Q01860 (PO5F1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
POU domain, class 5, transcription factor 1

Alternative name(s):
Octamer-binding protein 3
Short name=Oct-3
Octamer-binding protein 4
Short name=Oct-4
Octamer-binding transcription factor 3
Short name=OTF-3

Gene names

Name:	POU5F1
Synonyms:	OCT3, OCT4, OTF3

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	360 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Transcription factor that binds to the octamer motif (5'-ATTTGCAT-3'). Forms a trimeric complex with SOX2 on DNA and controls the expression of a number of genes involved in embryonic development such as YES1, FGF4, UTF1 and ZFP206. Critical for early embryogenesis and for embryonic stem cell pluripotency. Ref.11
Subunit structure	Interacts with UBE2I and ZSCAN10 By similarity. Interacts with PKM. Interacts with WWP2. Ref.12 Ref.13
Subcellular location	Cytoplasm. Nucleus. Note: Expressed in a diffuse and slightly punctuate pattern. Ref.12 Ref.13 Ref.14
Tissue specificity	Expressed in developing brain. Highest levels found in specific cell layers of the cortex, the olfactory bulb, the hippocampus and the cerebellum. Low levels of expression in adult tissues. Ref.1 Ref.8
Developmental stage	Highly expressed in undifferentiated embryonic stem cells and expression decreases gradually after embryoid body (EB) formation. Ref.13
Induction	Transcriptional activity is positively regulated by PKM. Ref.12
Domain	The POU-specific domain mediates interaction with PKM. Ref.12
Post-translational modification	Sumoylation enhances the protein stability, DNA binding and transactivation activity. Sumoylation is required for enhanced YES1 expression By similarity. Ubiquitinated; undergoes 'Lys-63'-linked polyubiquitination by WWP2 leading to proteasomal degradation By similarity. Ref.13 ERK1/2-mediated phosphorylation at Ser-111 promotes nuclear exclusion and proteasomal degradation. Phosphorylation at Thr-235 and Ser-236 decrease DNA-binding and alters ability to activate transcription.
Biotechnological use	POU5F1/OCT4, SOX2, MYC/c-Myc and KLF4 are the four Yamanaka factors. When combined, these factors are sufficient to reprogram differentiated cells to an embryonic-like state designated iPS (induced pluripotent stem) cells. iPS cells exhibit the morphology and growth properties of ES cells and express ES cell marker genes. Ref.11
Miscellaneous	Several pseudogenes of POU5F1 have been described on chromosomes 1, 3, 8, 10 and 12. 2 of them, localized in chromosomes 8 and 10, are transcribed in cancer tissues but not in normal ones and may be involved in the regulation of POU5F1 gene activity in carcinogenesis.
Sequence similarities	Belongs to the POU transcription factor family. Class-5 subfamily. Contains 1 homeobox DNA-binding domain. Contains 1 POU-specific domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Homeobox
Ligand	DNA-binding
Molecular function	Developmental protein
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	BMP signaling pathway involved in heart induction Inferred from mutant phenotype PubMed 19736317. Source: BHF-UCL blastocyst development Inferred from sequence or structural similarity. Source: BHF-UCL cardiac cell fate determination Inferred from direct assay PubMed 19736317. Source: BHF-UCL cell fate commitment involved in formation of primary germ layer Inferred from mutant phenotype PubMed 19736317. Source: BHF-UCL endodermal cell fate specification Inferred from direct assay PubMed 20713518. Source: MGI mRNA transcription from RNA polymerase II promoter Inferred from sequence or structural similarity. Source: BHF-UCL negative regulation of gene silencing by miRNA Inferred from mutant phenotype PubMed 19409607. Source: UniProtKB positive regulation of SMAD protein import into nucleus Inferred from direct assay PubMed 19736317. Source: BHF-UCL positive regulation of catenin import into nucleus Inferred from direct assay PubMed 19736317. Source: BHF-UCL positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay PubMed 19736317. Source: BHF-UCL regulation of asymmetric cell division Inferred from sequence or structural similarity. Source: BHF-UCL regulation of heart induction by regulation of canonical Wnt receptor signaling pathway Inferred from mutant phenotype PubMed 19736317. Source: BHF-UCL regulation of methylation-dependent chromatin silencing Inferred from direct assay PubMed 19736317. Source: BHF-UCL response to wounding Inferred from expression pattern PubMed 17982423. Source: UniProtKB somatic stem cell maintenance Inferred from direct assay PubMed 19409607. Source: UniProtKB
Cellular_component	cytosol Inferred from direct assay PubMed 18000303. Source: UniProtKB nucleoplasm Inferred from direct assay PubMed 20458727. Source: BHF-UCL transcription factor complex Inferred from direct assay PubMed 19736317. Source: BHF-UCL
Molecular_function	miRNA binding Inferred from direct assay PubMed 18710938PubMed 19409607. Source: UniProtKB sequence-specific DNA binding Inferred from direct assay PubMed 20713518. Source: MGI sequence-specific DNA binding RNA polymerase II transcription factor activity Inferred from sequence or structural similarity. Source: BHF-UCL transcription regulatory region DNA binding Inferred from direct assay PubMed 19736317. Source: BHF-UCL
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
FOXD3	Q9UJU5	2	EBI-475687,EBI-475674

