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O94992 (HEXI1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length359 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 359359Protein HEXIM1
PRO_0000305263

Regions

Region150 – 17728Basic region; mediates nuclear localization and interaction with 7SK snRNA and NR3C1
Region202 – 2054Interaction with P-TEFb
Region210 – 25041Autoinhibitory acidic region; in absence of 7SK snRNA interacts with the basic region preventing interaction with P-TEFb and modulating subcellular localization
Region286 – 31429Mediates interaction with CCNT1
Region310 – 35546Required for inhibition of ESR1-dependent transcription
Coiled coil283 – 34967 Potential

Amino acid modifications

Modified residue971Phosphoserine Ref.21
Modified residue981Phosphoserine Ref.21
Modified residue2331Phosphoserine Ref.21 Ref.22 Ref.23
Modified residue2361Phosphothreonine Ref.21 Ref.22 Ref.23
Modified residue2371Phosphoserine Ref.21 Ref.22 Ref.23
Modified residue2521Phosphoserine Ref.21 Ref.22 Ref.23 Ref.25

Experimental info

Mutagenesis152 – 1554KHRR → ILAA: Abolishes interaction with 7SK snRNA. Ref.8
Mutagenesis154 – 1563RRR → AAA: Abolishes interaction with 7SK snRNA. Ref.10
Mutagenesis2031Y → D: Abolishes interaction with P-TEFb; when associated with D-205. Ref.8
Mutagenesis2051T → D: Abolishes interaction with P-TEFb. Same effect; when associated with D-203. Ref.8
Mutagenesis2081F → A, D or K: Partial loss of function. Ref.13
Mutagenesis2711Y → A or E: Loss of function. Ref.13
Mutagenesis2871L → 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
Mutagenesis2941L → 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
Mutagenesis3321L → A: Loss of oligomerization; when associated with A-287; A-294 and A-339. Ref.14
Mutagenesis3391L → A: Loss of oligomerization; when associated with A-287; A-294 and A-332. Ref.14

Secondary structure

....... 359
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O94992 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: B12845C4E2595FF0

FASTA35940,623
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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.
CCDSCCDS11495.1.
RefSeqNP_006451.1. NM_006460.2.
UniGeneHs.586945.
Hs.741758.
Hs.745252.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2GD7NMR-A/B255-359[»]
3S9GX-ray2.10A/B255-359[»]
ProteinModelPortalO94992.
SMRO94992. Positions 254-359.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115860. 29 interactions.
DIPDIP-46463N.
IntActO94992. 5 interactions.
STRING9606.ENSP00000328773.

PTM databases

PhosphoSiteO94992.

Proteomic databases

MaxQBO94992.
PaxDbO94992.
PeptideAtlasO94992.
PRIDEO94992.

Protocols and materials databases

DNASU10614.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000332499; ENSP00000328773; ENSG00000186834.
GeneID10614.
KEGGhsa:10614.
UCSCuc002iig.3. human.

Organism-specific databases

CTD10614.
GeneCardsGC17P043224.
HGNCHGNC:24953. HEXIM1.
HPACAB011625.
HPA008926.
MIM607328. gene.
neXtProtNX_O94992.
PharmGKBPA142671694.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG72325.
HOGENOMHOG000060338.
HOVERGENHBG053249.
InParanoidO94992.
KOK15189.
OMAKGQNGDD.
OrthoDBEOG771281.
PhylomeDBO94992.
TreeFamTF336851.

Gene expression databases

BgeeO94992.
CleanExHS_CLP1.
HS_HEXIM1.
GenevestigatorO94992.

Family and domain databases

InterProIPR024872. HEXIM.
[Graphical view]
PANTHERPTHR13469. PTHR13469. 1 hit.
PfamPF15313. HEXIM. 1 hit.
[Graphical view]
PRINTSPR02094. HEXIMFAMILY.
ProtoNetSearch...

Other

ChiTaRSHEXIM1. human.
EvolutionaryTraceO94992.
GeneWikiHEXIM1.
GenomeRNAi10614.
NextBio40326.
PROO94992.
SOURCESearch...

Entry information

Entry nameHEXI1_HUMAN
AccessionPrimary (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: July 9, 2014
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM