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P14859

- PO2F1_HUMAN

UniProt

P14859 - PO2F1_HUMAN

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Protein

POU domain, class 2, transcription factor 1

Gene
POU2F1, OCT1, OTF1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Transcription factor that binds to the octamer motif (5'-ATTTGCAT-3') and activates the promoters of the genes for some small nuclear RNAs (snRNA) and of genes such as those for histone H2B and immunoglobulins. Modulates transcription transactivation by NR3C1, AR and PGR By similarity. In case of human herpes simplex virus (HSV) infection, POU2F1 forms a multiprotein-DNA complex with the viral transactivator protein VP16 and HCFC1 thereby enabling the transcription of the viral immediate early genes.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi379 – 43860Homeobox1 PublicationAdd
BLAST

GO - Molecular functioni

  1. protein binding Source: UniProtKB
  2. sequence-specific DNA binding Source: UniProtKB
  3. sequence-specific DNA binding transcription factor activity Source: ProtInc

GO - Biological processi

  1. gene expression Source: Reactome
  2. negative regulation of transcription, DNA-templated Source: UniProtKB
  3. transcription from RNA polymerase III promoter Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_22339. RNA Polymerase III Abortive And Retractive Initiation.
REACT_571. RNA Polymerase III Transcription Initiation From Type 3 Promoter.
SignaLinkiP14859.

Names & Taxonomyi

Protein namesi
Recommended name:
POU domain, class 2, transcription factor 1
Alternative name(s):
NF-A1
Octamer-binding protein 1
Short name:
Oct-1
Octamer-binding transcription factor 1
Short name:
OTF-1
Gene namesi
Name:POU2F1
Synonyms:OCT1, OTF1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:9212. POU2F1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. nucleoplasm Source: Reactome
  3. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi385 – 3851S → A: Loss of inhibition of DNA binding. 1 Publication

Organism-specific databases

PharmGKBiPA33536.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 743743POU domain, class 2, transcription factor 1PRO_0000100707Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei270 – 2701Phosphothreonine1 Publication
Modified residuei283 – 2831Phosphoserine1 Publication
Modified residuei385 – 3851Phosphoserine1 Publication
Modified residuei448 – 4481Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated by PRKDC.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP14859.
PaxDbiP14859.
PRIDEiP14859.

PTM databases

PhosphoSiteiP14859.

Expressioni

Tissue specificityi

Ubiquitous. Isoform 2 is lymphocyte-specific.

Gene expression databases

ArrayExpressiP14859.
BgeeiP14859.
CleanExiHS_POU2F1.
GenevestigatoriP14859.

Organism-specific databases

HPAiCAB002608.
HPA045784.

Interactioni

Subunit structurei

Interacts with NR3C1, AR, PGR and HCFC1. Associates with the herpes simplex virus VP16-induced complex; binding to HCFC1 activates the viral transcriptional activator VP16 for association with POU2F1, to form a multiprotein-DNA complex responsible for activating transcription of the viral immediate early genes.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SP1P080477EBI-624770,EBI-298336

Protein-protein interaction databases

BioGridi111447. 51 interactions.
DIPiDIP-226N.
IntActiP14859. 3 interactions.
MINTiMINT-149153.
STRINGi9606.ENSP00000271411.

Structurei

Secondary structure

1
743
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi285 – 30117
Helixi306 – 31712
Helixi323 – 3319
Helixi336 – 35318
Helixi388 – 40013
Helixi406 – 41611
Helixi420 – 43415

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CQTX-ray3.20A/B278-439[»]
1E3OX-ray1.90C280-438[»]
1GT0X-ray2.60C280-438[»]
1HF0X-ray2.70A/B280-438[»]
1O4XNMR-A280-442[»]
1OCTX-ray3.00C284-439[»]
1POGNMR-A378-437[»]
1POUNMR-A284-354[»]
DisProtiDP00231.
ProteinModelPortaliP14859.
SMRiP14859. Positions 282-438.