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform A (identifier: Q01860-1)

Also known as: Oct-3A; Oct3A;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform B (identifier: Q01860-2)

Also known as: Oct-3B; Oct3B;

The sequence of this isoform differs from the canonical sequence as follows:
     1-135: MAGHLASDFA...KEKLEQNPEE → MHFYRLFLGA...LTSLLPFKIQ

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 360	360	POU domain, class 5, transcription factor 1		PRO_0000100747
Regions
	Domain	138 – 212	75	POU-specific
	DNA binding	230 – 289	60	Homeobox
Amino acid modifications
	Modified residue	111	1	Phosphoserine; by MAPK Ref.14 Ref.15
	Modified residue	235	1	Phosphothreonine Ref.15
	Modified residue	236	1	Phosphoserine Ref.15
	Modified residue	289	1	Phosphoserine Ref.15
	Modified residue	290	1	Phosphoserine Ref.15
	Modified residue	355	1	Phosphoserine Ref.15
	Cross-link	123		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Natural variations
	Alternative sequence	1 – 135	135	MAGHL…QNPEE → MHFYRLFLGATRRFLNPEWK GEIDNWCVYVLTSLLPFKIQ in isoform B.		VSP_002333
	Natural variant	226	1	L → F. Corresponds to variant rs1150767 [ dbSNP | Ensembl ].		VAR_046203
	Natural variant	322	1	T → A. Ref.1		VAR_003774
	Natural variant	351	1	T → I. Corresponds to variant rs1061120 [ dbSNP | Ensembl ].		VAR_046204
	Natural variant	357	1	M → L. Ref.1		VAR_003775
Experimental info
	Sequence conflict	189	1	A → G in CAA79974. Ref.8
	Sequence conflict	220	1	I → T in CAA79974. Ref.8
	Sequence conflict	227	1	V → L in CAA79974. Ref.8
	Sequence conflict	230	1	R → G in CAA79975. Ref.8
	Sequence conflict	240	1	R → Q in CAA79975. Ref.8
	Sequence conflict	251	1	Q → R in CAA79975. Ref.8
	Sequence conflict	272	1	D → DVVR in AAB35990. Ref.9

