O94992 (HEXI1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein HEXIM1

Alternative name(s):
Cardiac lineage protein 1
Estrogen down-regulated gene 1 protein
Hexamethylene bis-acetamide-inducible protein 1
Menage a quatre protein 1

Gene names

Name:	HEXIM1
Synonyms:	CLP1, EDG1, HIS1, MAQ1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	359 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.11 Ref.15 Ref.16 Ref.17
Subunit structure	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. Ref.5 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.18 Ref.19 Ref.26
Subcellular location	Nucleus. Cytoplasm. Note: Binds alpha-importin and is mostly nuclear. Ref.4 Ref.5 Ref.7 Ref.10 Ref.20
Tissue specificity	Ubiquitously expressed with higher expression in placenta. HEXIM1 and HEXIM2 are differentially expressed. Expressed in endocrine tissues. Ref.4 Ref.11
Induction	Up-regulated by HMBA (hexamethylene bisacetamide) (at protein level). Down-regulated by estrogen. Ref.4 Ref.5 Ref.11
Domain	The coiled-coil domain mediates oligomerization.
Miscellaneous	Inhibits Tat activity which is required for HIV-1 transcription.
Sequence similarities	Belongs to the HEXIM family.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Domain	Coiled coil
Molecular function	Repressor
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	heart development Inferred from electronic annotation. Source: Compara negative regulation of cyclin-dependent protein serine/threonine kinase activity Inferred from direct assay Ref.6. Source: HGNC negative regulation of transcription from RNA polymerase II promoter Inferred from direct assay Ref.6. Source: HGNC transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from direct assay Ref.5. Source: HGNC nucleus Inferred from direct assay Ref.5. Source: HGNC
Molecular_function	cyclin-dependent protein serine/threonine kinase inhibitor activity Inferred from direct assay Ref.6. Source: HGNC snRNA binding Inferred from direct assay Ref.6. Source: HGNC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 359

359

Protein HEXIM1

PRO_0000305263

Regions

Region

150 – 177

28

Basic region; mediates nuclear localization and interaction with 7SK snRNA and NR3C1

Region

202 – 205

4

Interaction with P-TEFb

Region

210 – 250

41

Autoinhibitory acidic region; in absence of 7SK snRNA interacts with the basic region preventing interaction with P-TEFb and modulating subcellular localization

Region

286 – 314

29

Mediates interaction with CCNT1

Region

310 – 355

46

Required for inhibition of ESR1-dependent transcription

Coiled coil

283 – 349

67

Potential

Amino acid modifications

Modified residue

97

1

Phosphoserine Ref.21

Modified residue

98

1

Phosphoserine Ref.21

Modified residue

233

1

Phosphoserine Ref.21 Ref.22 Ref.23

Modified residue

236

1

Phosphothreonine Ref.21 Ref.22 Ref.23

Modified residue

237

1

Phosphoserine Ref.21 Ref.22 Ref.23

Modified residue

252

1

Phosphoserine Ref.21 Ref.22 Ref.23 Ref.25

Experimental info

Mutagenesis

152 – 155

4

KHRR → ILAA: Abolishes interaction with 7SK snRNA. Ref.8

Mutagenesis

154 – 156

3

RRR → AAA: Abolishes interaction with 7SK snRNA. Ref.10

Mutagenesis

203

1

Y → D: Abolishes interaction with P-TEFb; when associated with D-205. Ref.8

Mutagenesis

205

1

T → D: Abolishes interaction with P-TEFb. Same effect; when associated with D-203. Ref.8

Mutagenesis

208

1

F → A, D or K: Partial loss of function. Ref.13

Mutagenesis

271

1

Y → A or E: Loss of function. Ref.13

Mutagenesis

287

1

L → A: Loss of oligomerization; when associated with A-294; A-332 and A-339. Loss of function and interaction with P-TEFb; when associated with A-294. Ref.14

Mutagenesis

294

1

L → A: Loss of oligomerization; when associated with A-287; A-332 and A-339. Loss of function and interaction with P-TEFb; when associated with A-287. Ref.14

Mutagenesis

332

1

L → A: Loss of oligomerization; when associated with A-287; A-294 and A-339. Ref.14

Mutagenesis

339

1

L → A: Loss of oligomerization; when associated with A-287; A-294 and A-332. Ref.14

Secondary structure

1

.

.

.

.

.

.

.

359

Helix Strand Turn

Details...