Miscellaneous databases

EvolutionaryTraceiP14859.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini280 – 35475POU-specificAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Homeobox

Phylogenomic databases

eggNOGiNOG267922.
HOGENOMiHOG000220842.
HOVERGENiHBG057016.
InParanoidiP14859.
KOiK09364.
PhylomeDBiP14859.

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
1.10.260.40. 1 hit.
InterProiIPR017970. Homeobox_CS.
IPR001356. Homeobox_dom.
IPR009057. Homeodomain-like.
IPR010982. Lambda_DNA-bd_dom.
IPR013847. POU.
IPR000327. POU_specific.
IPR000972. TF_octamer.
[Graphical view]
PfamiPF00046. Homeobox. 1 hit.
PF00157. Pou. 1 hit.
[Graphical view]
PRINTSiPR00029. OCTAMER.
PR00028. POUDOMAIN.
SMARTiSM00389. HOX. 1 hit.
SM00352. POU. 1 hit.
[Graphical view]
SUPFAMiSSF46689. SSF46689. 1 hit.
SSF47413. SSF47413. 1 hit.
PROSITEiPS00027. 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]

Sequences (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P14859-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MNNPSETSKP SMESGDGNTG TQTNGLDFQK QPVPVGGAIS TAQAQAFLGH    50
LHQVQLAGTS LQAAAQSLNV QSKSNEESGD SQQPSQPSQQ PSVQAAIPQT 100
QLMLAGGQIT GLTLTPAQQQ LLLQQAQAQA QLLAAAVQQH SASQQHSAAG 150
ATISASAATP MTQIPLSQPI QIAQDLQQLQ QLQQQNLNLQ QFVLVHPTTN 200
LQPAQFIISQ TPQGQQGLLQ AQNLLTQLPQ QSQANLLQSQ PSITLTSQPA 250
TPTRTIAATP IQTLPQSQST PKRIDTPSLE EPSDLEELEQ FAKTFKQRRI 300
KLGFTQGDVG LAMGKLYGND FSQTTISRFE ALNLSFKNMC KLKPLLEKWL 350
NDAENLSSDS SLSSPSALNS PGIEGLSRRR KKRTSIETNI RVALEKSFLE 400
NQKPTSEEIT MIADQLNMEK EVIRVWFCNR RQKEKRINPP SSGGTSSSPI 450
KAIFPSPTSL VATTPSLVTS SAATTLTVSP VLPLTSAAVT NLSVTGTSDT 500
TSNNTATVIS TAPPASSAVT SPSLSPSPSA SASTSEASSA SETSTTQTTS 550
TPLSSPLGTS QVMVTASGLQ TAAAAALQGA AQLPANASLA AMAAAAGLNP 600
SLMAPSQFAA GGALLSLNPG TLSGALSPAL MSNSTLATIQ ALASGGSLPI 650
TSLDATGNLV FANAGGAPNI VTAPLFLNPQ NLSLLTSNPV SLVSAAAASA 700
GNSAPVASLH ATSTSAESIQ NSLFTVASAS GAASTTTTAS KAQ 743
Length:743
Mass (Da):76,472
Last modified:February 1, 2003 - v2
Checksum:iFAB27FFC79CF2276
GO
Isoform 2 (identifier: P14859-2) [UniParc]FASTAAdd to Basket

Also known as: Oct-1L, lymphocyte-specific

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MLDCSDYVLDSRM

Show »
Length:755
Mass (Da):77,870
Checksum:i084E222919B616AA
GO
Isoform 3 (identifier: P14859-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-20: MNNPSETSKPSMESGDGNTG → MKTRMKIFVMIHFHLMNS

Note: No experimental confirmation available.

Show »
Length:741
Mass (Da):76,696
Checksum:i28E72DF211628CE3
GO
Isoform 6 (identifier: P14859-6) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MADGGAASQDESSAAAAAAADSRM

Note: No experimental confirmation available.

Show »
Length:766
Mass (Da):78,535
Checksum:i54C541CD1D6BA426
GO
Isoform 4 (identifier: P14859-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     641-653: ALASGGSLPITSL → GLLHGLENFLTKN
     654-743: Missing.

Note: No experimental confirmation available.