Sequences

	Sequence		Length	Mass (Da)
	Isoform A (Oct-3A) (Oct3A) [UniParc]. Last modified July 1, 1993. Version 1. Checksum: 934C58DAEA0C535B	FASTA	360	38,571
	10 20 30 40 50 60 MAGHLASDFA FSPPPGGGGD GPGGPEPGWV DPRTWLSFQG PPGGPGIGPG VGPGSEVWGI 70 80 90 100 110 120 PPCPPPYEFC GGMAYCGPQV GVGLVPQGGL ETSQPEGEAG VGVESNSDGA SPEPCTVTPG 130 140 150 160 170 180 AVKLEKEKLE QNPEESQDIK ALQKELEQFA KLLKQKRITL GYTQADVGLT LGVLFGKVFS 190 200 210 220 230 240 QTTICRFEAL QLSFKNMCKL RPLLQKWVEE ADNNENLQEI CKAETLVQAR KRKRTSIENR 250 260 270 280 290 300 VRGNLENLFL QCPKPTLQQI SHIAQQLGLE KDVVRVWFCN RRQKGKRSSS DYAQREDFEA 310 320 330 340 350 360 AGSPFSGGPV SFPLAPGPHF GTPGYGSPHF TALYSSVPFP EGEAFPPVSV TTLGSPMHSN
	Isoform B (Oct-3B) (Oct3B) [UniParc]. Checksum: 41C21E136EFBCBB2	FASTA	265	30,085
	10 20 30 40 50 60 MHFYRLFLGA TRRFLNPEWK GEIDNWCVYV LTSLLPFKIQ SQDIKALQKE LEQFAKLLKQ 70 80 90 100 110 120 KRITLGYTQA DVGLTLGVLF GKVFSQTTIC RFEALQLSFK NMCKLRPLLQ KWVEEADNNE 130 140 150 160 170 180 NLQEICKAET LVQARKRKRT SIENRVRGNL ENLFLQCPKP TLQQISHIAQ QLGLEKDVVR 190 200 210 220 230 240 VWFCNRRQKG KRSSSDYAQR EDFEAAGSPF SGGPVSFPLA PGPHFGTPGY GSPHFTALYS 250 260 SVPFPEGEAF PPVSVTTLGS PMHSN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human Oct3 gene family: cDNA sequences, alternative splicing, gene organization, chromosomal location, and expression at low levels in adult tissues." Takeda J., Seino S., Bell G.I. Nucleic Acids Res. 20:4613-4620(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), VARIANTS ALA-322 AND LEU-357, TISSUE SPECIFICITY. Tissue: Kidney.
[2]	"Comparison of MHC class I risk haplotypes in Thai and Caucasian psoriatics shows locus heterogeneity at PSORS1." Stuart P.E., Nair R.P., Hiremagalore R., Kullavanijaya P., Kullavanijaya P., Tejasvi T., Lim H.W., Voorhees J.J., Elder J.T. Tissue Antigens 76:387-397(2010) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Blood.
[3]	"Rapid evolution of major histocompatibility complex class I genes in primates generates new disease alleles in humans via hitchhiking diversity." Shiina T., Ota M., Shimizu S., Katsuyama Y., Hashimoto N., Takasu M., Anzai T., Kulski J.K., Kikkawa E., Naruse T., Kimura N., Yanagiya K., Watanabe A., Hosomichi K., Kohara S., Iwamoto C., Umehara Y., Meyer A. , Wanner V., Sano K., Macquin C., Ikeo K., Tokunaga K., Gojobori T., Inoko H., Bahram S. Genetics 173:1555-1570(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Peripheral blood leukocyte.
[4]	"Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region." Shiina S., Tamiya G., Oka A., Inoko H. Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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.
[8]	"A human POU domain gene, mPOU, is expressed in developing brain and specific adult tissues." Wey E., Lyons G.E., Schaefer B.W. Eur. J. Biochem. 220:753-762(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 188-274, TISSUE SPECIFICITY. Tissue: Heart and Skeletal muscle.
[9]	"Expression of transcription regulating genes in human preimplantation embryos." Abdel-Rahman B., Fiddler M., Rappolee D., Pergament E. Hum. Reprod. 10:2787-2792(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 212-283.
[10]	"Oct4 pseudogenes are transcribed in cancers." Suo G., Han J., Wang X., Zhang J., Zhao Y., Zhao Y., Dai J. Biochem. Biophys. Res. Commun. 337:1047-1051(2005) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION.
[11]	"Induction of pluripotent stem cells from adult human fibroblasts by defined factors." Takahashi K., Tanabe K., Ohnuki M., Narita M., Ichisaka T., Tomoda K., Yamanaka S. Cell 131:861-872(2007) [PubMed] [Europe PMC] [Abstract] Cited for: BIOTECHNOLOGY, FUNCTION.
[12]	"Pyruvate kinase isozyme type M2 (PKM2) interacts and cooperates with Oct-4 in regulating transcription." Lee J., Kim H.K., Han Y.-M., Kim J. Int. J. Biochem. Cell Biol. 40:1043-1054(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PKM, SUBCELLULAR LOCATION, DOMAIN, INDUCTION.
[13]	"WWP2 promotes degradation of transcription factor OCT4 in human embryonic stem cells." Xu H., Wang W., Li C., Yu H., Yang A., Wang B., Jin Y. Cell Res. 19:561-573(2009) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, INTERACTION WITH WWP2.
[14]	"Serine 111 phosphorylation regulates OCT4A protein subcellular distribution and degradation." Spelat R., Ferro F., Curcio F. J. Biol. Chem. 287:38279-38288(2012) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-111, SUBCELLULAR LOCATION.
[15]	"Phosphorylation regulates human OCT4." Brumbaugh J., Hou Z., Russell J.D., Howden S.E., Yu P., Ledvina A.R., Coon J.J., Thomson J.A. Proc. Natl. Acad. Sci. U.S.A. 109:7162-7168(2012) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-111; THR-235; SER-236; SER-289; SER-290 AND SER-355.
+	Additional computationally mapped references.

