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Protein

Protein HEXIM2

Gene

HEXIM2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 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.2 Publications

GO - Molecular functioni

  • cyclin-dependent protein serine/threonine kinase inhibitor activity Source: HGNC
  • snRNA binding Source: HGNC

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Protein HEXIM2
Alternative name(s):
Hexamethylene bis-acetamide-inducible protein 2
Gene namesi
Name:HEXIM2
ORF Names:L3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:28591. HEXIM2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi143 – 1431T → A: Loss of interaction with P-TEFb. 1 Publication
Mutagenesisi143 – 1431T → D: Loss of interaction with P-TEFb. 1 Publication

Organism-specific databases

PharmGKBiPA142671695.

Polymorphism and mutation databases

BioMutaiHEXIM2.
DMDMi74732374.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 286286Protein HEXIM2PRO_0000305267Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei29 – 291Phosphoserine2 Publications
Modified residuei32 – 321Phosphothreonine2 Publications
Modified residuei39 – 391Phosphoserine1 Publication
Modified residuei46 – 461Phosphothreonine2 Publications
Modified residuei51 – 511Phosphoserine4 Publications
Modified residuei53 – 531Phosphoserine4 Publications
Modified residuei71 – 711Phosphoserine1 Publication
Modified residuei76 – 761Phosphoserine2 Publications
Modified residuei81 – 811Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ96MH2.
PaxDbiQ96MH2.
PRIDEiQ96MH2.

PTM databases

PhosphoSiteiQ96MH2.

Expressioni

Tissue specificityi

Ubiquitously expressed with higher expression in testis. HEXIM1 and HEXIM2 are differentially expressed.1 Publication

Inductioni

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

Gene expression databases

BgeeiQ96MH2.
CleanExiHS_HEXIM2.
ExpressionAtlasiQ96MH2. baseline and differential.
GenevisibleiQ96MH2. HS.

Organism-specific databases

HPAiHPA023323.
HPA028455.

Interactioni

Subunit structurei

Homooligomer and heterooligomer with HEXIM1; 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.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CCDC36Q8IYA83EBI-5460660,EBI-8638439
GATA1P159763EBI-5460660,EBI-3909284
MEOX2A4D1273EBI-5460660,EBI-10172134
PIM1P113093EBI-5460660,EBI-696621
PIN1Q135263EBI-5460660,EBI-714158
PRDM14Q9GZV84EBI-5460660,EBI-3957793
RNPS1D3DU923EBI-5460660,EBI-10176640
SPRY1O436093EBI-5460660,EBI-3866665
SPRY2O435973EBI-5460660,EBI-742487
TADA3O755283EBI-5460660,EBI-473249
TCF12Q990814EBI-5460660,EBI-722877

Protein-protein interaction databases

BioGridi125888. 34 interactions.
IntActiQ96MH2. 12 interactions.
STRINGi9606.ENSP00000302276.

Structurei

3D structure databases

ProteinModelPortaliQ96MH2.
SMRiQ96MH2. Positions 187-276.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni140 – 1434Interaction with P-TEFb
Regioni226 – 28661Interaction with CCNT1, HEXIM1 and HEXIM2Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili207 – 27771Sequence AnalysisAdd
BLAST

Domaini

The coiled-coil domain mediates oligomerization.

Sequence similaritiesi

Belongs to the HEXIM family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG72325.
GeneTreeiENSGT00390000002808.
HOGENOMiHOG000060338.
HOVERGENiHBG107976.
InParanoidiQ96MH2.
KOiK15189.
OMAiPCRQVEE.
OrthoDBiEOG771281.
PhylomeDBiQ96MH2.
TreeFamiTF336851.

Family and domain databases

InterProiIPR024872. HEXIM.
IPR024876. HEXIM2.
[Graphical view]
PANTHERiPTHR13469. PTHR13469. 1 hit.
PTHR13469:SF3. PTHR13469:SF3. 1 hit.
PfamiPF15313. HEXIM. 1 hit.
[Graphical view]
PRINTSiPR02094. HEXIMFAMILY.

Sequencei

Sequence statusi: Complete.

