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

Protein HEXIM1

Gene

Hexim1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Transcriptional regulator which functions as a general RNA polymerase II transcription inhibitor. In cooperation with 7SK snRNA sequesters P-TEFb in a large inactive 7SK snRNP complex preventing RNA polymerase II phosphorylation and subsequent transcriptional elongation. May also regulate NF-kappa-B, ESR1, NR3C1 and CIITA-dependent transcriptional activity (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Protein HEXIM1
Alternative name(s):
Cardiac lineage protein 1
Gene namesi
Name:Hexim1
Synonyms:Clp1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 10

Organism-specific databases

RGDi1559851. Hexim1.

Subcellular locationi

  • Nucleus By similarity
  • Cytoplasm By similarity

  • Note: Binds alpha-importin and is mostly nuclear.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 356356Protein HEXIM1PRO_0000305265Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei98 – 981PhosphoserineBy similarity
Modified residuei103 – 1031PhosphoserineCombined sources
Modified residuei230 – 2301PhosphoserineBy similarity
Modified residuei233 – 2331PhosphothreonineBy similarity
Modified residuei234 – 2341PhosphoserineBy similarity
Modified residuei249 – 2491PhosphoserineCombined sources
Modified residuei257 – 2571PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ5M9G1.
PRIDEiQ5M9G1.

PTM databases

iPTMnetiQ5M9G1.

Expressioni

Inductioni

Up-regulated by HMBA (hexamethylene bisacetamide).1 Publication

Gene expression databases

GenevisibleiQ5M9G1. RN.

Interactioni

Subunit structurei

Homooligomer and heterooligomer with HEXIM2; probably dimeric. Component of the 7SK snRNP complex at least composed of P-TEFb (composed of CDK9 and CCNT1/cyclin-T1), HEXIM1, HEXIM2, BCDIN3, SART3 proteins and 7SK and U6 snRNAs. Interacts with the N-CoR complex through NCOR1. Interacts with ESR1 and NR3C1. May interact with NF-kappa-B through RELA. Interacts with CCNT2; mediates formation of a tripartite complex with KPNA2.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000004272.

Structurei

3D structure databases

ProteinModelPortaliQ5M9G1.
SMRiQ5M9G1. Positions 251-356.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni147 – 17428Basic region; mediates nuclear localization and interaction with 7SK snRNA and NR3C1By similarityAdd
BLAST
Regioni199 – 2024Interaction with P-TEFbBy similarity
Regioni207 – 24741Autoinhibitory acidic region; in absence of 7SK snRNA interacts with the basic region preventing interaction with P-TEFb and modulating subcellular localizationBy similarityAdd
BLAST
Regioni283 – 31129Mediates interaction with CCNT1By similarityAdd
BLAST
Regioni307 – 35246Required for inhibition of ESR1-dependent transcriptionBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili280 – 34667Sequence analysisAdd
BLAST

Domaini

The coiled-coil domain mediates oligomerization.By similarity

Sequence similaritiesi

Belongs to the HEXIM family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IH8I. Eukaryota.
ENOG4111K9Z. LUCA.
GeneTreeiENSGT00390000002808.
HOGENOMiHOG000060338.
HOVERGENiHBG053249.
InParanoidiQ5M9G1.
KOiK15189.
OMAiEAWGQQQ.
OrthoDBiEOG771281.
PhylomeDBiQ5M9G1.
TreeFamiTF336851.

Family and domain databases

InterProiIPR024872. HEXIM.
[Graphical view]
PANTHERiPTHR13469. PTHR13469. 2 hits.
PfamiPF15313. HEXIM. 1 hit.
[Graphical view]
PRINTSiPR02094. HEXIMFAMILY.

Sequencei

Sequence statusi: Complete.

Q5M9G1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEPLLSEHQ HQPQTSNCTG AAVVHEEQNS ERPPSAEERV PKEDSRWQSR
60 70 80 90 100
ASLQSGSRPG QEGDGGLKHQ LPPLQTNACP ELSCLEKGEK GQNGEDLSTG
110 120 130 140 150
GASPSAEGEP MSESLVQPGH DSEATKLEAP VAGVEEPWGQ QQRQLGKKKH
160 170 180 190 200
RRRPSKKKRH WKPYYKLTWE EKKKFDEKQS LRASRVRAEM FAKGQPVAPY
210 220 230 240 250
NTTQFLMDDH DQEEPDLKTG LYPKRAAAKS DDTSDEDFVE EAGEEDGGSD
260 270 280 290 300
GMGGDGSEFL QRDFSETYER YHAESLQNMS KQELIKEYLE LEKCLSRKED
310 320 330 340 350
ENNRLRLESK RLGGVDARVR ELELELDRLR AENRQLLTEN ELHRQQERAP

PSKFGD
Length:356
Mass (Da):40,317
Last modified:February 1, 2005 - v1
Checksum:i7854474F7E628E6C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC087133 mRNA. Translation: AAH87133.1.
RefSeqiNP_001020307.1. NM_001025136.1.
UniGeneiRn.113703.

Genome annotation databases

EnsembliENSRNOT00000004272; ENSRNOP00000004272; ENSRNOG00000003203.
GeneIDi498008.
KEGGirno:498008.
UCSCiRGD:1559851. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC087133 mRNA. Translation: AAH87133.1.
RefSeqiNP_001020307.1. NM_001025136.1.
UniGeneiRn.113703.

3D structure databases

ProteinModelPortaliQ5M9G1.
SMRiQ5M9G1. Positions 251-356.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000004272.

PTM databases

iPTMnetiQ5M9G1.

Proteomic databases

PaxDbiQ5M9G1.
PRIDEiQ5M9G1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000004272; ENSRNOP00000004272; ENSRNOG00000003203.
GeneIDi498008.
KEGGirno:498008.
UCSCiRGD:1559851. rat.

Organism-specific databases

CTDi10614.
RGDi1559851. Hexim1.

Phylogenomic databases

eggNOGiENOG410IH8I. Eukaryota.
ENOG4111K9Z. LUCA.
GeneTreeiENSGT00390000002808.
HOGENOMiHOG000060338.
HOVERGENiHBG053249.
InParanoidiQ5M9G1.
KOiK15189.
OMAiEAWGQQQ.
OrthoDBiEOG771281.
PhylomeDBiQ5M9G1.
TreeFamiTF336851.

Miscellaneous databases

NextBioi698394.
PROiQ5M9G1.

Gene expression databases

GenevisibleiQ5M9G1. RN.

Family and domain databases

InterProiIPR024872. HEXIM.
[Graphical view]
PANTHERiPTHR13469. PTHR13469. 2 hits.
PfamiPF15313. HEXIM. 1 hit.
[Graphical view]
PRINTSiPR02094. HEXIMFAMILY.
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: Lung.
  2. "Structure, expression, and functional characterization of the mouse CLP-1 gene."
    Huang F., Wagner M., Siddiqui M.A.Q.
    Gene 292:245-259(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INDUCTION.
  3. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103 AND SER-249, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiHEXI1_RAT
AccessioniPrimary (citable) accession number: Q5M9G1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: February 1, 2005
Last modified: May 11, 2016
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.