Helix

268 – 280

13

Helix

284 – 315

32

Helix

319 – 348

30

Sequences

	Sequence		Length	Mass (Da)
	O94992 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: B12845C4E2595FF0	FASTA	359	40,623
	10 20 30 40 50 60 MAEPFLSEYQ HQPQTSNCTG AAAVQEELNP ERPPGAEERV PEEDSRWQSR AFPQLGGRPG 70 80 90 100 110 120 PEGEGSLESQ PPPLQTQACP ESSCLREGEK GQNGDDSSAG GDFPPPAEVE PTPEAELLAQ 130 140 150 160 170 180 PCHDSEASKL GAPAAGGEEE WGQQQRQLGK KKHRRRPSKK KRHWKPYYKL TWEEKKKFDE 190 200 210 220 230 240 KQSLRASRIR AEMFAKGQPV APYNTTQFLM DDHDQEEPDL KTGLYSKRAA AKSDDTSDDD 250 260 270 280 290 300 FMEEGGEEDG GSDGMGGDGS EFLQRDFSET YERYHTESLQ NMSKQELIKE YLELEKCLSR 310 320 330 340 350 MEDENNRLRL ESKRLGGDDA RVRELELELD RLRAENLQLL TENELHRQQE RAPLSKFGD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of hexamethylene-bis-acetamide-inducible transcript, HEXIM1, in human vascular smooth muscle cells." Kusuhara M., Nagasaki K., Kimura K., Maass N., Manabe T., Ishikawa S., Aikawa M., Miyazaki K., Yamaguchi K. Biomed. Res. 20:273-279(1999) Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Vascular smooth muscle.
[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: Pericardium.
[3]	"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.
[4]	"Identification of a novel inhibitor of breast cell growth that is down-regulated by estrogens and decreased in breast tumors." Wittmann B.M., Wang N., Montano M.M. Cancer Res. 63:5151-5158(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION BY ESTROGEN.
[5]	"Suppression of NF-kappaB-dependent gene expression by a hexamethylene bisacetamide-inducible protein HEXIM1 in human vascular smooth muscle cells." Ouchida R., Kusuhara M., Shimizu N., Hisada T., Makino Y., Morimoto C., Handa H., Ohsuzu F., Tanaka H. Genes Cells 8:95-107(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH RELA, SUBCELLULAR LOCATION, INDUCTION BY HMBA.
[6]	"Inhibition of P-TEFb (CDK9/Cyclin T) kinase and RNA polymerase II transcription by the coordinated actions of HEXIM1 and 7SK snRNA." Yik J.H.N., Chen R., Nishimura R., Jennings J.L., Link A.J., Zhou Q. Mol. Cell 12:971-982(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[7]	"MAQ1 and 7SK RNA interact with CDK9/cyclin T complexes in a transcription-dependent manner." Michels A.A., Nguyen V.T., Fraldi A., Labas V., Edwards M., Bonnet F., Lania L., Bensaude O. Mol. Cell. Biol. 23:4859-4869(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE 7SK SNRNP COMPLEX, INTERACTION WITH CCNT1, SUBCELLULAR LOCATION.
[8]	"Binding of the 7SK snRNA turns the HEXIM1 protein into a P-TEFb (CDK9/cyclin T) inhibitor." Michels A.A., Fraldi A., Li Q., Adamson T.E., Bonnet F., Nguyen V.T., Sedore S.C., Price J.P., Price D.H., Lania L., Bensaude O. EMBO J. 23:2608-2619(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF 152-LYS--ARG-155; TYR-203 AND THR-205, INTERACTION WITH P-TEFB.
[9]	"A human immunodeficiency virus type 1 Tat-like arginine-rich RNA-binding domain is essential for HEXIM1 to inhibit RNA polymerase II transcription through 7SK snRNA-mediated inactivation of P-TEFb." Yik J.H.N., Chen R., Pezda A.C., Samford C.S., Zhou Q. Mol. Cell. Biol. 24:5094-5105(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH P-TEFB.
[10]	"Interplay between 7SK snRNA and oppositely charged regions in HEXIM1 direct the inhibition of P-TEFb." Barboric M., Kohoutek J., Price J.P., Blazek D., Price D.H., Peterlin B.M. EMBO J. 24:4291-4303(2005) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH THE 7SK SNRNA AND P-TEFB, MUTAGENESIS OF 154-ARG--ARG-156.
[11]	"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, INTERACTION WITH HEXIM2, OLIGOMERIZATION, TISSUE SPECIFICITY, INDUCTION.
[12]	"Identification of a cyclin T-binding domain in Hexim1 and biochemical analysis of its binding competition with HIV-1 Tat." Schulte A., Czudnochowski N., Barboric M., Schoenichen A., Blazek D., Peterlin B.M., Geyer M. J. Biol. Chem. 280:24968-24977(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CCNT1.
[13]	"Analysis of the large inactive P-TEFb complex indicates that it contains one 7SK molecule, a dimer of HEXIM1 or HEXIM2, and two P-TEFb molecules containing Cdk9 phosphorylated at threonine 186." Li Q., Price J.P., Byers S.A., Cheng D., Peng J., Price D.H. J. Biol. Chem. 280:28819-28826(2005) [PubMed] [Europe PMC] [Abstract] Cited for: OLIGOMERIZATION, MUTAGENESIS OF PHE-208 AND TYR-271.
[14]	"Oligomerization of HEXIM1 via 7SK snRNA and coiled-coil region directs the inhibition of P-TEFb." Blazek D., Barboric M., Kohoutek J., Oven I., Peterlin B.M. Nucleic Acids Res. 33:7000-7010(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH P-TEFB, OLIGOMERIZATION, MUTAGENESIS OF LEU-287; LEU-294; LEU-332 AND LEU-339.
[15]	"The breast cell growth inhibitor, estrogen down regulated gene 1, modulates a novel functional interaction between estrogen receptor alpha and transcriptional elongation factor cyclin T1." Wittmann B.M., Fujinaga K., Deng H., Ogba N., Montano M.M. Oncogene 24:5576-5588(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN ESR1-DEPENDENT TRANSCRIPTION, INTERACTION WITH ESR1.
[16]	"HEXIM1 forms a transcriptionally abortive complex with glucocorticoid receptor without involving 7SK RNA and positive transcription elongation factor b." Shimizu N., Ouchida R., Yoshikawa N., Hisada T., Watanabe H., Okamoto K., Kusuhara M., Handa H., Morimoto C., Tanaka H. Proc. Natl. Acad. Sci. U.S.A. 102:8555-8560(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN NR3C1-DEPENDENT TRANSCRIPTION, INTERACTION WITH NR3C1.
[17]	"Hexim1 sequesters positive transcription elongation factor b from the class II transactivator on MHC class II promoters." Kohoutek J., Blazek D., Peterlin B.M. Proc. Natl. Acad. Sci. U.S.A. 103:17349-17354(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN CIITA-DEPENDENT TRANSCRIPTION.
[18]	"Systematic analysis of the protein interaction network for the human transcription machinery reveals the identity of the 7SK capping enzyme." Jeronimo C., Forget D., Bouchard A., Li Q., Chua G., Poitras C., Therien C., Bergeron D., Bourassa S., Greenblatt J., Chabot B., Poirier G.G., Hughes T.R., Blanchette M., Price D.H., Coulombe B. Mol. Cell 27:262-274(2007) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE 7SK SNRNP COMPLEX.
[19]	"Regulation of P-TEFb elongation complex activity by CDK9 acetylation." Fu J., Yoon H.-G., Qin J., Wong J. Mol. Cell. Biol. 27:4641-4651(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NCOR1.
[20]	"HEXIM1 is a promiscuous double-stranded RNA-binding protein and interacts with RNAs in addition to 7SK in cultured cells." Li Q., Cooper J.J., Altwerger G.H., Feldkamp M.D., Shea M.A., Price D.H. Nucleic Acids Res. 35:2503-2512(2007) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[21]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97; SER-98; SER-233; THR-236; SER-237 AND SER-252, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[22]	"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-233; THR-236; SER-237 AND SER-252, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[23]	"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-233; THR-236; SER-237 AND SER-252, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[24]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]	"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-252, MASS SPECTROMETRY.
[26]	"Structure of the Cyclin T binding domain of Hexim1 and molecular basis for its recognition of P-TEFb." Dames S.A., Schoenichen A., Schulte A., Barboric M., Peterlin B.M., Grzesiek S., Geyer M. Proc. Natl. Acad. Sci. U.S.A. 104:14312-14317(2007) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 255-359, SUBUNIT, INTERACTION WITH CCNT1.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB021179 mRNA. Translation: BAA36166.1.
AK313557 mRNA. Translation: BAG36332.1.
BC006460 mRNA. Translation: AAH06460.1.

