ELVEIPTRPL LTKLSLITAP RRERGRPSLY
360 370 380 390 400
VQRDIVQETQ REEDHRREGL HVGRASTPDW VSEGPQPGLR RALSSDSILS
410 420 430 440 450
PAPDARAADP APEVRKVNRI PPDAYQPYLS PGTPQLEFSA FGAFGKPSSL
460 470 480 490 500
STAEAKAATS PKATMSPRHL SESSGKPLST KQEASKPPRG CPQANRGVVR
510 520 530 540 550
WEYFRLRPLR FRAPDEPQQA QVPHVWGWEV AGAPALRLQK SQSSDLLERE
560 570 580 590 600
RESVLRREQE VAEERRNALF PEVFSPTPDE NSDQNSRSSS QASGITGSYS
610 620 630 640 650
VSESPFFSPI HLHSNVAWTV EDPVDSAPPG QRKKEQWYAG INPSDGINSE
660 670
VLEAIRVTRH KNAMAERWES RIYASEEDD
Length:679
Mass (Da):75,357
Last modified:March 1, 2003 - v1
Checksum:iD2881CF5087E61F8
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti99 – 991A → T.
Corresponds to variant rs45477999 [ dbSNP | Ensembl ].
VAR_061629
Natural varianti156 – 1561S → G.
Corresponds to variant rs3746173 [ dbSNP | Ensembl ].
VAR_033754
Natural varianti232 – 2321K → R.
Corresponds to variant rs3746175 [ dbSNP | Ensembl ].
VAR_033755
Natural varianti269 – 2691S → N.
Corresponds to variant rs35384259 [ dbSNP | Ensembl ].
VAR_050910
Natural varianti653 – 6531E → G.
Corresponds to variant rs8107847 [ dbSNP | Ensembl ].
VAR_033756

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC042125 mRNA. Translation: AAH42125.1.
BC052236 mRNA. Translation: AAH52236.1.
CCDSiCCDS12042.1.
PIRiT00636.
RefSeqiNP_775752.1. NM_173481.3.
XP_011525987.1. XM_011527685.1.
XP_011525988.1. XM_011527686.1.
UniGeneiHs.439180.

Genome annotation databases

EnsembliENST00000215582; ENSP00000215582; ENSG00000099812.
GeneIDi126353.
KEGGihsa:126353.
UCSCiuc002lpo.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC042125 mRNA. Translation: AAH42125.1.
BC052236 mRNA. Translation: AAH52236.1.
CCDSiCCDS12042.1.
PIRiT00636.
RefSeqiNP_775752.1. NM_173481.3.
XP_011525987.1. XM_011527685.1.
XP_011525988.1. XM_011527686.1.
UniGeneiHs.439180.

3D structure databases

ProteinModelPortaliQ8IVT2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi125982. 56 interactions.
IntActiQ8IVT2. 43 interactions.
MINTiMINT-4992628.
STRINGi9606.ENSP00000215582.

PTM databases

iPTMnetiQ8IVT2.
PhosphoSiteiQ8IVT2.

Polymorphism and mutation databases

BioMutaiMISP.
DMDMi73620663.

Proteomic databases

EPDiQ8IVT2.
MaxQBiQ8IVT2.
PaxDbiQ8IVT2.
PRIDEiQ8IVT2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000215582; ENSP00000215582; ENSG00000099812.
GeneIDi126353.
KEGGihsa:126353.
UCSCiuc002lpo.4. human.

Organism-specific databases

CTDi126353.
GeneCardsiMISP.
H-InvDBHIX0027524.
HGNCiHGNC:27000. MISP.
HPAiHPA049511.
HPA062232.
MIMi615289. gene.
neXtProtiNX_Q8IVT2.
PharmGKBiPA134861073.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IP6Q. Eukaryota.
ENOG41127B9. LUCA.
GeneTreeiENSGT00510000049581.
HOGENOMiHOG000111983.
HOVERGENiHBG081352.
InParanoidiQ8IVT2.
OMAiPQTHHAT.
OrthoDBiEOG7CCBSC.
PhylomeDBiQ8IVT2.
TreeFamiTF334067.

Miscellaneous databases

ChiTaRSiMISP. human.
GenomeRNAii126353.
PROiQ8IVT2.
SOURCEiSearch...

Gene expression databases

BgeeiQ8IVT2.
CleanExiHS_C19orf21.
GenevisibleiQ8IVT2. HS.

Family and domain databases

InterProiIPR029304. AKAP2_C.
[Graphical view]
PfamiPF15304. AKAP2_C. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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].
    Tissue: Brain and Colon.
  2. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  3. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-164, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  4. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284; THR-287 AND SER-400, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-164; THR-172; THR-219; THR-224; SER-284; THR-287; SER-394; SER-395; SER-397; SER-400; SER-430; SER-541; SER-543; SER-575; THR-577; SER-582 AND SER-675, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. "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-78; THR-164; SER-214; THR-219; THR-287; THR-377; SER-394; SER-395; SER-400; SER-471; SER-541; SER-575; THR-577 AND SER-582, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "The novel actin/focal adhesion-associated protein MISP is involved in mitotic spindle positioning in human cells."
    Maier B., Kirsch M., Anderhub S., Zentgraf H., Kraemer A.
    Cell Cycle 12:1457-1471(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH DCTN1; MAPRE1 AND PTK2, SUBCELLULAR LOCATION, PHOSPHORYLATION BY CDK1.
  8. "MISP is a novel Plk1 substrate required for proper spindle orientation and mitotic progression."
    Zhu M., Settele F., Kotak S., Sanchez-Pulido L., Ehret L., Ponting C.P., Goenczy P., Hoffmann I.
    J. Cell Biol. 200:773-787(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ACTIN AND DCTN1, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, PHOSPHORYLATION AT SER-78; THR-164; THR-172; SER-214; THR-224; SER-284; THR-287; THR-377; SER-382; SER-394; SER-395; SER-397; SER-575; SER-582 AND SER-586, MUTAGENESIS OF SER-78; THR-164; THR-172; SER-214; THR-224; SER-284; THR-287; THR-377; SER-382; SER-394; SER-395; SER-397; SER-471; SER-575; SER-582 AND SER-586.

Entry informationi

Entry nameiMISP_HUMAN
AccessioniPrimary (citable) accession number: Q8IVT2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: March 1, 2003
Last modified: June 8, 2016
This is version 107 of the entry and version 1 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 19
    Human chromosome 19: 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

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.