Show »
Length:653
Mass (Da):68,143
Checksum:i1C82E7818D70A368
GO
Isoform 5 (identifier: P14859-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MADGGAASQDESSAAAAAAADSRM
     112-174: Missing.

Note: No experimental confirmation available.

Show »
Length:703
Mass (Da):72,082
Checksum:i1E6037CDCF41F528
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti88 – 881S → F in a breast cancer sample; somatic mutation. 1 Publication
VAR_035816

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2020MNNPS…DGNTG → MKTRMKIFVMIHFHLMNS in isoform 3. VSP_013421Add
BLAST
Alternative sequencei1 – 11M → MLDCSDYVLDSRM in isoform 2. VSP_002320
Alternative sequencei1 – 11M → MADGGAASQDESSAAAAAAA DSRM in isoform 5 and isoform 6. VSP_043195
Alternative sequencei112 – 17463Missing in isoform 5. VSP_043196Add
BLAST
Alternative sequencei641 – 65313ALASG…PITSL → GLLHGLENFLTKN in isoform 4. VSP_013422Add
BLAST
Alternative sequencei654 – 74390Missing in isoform 4. VSP_013423Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti225 – 2251L → Q in CAA31767. 1 Publication
Sequence conflicti546 – 5461T → I in AAM77920. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X13403 mRNA. Translation: CAA31767.1.
AY113189 mRNA. Translation: AAM77920.1.
AK303201 mRNA. Translation: BAG64291.1.
AL136984 Genomic DNA. Translation: CAI15167.1.
AL136984 Genomic DNA. Translation: CAI15169.1.
AL136984 Genomic DNA. Translation: CAI15170.1.
AL136984 Genomic DNA. Translation: CAI15171.1.
AL359962 Genomic DNA. No translation available.
AL451050 Genomic DNA. No translation available.
CH471067 Genomic DNA. Translation: EAW90786.1.
CH471067 Genomic DNA. Translation: EAW90788.1.
BC001664 mRNA. Translation: AAH01664.1.
BC003571 mRNA. Translation: AAH03571.1.
BC007388 mRNA. Translation: AAH07388.1.
BC052274 mRNA. Translation: AAH52274.1.
CCDSiCCDS1259.2. [P14859-6]
CCDS55655.1. [P14859-5]
CCDS55656.1. [P14859-2]
PIRiA47001.
RefSeqiNP_001185712.1. NM_001198783.1. [P14859-2]
NP_001185715.1. NM_001198786.1. [P14859-5]
NP_002688.3. NM_002697.3. [P14859-6]
UniGeneiHs.283402.

Genome annotation databases

EnsembliENST00000367862; ENSP00000356836; ENSG00000143190. [P14859-2]
ENST00000420254; ENSP00000414660; ENSG00000143190. [P14859-4]
ENST00000429375; ENSP00000401217; ENSG00000143190. [P14859-5]
ENST00000443275; ENSP00000415993; ENSG00000143190.
ENST00000541643; ENSP00000441285; ENSG00000143190. [P14859-1]
GeneIDi5451.
KEGGihsa:5451.
UCSCiuc001gec.3. human. [P14859-1]
uc001ged.3. human. [P14859-3]
uc001gee.3. human.
uc001gef.3. human. [P14859-2]
uc001geg.3. human. [P14859-4]
uc010plh.2. human. [P14859-5]