Web resources

Wikipedia

Oct-4 entry

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z11898 mRNA. Translation: CAA77951.1. Z11899 mRNA. Translation: CAA77952.1. GQ472773 Genomic DNA. Translation: ACZ95700.1. AB088113 Genomic DNA. Translation: BAC54946.1. AB202105 Genomic DNA. Translation: BAE78630.1. AB103619 Genomic DNA. Translation: BAF31281.1. BA000025 Genomic DNA. Translation: BAB63311.1. AL662833 Genomic DNA. Translation: CAI17407.1. AL662833 Genomic DNA. Translation: CAI17408.1. AL662844 Genomic DNA. Translation: CAI18331.1. AL773544 Genomic DNA. Translation: CAI18485.1. AL773544 Genomic DNA. Translation: CAI18486.1. BX088580 Genomic DNA. Translation: CAI18708.1. BX088580 Genomic DNA. Translation: CAI18709.1. CR759815 Genomic DNA. Translation: CAQ07092.1. CR759815 Genomic DNA. Translation: CAQ07093.1. CR388229 Genomic DNA. Translation: CAQ09226.1. CR388229 Genomic DNA. Translation: CAQ09227.1. CR847794 Genomic DNA. Translation: CAQ10780.1. CR847794 Genomic DNA. Translation: CAQ10781.1. CH471081 Genomic DNA. Translation: EAX03367.1. CH471081 Genomic DNA. Translation: EAX03368.1. BC117435 mRNA. Translation: AAI17436.1. BC117437 mRNA. Translation: AAI17438.1. Z21963 mRNA. Translation: CAA79974.1. Z21964 mRNA. Translation: CAA79975.1. S81255 mRNA. Translation: AAB35990.1.
IPI	IPI00219089. IPI00294177.
PIR	S25561. S32652.
RefSeq	NP_002692.2. NM_002701.4.
UniGene	Hs.249184. Hs.632482. Hs.646545.
3D structure databases
ProteinModelPortal	Q01860.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-33440N.
IntAct	Q01860. 2 interactions.
MINT	MINT-87567.
PTM databases
PhosphoSite	Q01860.
Polymorphism databases
DMDM	400659.
Proteomic databases
PaxDb	Q01860.
PRIDE	Q01860.
Protocols and materials databases
DNASU	5460.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000259915; ENSP00000259915; ENSG00000204531. ENST00000376243; ENSP00000365419; ENSG00000206454. ENST00000383524; ENSP00000373016; ENSG00000206454. ENST00000412166; ENSP00000387646; ENSG00000229094. ENST00000419095; ENSP00000413622; ENSG00000235068. ENST00000429314; ENSP00000387619; ENSG00000237582. ENST00000429603; ENSP00000392877; ENSG00000233911. ENST00000433063; ENSP00000405041; ENSG00000235068. ENST00000433348; ENSP00000412665; ENSG00000230336. ENST00000434616; ENSP00000388842; ENSG00000229094. ENST00000437747; ENSP00000391681; ENSG00000237582. ENST00000451077; ENSP00000391507; ENSG00000233911. ENST00000454714; ENSP00000400047; ENSG00000230336.
GeneID	5460.
KEGG	hsa:5460.
UCSC	uc003nsu.3. human.
Organism-specific databases
CTD	5460.
GeneCards	GC06M031136.
H-InvDB	HIX0159939. HIX0164984. HIX0166817. HIX0167068. HIX0167306. HIX0167552. HIX0168865. HIX0201948.
HGNC	HGNC:9221. POU5F1.
HPA	CAB025600. CAB026380.
MIM	164177. gene.
neXtProt	NX_Q01860.
PharmGKB	PA33545.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG329627.
HOVERGEN	HBG057998.
InParanoid	Q01860.
KO	K09367.
OMA	LENMFLQ.
OrthoDB	EOG46MBK1.
Enzyme and pathway databases
SignaLink	Q01860.
Gene expression databases
ArrayExpress	Q01860.
Bgee	Q01860.
Genevestigator	Q01860.
GermOnline	ENSG00000204531. Homo sapiens.
Family and domain databases
Gene3D	1.10.10.60. 1 hit. 1.10.260.40. 1 hit.
InterPro	IPR017970. Homeobox_CS. IPR001356. Homeodomain. IPR009057. Homeodomain-like. IPR010982. Lambda_DNA-bd_dom. IPR013847. POU. IPR015585. POU_dom_5. IPR000327. POU_specific. [Graphical view]
PANTHER	PTHR11636:SF15. PTHR11636:SF15. 1 hit.
Pfam	PF00046. Homeobox. 1 hit. PF00157. Pou. 1 hit. [Graphical view]
PRINTS	PR00028. POUDOMAIN.
SMART	SM00389. HOX. 1 hit. SM00352. POU. 1 hit. [Graphical view]
SUPFAM	SSF46689. Homeodomain_like. 1 hit. SSF47413. Lambda_like_DNA. 1 hit.
PROSITE	PS00027. HOMEOBOX_1. 1 hit. PS50071. HOMEOBOX_2. 1 hit. PS00035. POU_1. 1 hit. PS00465. POU_2. 1 hit. PS51179. POU_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	5460.
NextBio	21135.
SOURCE	Search...

Entry information

Entry name

PO5F1_HUMAN

Accession

Primary (citable) accession number: Q01860
Secondary accession number(s): A6NCS1 , A6NLL8, D2IYK4, P31359, Q15167, Q15168, Q16422, Q5STF3, Q5STF4

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	July 1, 1993
Last modified:	May 29, 2013
This is version 148 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.