IPI

IPI00007941.

RefSeq

NP_006451.1. NM_006460.2.

UniGene

Hs.586945.
Hs.634944.
Hs.741758.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2GD7	NMR	-	A/B	257-359	[»]
3S9G	X-ray	2.10	A/B	255-359	[»]

ProteinModelPortal

O94992.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-46463N.

IntAct

O94992. 3 interactions.

STRING

9606.ENSP00000328773.

PTM databases

PhosphoSite

O94992.

Proteomic databases

PaxDb

O94992.

PeptideAtlas

O94992.

PRIDE

O94992.

Protocols and materials databases

DNASU

10614.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000332499; ENSP00000328773; ENSG00000186834.

GeneID

10614.

KEGG

hsa:10614.

UCSC

uc002iig.3. human.

Organism-specific databases

CTD

10614.

GeneCards

GC17P043224.

HGNC

HGNC:24953. HEXIM1.

HPA

CAB011625.
HPA008926.

MIM

607328. gene.

neXtProt

NX_O94992.

PharmGKB

PA142671694.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG72325.

HOGENOM

HOG000060338.

HOVERGEN

HBG053249.

InParanoid

O94992.

KO

K15189.

OMA

EDSRWQS.

OrthoDB

EOG40GCRK.

PhylomeDB

O94992.

Gene expression databases

Bgee

O94992.

CleanEx

HS_CLP1.
HS_HEXIM1.

Genevestigator

O94992.

Family and domain databases

InterPro

IPR024872. HEXIM.
[Graphical view]

PANTHER

PTHR13469. PTHR13469. 1 hit.

PRINTS

PR02094. HEXIMFAMILY.

ProtoNet

Search...

Other

ChiTaRS

HEXIM1. human.

EvolutionaryTrace

O94992.

GenomeRNAi

10614.

NextBio

40326.

SOURCE

Search...

Entry information

Entry name

HEXI1_HUMAN

Accession

Primary (citable) accession number: O94992
Secondary accession number(s): B2R8Y5

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 2, 2007
Last sequence update:	May 1, 1999
Last modified:	May 1, 2013
This is version 91 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.