Polymorphism databases

DMDMi28202257.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X13403 mRNA. Translation: CAA31767.1 .
AY113189 mRNA. Translation: AAM77920.1 .
AK303201 mRNA. Translation: BAG64291.1 .
AL136984 Genomic DNA. Translation: CAI15167.1 .
AL136984 Genomic DNA. Translation: CAI15169.1 .
AL136984 Genomic DNA. Translation: CAI15170.1 .
AL136984 Genomic DNA. Translation: CAI15171.1 .
AL359962 Genomic DNA. No translation available.
AL451050 Genomic DNA. No translation available.
CH471067 Genomic DNA. Translation: EAW90786.1 .
CH471067 Genomic DNA. Translation: EAW90788.1 .
BC001664 mRNA. Translation: AAH01664.1 .
BC003571 mRNA. Translation: AAH03571.1 .
BC007388 mRNA. Translation: AAH07388.1 .
BC052274 mRNA. Translation: AAH52274.1 .
CCDSi CCDS1259.2. [P14859-6 ]
CCDS55655.1. [P14859-5 ]
CCDS55656.1. [P14859-2 ]
PIRi A47001.
RefSeqi NP_001185712.1. NM_001198783.1. [P14859-2 ]
NP_001185715.1. NM_001198786.1. [P14859-5 ]
NP_002688.3. NM_002697.3. [P14859-6 ]
UniGenei Hs.283402.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1CQT X-ray 3.20 A/B 278-439 [» ]
1E3O X-ray 1.90 C 280-438 [» ]
1GT0 X-ray 2.60 C 280-438 [» ]
1HF0 X-ray 2.70 A/B 280-438 [» ]
1O4X NMR - A 280-442 [» ]
1OCT X-ray 3.00 C 284-439 [» ]
1POG NMR - A 378-437 [» ]
1POU NMR - A 284-354 [» ]
DisProti DP00231.
ProteinModelPortali P14859.
SMRi P14859. Positions 282-438.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111447. 51 interactions.
DIPi DIP-226N.
IntActi P14859. 3 interactions.
MINTi MINT-149153.
STRINGi 9606.ENSP00000271411.

PTM databases

PhosphoSitei P14859.

Polymorphism databases

DMDMi 28202257.

Proteomic databases

MaxQBi P14859.
PaxDbi P14859.
PRIDEi P14859.

Protocols and materials databases

DNASUi 5451.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000367862 ; ENSP00000356836 ; ENSG00000143190 . [P14859-2 ]
ENST00000420254 ; ENSP00000414660 ; ENSG00000143190 . [P14859-4 ]
ENST00000429375 ; ENSP00000401217 ; ENSG00000143190 . [P14859-5 ]
ENST00000443275 ; ENSP00000415993 ; ENSG00000143190 .
ENST00000541643 ; ENSP00000441285 ; ENSG00000143190 . [P14859-1 ]
GeneIDi 5451.
KEGGi hsa:5451.
UCSCi uc001gec.3. human. [P14859-1 ]
uc001ged.3. human. [P14859-3 ]
uc001gee.3. human.
uc001gef.3. human. [P14859-2 ]
uc001geg.3. human. [P14859-4 ]
uc010plh.2. human. [P14859-5 ]

Organism-specific databases

CTDi 5451.
GeneCardsi GC01P167190.
H-InvDB HIX0018279.
HGNCi HGNC:9212. POU2F1.
HPAi CAB002608.
HPA045784.
MIMi 164175. gene.
neXtProti NX_P14859.
PharmGKBi PA33536.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG267922.
HOGENOMi HOG000220842.
HOVERGENi HBG057016.
InParanoidi P14859.
KOi K09364.
PhylomeDBi P14859.

Enzyme and pathway databases

Reactomei REACT_22339. RNA Polymerase III Abortive And Retractive Initiation.
REACT_571. RNA Polymerase III Transcription Initiation From Type 3 Promoter.
SignaLinki P14859.

Miscellaneous databases

ChiTaRSi POU2F1. human.
EvolutionaryTracei P14859.
GeneWikii POU2F1.
GenomeRNAii 5451.
NextBioi 21097.
PROi P14859.
SOURCEi Search...

Gene expression databases

ArrayExpressi P14859.
Bgeei P14859.
CleanExi HS_POU2F1.
Genevestigatori P14859.