Q96MH2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMATPNQTAC NAESPVALEE AKTSGAPGSP QTPPERHDSG GSLPLTPRME
60 70 80 90 100
SHSEDEDLAG AVGGLGWNSR SPRTQSPGGC SAEAVLARKK HRRRPSKRKR
110 120 130 140 150
HWRPYLELSW AEKQQRDERQ SQRASRVREE MFAKGQPVAP YNTTQFLMND
160 170 180 190 200
RDPEEPNLDV PHGISHPGSS GESEAGDSDG RGRAHGEFQR KDFSETYERF
210 220 230 240 250
HTESLQGRSK QELVRDYLEL EKRLSQAEEE TRRLQQLQAC TGQQSCRQVE
260 270 280
ELAAEVQRLR TENQRLRQEN QMWNREGCRC DEEPGT
Length:286
Mass (Da):32,419
Last modified:December 1, 2001 - v1
Checksum:i58576D72096A8A6F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY598322 mRNA. Translation: AAT06733.1.
AK056946 mRNA. Translation: BAB71319.1.
CH471178 Genomic DNA. Translation: EAW51541.1.
CH471178 Genomic DNA. Translation: EAW51542.1.
BC003531 mRNA. Translation: AAH03531.1.
BC012474 mRNA. Translation: AAH12474.1.
BC025970 mRNA. Translation: AAH25970.1.
CCDSiCCDS11496.1.
RefSeqiNP_001290365.1. NM_001303436.1.
NP_001290366.1. NM_001303437.1.
NP_001290367.1. NM_001303438.1.
NP_001290368.1. NM_001303439.1.
NP_001290369.1. NM_001303440.1.
NP_001290370.1. NM_001303441.1.
NP_001290371.1. NM_001303442.1.
NP_001290372.1. NM_001303443.1.
NP_001290373.1. NM_001303444.1.
NP_653209.1. NM_144608.2.
XP_011522604.1. XM_011524302.1.
XP_011522605.1. XM_011524303.1.
XP_011522606.1. XM_011524304.1.
XP_011522607.1. XM_011524305.1.
XP_011522608.1. XM_011524306.1.
XP_011522609.1. XM_011524307.1.
XP_011522610.1. XM_011524308.1.
UniGeneiHs.56382.
Hs.569733.
Hs.594840.

Genome annotation databases

EnsembliENST00000307275; ENSP00000302276; ENSG00000168517.
ENST00000591576; ENSP00000465727; ENSG00000168517.
ENST00000592695; ENSP00000467517; ENSG00000168517.
GeneIDi124790.
KEGGihsa:124790.
UCSCiuc002iih.1. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY598322 mRNA. Translation: AAT06733.1.
AK056946 mRNA. Translation: BAB71319.1.
CH471178 Genomic DNA. Translation: EAW51541.1.
CH471178 Genomic DNA. Translation: EAW51542.1.
BC003531 mRNA. Translation: AAH03531.1.
BC012474 mRNA. Translation: AAH12474.1.
BC025970 mRNA. Translation: AAH25970.1.
CCDSiCCDS11496.1.
RefSeqiNP_001290365.1. NM_001303436.1.
NP_001290366.1. NM_001303437.1.
NP_001290367.1. NM_001303438.1.
NP_001290368.1. NM_001303439.1.
NP_001290369.1. NM_001303440.1.
NP_001290370.1. NM_001303441.1.
NP_001290371.1. NM_001303442.1.
NP_001290372.1. NM_001303443.1.
NP_001290373.1. NM_001303444.1.
NP_653209.1. NM_144608.2.
XP_011522604.1. XM_011524302.1.
XP_011522605.1. XM_011524303.1.
XP_011522606.1. XM_011524304.1.
XP_011522607.1. XM_011524305.1.
XP_011522608.1. XM_011524306.1.
XP_011522609.1. XM_011524307.1.
XP_011522610.1. XM_011524308.1.
UniGeneiHs.56382.
Hs.569733.
Hs.594840.

3D structure databases

ProteinModelPortaliQ96MH2.
SMRiQ96MH2. Positions 187-276.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi125888. 34 interactions.
IntActiQ96MH2. 12 interactions.
STRINGi9606.ENSP00000302276.

