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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 PLK11 Publication
Alternative name(s):
Mitotic spindle positioning proteinImported
Gene namesi
Name:MISPImported
Synonyms:C19orf21Imported
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)DescriptionActionsGraphical viewLength
Mutagenesisi78S → 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 Publication1
Mutagenesisi164T → 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 Publication1
Mutagenesisi172T → 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 Publication1
Mutagenesisi214S → 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 Publication1
Mutagenesisi224T → 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 Publication1
Mutagenesisi284S → 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 Publication1
Mutagenesisi287T → 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 Publication1
Mutagenesisi377T → 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 Publication1
Mutagenesisi382S → 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 Publication1
Mutagenesisi394S → 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 Publication1
Mutagenesisi394S → D: No effect on cortical localization; when associated with D-395; D-397; D-471; D-582 and D-586. 1 Publication1
Mutagenesisi395S → 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 Publication1
Mutagenesisi395S → D: No effect on cortical localization; when associated with D-394; D-397; D-471; D-582 and D-586. 1 Publication1
Mutagenesisi397S → 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 Publication1
Mutagenesisi397S → D: No effect on cortical localization; when associated with D-394; D-395; D-471; D-582 and D-586. 1 Publication1
Mutagenesisi471S → 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 Publication1
Mutagenesisi471S → D: No effect on cortical localization; when associated with D-394; D-395; D-397; D-582 and D-586. 1 Publication1
Mutagenesisi575S → 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 Publication1
Mutagenesisi582S → 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 Publication1
Mutagenesisi582S → D: No effect on cortical localization; when associated with D-394; D-395; D-397; D-471 and D-586. 1 Publication1
Mutagenesisi586S → 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 Publication1
Mutagenesisi586S → D: No effect on cortical localization; when associated with D-394; D-395; D-397; D-471 and D-582. 1 Publication1

Organism-specific databases

OpenTargetsiENSG00000099812.
PharmGKBiPA134861073.

Polymorphism and mutation databases

BioMutaiMISP.
DMDMi73620663.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000793811 – 679Mitotic interactor and substrate of PLK1Add BLAST679

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei78Phosphoserine; by CDK1; in vitroCombined sources1 Publication1
Modified residuei156PhosphoserineCombined sources1
Modified residuei164Phosphothreonine; by CDK1; in vitroCombined sources1 Publication1
Modified residuei172Phosphothreonine; by CDK1; in vitroCombined sources1 Publication1
Modified residuei179PhosphothreonineCombined sources1
Modified residuei214Phosphoserine; by CDK1; in vitroCombined sources1 Publication1
Modified residuei219PhosphothreonineCombined sources1
Modified residuei224Phosphothreonine; by CDK1; in vitroCombined sources1 Publication1
Modified residuei284Phosphoserine; by CDK1; in vitroCombined sources1 Publication1
Modified residuei287Phosphothreonine; by CDK1; in vitroCombined sources1 Publication1
Modified residuei348PhosphoserineCombined sources1
Modified residuei377Phosphothreonine; by CDK1; in vitroCombined sources1 Publication1
Modified residuei382Phosphoserine; by CDK1; in vitro1 Publication1
Modified residuei394Phosphoserine; by PLK1; in vitroCombined sources1 Publication1
Modified residuei395Phosphoserine; by PLK1; in vitroCombined sources1 Publication1
Modified residuei397Phosphoserine; by PLK1; in vitroCombined sources1 Publication1
Modified residuei400PhosphoserineCombined sources1
Modified residuei430PhosphoserineCombined sources1
Modified residuei471Phosphoserine; by PLK1; in vitroCombined sources1
Modified residuei541PhosphoserineCombined sources1
Modified residuei543PhosphoserineCombined sources1
Modified residuei575Phosphoserine; by CDK1; in vitroCombined sources1 Publication1
Modified residuei577PhosphothreonineCombined sources1
Modified residuei582Phosphoserine; by PLK1; in vitroCombined sources1 Publication1
Modified residuei586Phosphoserine; by PLK1; in vitro1 Publication1
Modified residuei675PhosphoserineCombined sources1

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.
PeptideAtlasiQ8IVT2.
PRIDEiQ8IVT2.

PTM databases

iPTMnetiQ8IVT2.
PhosphoSitePlusiQ8IVT2.

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

BgeeiENSG00000099812.
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 interactors.
IntActiQ8IVT2. 58 interactors.
MINTiMINT-4992628.
STRINGi9606.ENSP00000215582.

Structurei

3D structure databases

ProteinModelPortaliQ8IVT2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili545 – 569Sequence analysisAdd BLAST25

Sequence similaritiesi

Belongs to the MISP family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IP6Q. Eukaryota.
ENOG41127B9. LUCA.
GeneTreeiENSGT00510000049581.
HOGENOMiHOG000111983.
HOVERGENiHBG081352.
InParanoidiQ8IVT2.
OMAiPQTHHAT.
OrthoDBiEOG091G012B.
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)DescriptionActionsGraphical viewLength
Natural variantiVAR_06162999A → T.Corresponds to variant rs45477999dbSNPEnsembl.1
Natural variantiVAR_033754156S → G.Corresponds to variant rs3746173dbSNPEnsembl.1
Natural variantiVAR_033755232K → R.Corresponds to variant rs3746175dbSNPEnsembl.1
Natural variantiVAR_050910269S → N.Corresponds to variant rs35384259dbSNPEnsembl.1
Natural variantiVAR_033756653E → G.Corresponds to variant rs8107847dbSNPEnsembl.1

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_011527685.2.
XP_011525988.1. XM_011527686.2.
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_011527685.2.
XP_011525988.1. XM_011527686.2.
UniGeneiHs.439180.

3D structure databases

ProteinModelPortaliQ8IVT2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi125982. 56 interactors.
IntActiQ8IVT2. 58 interactors.
MINTiMINT-4992628.
STRINGi9606.ENSP00000215582.

PTM databases

iPTMnetiQ8IVT2.
PhosphoSitePlusiQ8IVT2.

Polymorphism and mutation databases

BioMutaiMISP.
DMDMi73620663.

Proteomic databases

EPDiQ8IVT2.
MaxQBiQ8IVT2.
PaxDbiQ8IVT2.
PeptideAtlasiQ8IVT2.
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.
OpenTargetsiENSG00000099812.
PharmGKBiPA134861073.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IP6Q. Eukaryota.
ENOG41127B9. LUCA.
GeneTreeiENSGT00510000049581.
HOGENOMiHOG000111983.
HOVERGENiHBG081352.
InParanoidiQ8IVT2.
OMAiPQTHHAT.
OrthoDBiEOG091G012B.
PhylomeDBiQ8IVT2.
TreeFamiTF334067.

Miscellaneous databases

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

Gene expression databases

BgeeiENSG00000099812.
CleanExiHS_C19orf21.
GenevisibleiQ8IVT2. HS.

Family and domain databases

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

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: November 30, 2016
This is version 112 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
  5. 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.