Family and domain databases

Gene3Di 1.10.10.60. 1 hit.
1.10.260.40. 1 hit.
InterProi IPR017970. Homeobox_CS.
IPR001356. Homeobox_dom.
IPR009057. Homeodomain-like.
IPR010982. Lambda_DNA-bd_dom.
IPR013847. POU.
IPR000327. POU_specific.
IPR000972. TF_octamer.
[Graphical view ]
Pfami PF00046. Homeobox. 1 hit.
PF00157. Pou. 1 hit.
[Graphical view ]
PRINTSi PR00029. OCTAMER.
PR00028. POUDOMAIN.
SMARTi SM00389. HOX. 1 hit.
SM00352. POU. 1 hit.
[Graphical view ]
SUPFAMi SSF46689. SSF46689. 1 hit.
SSF47413. SSF47413. 1 hit.
PROSITEi 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The ubiquitous octamer-binding protein Oct-1 contains a POU domain with a homeo box subdomain."
    Sturm R.A., Das G., Herr W.
    Genes Dev. 2:1582-1599(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6).
    Tissue: Teratocarcinoma.
  2. "Human Oct-1L isoform has tissue-specific expression pattern similar to Oct-2."
    Luchina N.N., Krivega I.V., Pankratova E.V.
    Immunol. Lett. 85:237-241(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: B-cell lymphoma.
  3. "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] (ISOFORM 5).
    Tissue: Thymus.
  4. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 93-653 (ISOFORM 4).
    Tissue: Lung, Lymph and Skin.
  7. "Mitotic phosphorylation of the Oct-1 homeodomain and regulation of Oct-1 DNA binding activity."
    Segil N., Roberts S.B., Heintz N.
    Science 254:1814-1816(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-385, MUTAGENESIS OF SER-385, FUNCTION IN DNA-BINDING ACTIVITY.
  8. "Selective binding of steroid hormone receptors to octamer transcription factors determines transcriptional synergism at the mouse mammary tumor virus promoter."
    Prefontaine G.G., Walther R., Giffin W., Lemieux M.E., Pope L., Hache R.J.G.
    J. Biol. Chem. 274:26713-26719(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NR3C1; AR AND PGR.
  9. "Mutations in host cell factor 1 separate its role in cell proliferation from recruitment of VP16 and LZIP."
    Mahajan S.S., Wilson A.C.
    Mol. Cell. Biol. 20:919-928(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HCFC1.
  10. "Down-regulation of histone H2B by DNA-dependent protein kinase in response to DNA damage through modulation of octamer transcription factor 1."
    Schild-Poulter C., Shih A., Yarymowich N.C., Hache R.J.G.
    Cancer Res. 63:7197-7205(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION.
  11. "The herpes simplex virus VP16-induced complex: the makings of a regulatory switch."
    Wysocka J., Herr W.
    Trends Biochem. Sci. 28:294-304(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON HERPES INFECTION.
  12. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-270; SER-283 AND SER-448, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "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].
  15. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "Solution structure of the POU-specific DNA-binding domain of Oct-1."
    Dekker N., Cox M., Boelens R., Verrijzer C.P., van der Vliet P.C., Kaptein R.
    Nature 362:852-855(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 284-359.
  19. "The solution structure of the Oct-1 POU-specific domain reveals a striking similarity to the bacteriophage lambda repressor DNA-binding domain."
    Assa-Munt N., Mortishire-Smith R.J., Aurora R., Herr W., Wright P.E.
    Cell 73:193-205(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 284-354.
  20. "Solution structure of the Oct-1 POU homeodomain determined by NMR and restrained molecular dynamics."
    Cox M., van Tilborg P.J.A., de Laat W., Boelens R., van Leeuwen H.C., van der Vliet P.C., Kaptein R.
    J. Biomol. NMR 6:23-32(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 378-437.
  21. "Crystal structure of the Oct-1 POU domain bound to an octamer site: DNA recognition with tethered DNA-binding modules."
    Klemm J.D., Rould M.A., Aurora R., Herr W., Pabo C.O.
    Cell 77:21-32(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 284-439.
  22. Cited for: VARIANT [LARGE SCALE ANALYSIS] PHE-88.

Entry informationi

Entry nameiPO2F1_HUMAN
AccessioniPrimary (citable) accession number: P14859
Secondary accession number(s): B1AL91
, B1AL93, B4E029, J3KP77, Q5TBT7, Q6PK46, Q8NEU9, Q9BPV1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: February 1, 2003
Last modified: September 3, 2014
This is version 177 of the entry and version 2 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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