PTM databases

PhosphoSiteiQ96MH2.

Polymorphism and mutation databases

BioMutaiHEXIM2.
DMDMi74732374.

Proteomic databases

MaxQBiQ96MH2.
PaxDbiQ96MH2.
PRIDEiQ96MH2.

Protocols and materials databases

DNASUi124790.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000307275; ENSP00000302276; ENSG00000168517.
ENST00000591576; ENSP00000465727; ENSG00000168517.
ENST00000592695; ENSP00000467517; ENSG00000168517.
GeneIDi124790.
KEGGihsa:124790.
UCSCiuc002iih.1. human.

Organism-specific databases

CTDi124790.
GeneCardsiGC17P043238.
HGNCiHGNC:28591. HEXIM2.
HPAiHPA023323.
HPA028455.
MIMi615695. gene.
neXtProtiNX_Q96MH2.
PharmGKBiPA142671695.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG72325.
GeneTreeiENSGT00390000002808.
HOGENOMiHOG000060338.
HOVERGENiHBG107976.
InParanoidiQ96MH2.
KOiK15189.
OMAiPCRQVEE.
OrthoDBiEOG771281.
PhylomeDBiQ96MH2.
TreeFamiTF336851.

Miscellaneous databases

ChiTaRSiHEXIM2. human.
GeneWikiiHEXIM2.
GenomeRNAii124790.
NextBioi81380.
PROiQ96MH2.
SOURCEiSearch...

Gene expression databases

BgeeiQ96MH2.
CleanExiHS_HEXIM2.
ExpressionAtlasiQ96MH2. baseline and differential.
GenevisibleiQ96MH2. HS.

Family and domain databases

InterProiIPR024872. HEXIM.
IPR024876. HEXIM2.
[Graphical view]
PANTHERiPTHR13469. PTHR13469. 1 hit.
PTHR13469:SF3. PTHR13469:SF3. 1 hit.
PfamiPF15313. HEXIM. 1 hit.
[Graphical view]
PRINTSiPR02094. HEXIMFAMILY.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Suppression subtractive hybridization and expression profiling identifies a unique set of genes overexpressed in non-small-cell lung cancer."
    Petroziello J., Yamane A., Westendorf L., Thompson M., McDonagh C., Cerveny C., Law C.-L., Wahl A., Carter P.
    Oncogene 23:7734-7745(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "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].
    Tissue: Skeletal muscle.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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: Eye, Prostate and Uterus.
  5. "HEXIM2, a HEXIM1-related protein, regulates positive transcription elongation factor b through association with 7SK."
    Byers S.A., Price J.P., Cooper J.J., Li Q., Price D.H.
    J. Biol. Chem. 280:16360-16367(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE 7SK SNRNP COMPLEX, MUTAGENESIS OF THR-143.
  6. "Compensatory contributions of HEXIM1 and HEXIM2 in maintaining the balance of active and inactive positive transcription elongation factor b complexes for control of transcription."
    Yik J.H.N., Chen R., Pezda A.C., Zhou Q.
    J. Biol. Chem. 280:16368-16376(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE 7SK SNRNP COMPLEX, INTERACTION WITH HEXIM1, OLIGOMERIZATION, TISSUE SPECIFICITY, INDUCTION.
  7. "Transcription-dependent association of multiple positive transcription elongation factor units to a HEXIM multimer."
    Dulac C., Michels A.A., Fraldi A., Bonnet F., Nguyen V.T., Napolitano G., Lania L., Bensaude O.
    J. Biol. Chem. 280:30619-30629(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: OLIGOMERIZATION, INTERACTION WITH CCNT1, SUBCELLULAR LOCATION.
  8. "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-46, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29; THR-32; THR-46; SER-51; SER-53; SER-71; SER-76 AND SER-81, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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-51 AND SER-53, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "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-51 AND SER-53, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29; THR-32; SER-39; SER-51; SER-53 AND SER-76, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiHEXI2_HUMAN
AccessioniPrimary (citable) accession number: Q96MH2
Secondary accession number(s): D3DX66
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: December 1, 2001
Last modified: July 22, 2015
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 17
    Human chromosome 17: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.