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Protein

Transcriptional repressor NF-X1

Gene

NFX1

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

Functioni

Binds to the X-box motif of MHC class II genes and represses their expression. May play an important role in regulating the duration of an inflammatory response by limiting the period in which MHC class II molecules are induced by interferon-gamma. Isoform 3 binds to the X-box motif of TERT promoter and represses its expression. Together with PABPC1 or PABPC4, isoform 1 acts as a coactivator for TERT expression. Mediates E2-dependent ubiquitination.3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri358 – 40952RING-type; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri453 – 47119NF-X1-type 1Add
BLAST
Zinc fingeri506 – 52520NF-X1-type 2Add
BLAST
Zinc fingeri567 – 58620NF-X1-type 3Add
BLAST
Zinc fingeri632 – 65524NF-X1-type 4Add
BLAST
Zinc fingeri694 – 71320NF-X1-type 5Add
BLAST
Zinc fingeri721 – 74020NF-X1-type 6Add
BLAST
Zinc fingeri832 – 85423NF-X1-type 7Add
BLAST
Zinc fingeri863 – 88422NF-X1-type 8Add
BLAST

GO - Molecular functioni

  1. ligase activity Source: UniProtKB-KW
  2. poly(A) RNA binding Source: UniProtKB
  3. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription Source: NTNU_SB
  4. RNA polymerase II regulatory region sequence-specific DNA binding Source: NTNU_SB
  5. sequence-specific DNA binding transcription factor activity Source: ProtInc
  6. zinc ion binding Source: InterPro

GO - Biological processi

  1. inflammatory response Source: ProtInc
  2. negative regulation of MHC class II biosynthetic process Source: Ensembl
  3. negative regulation of transcription from RNA polymerase II promoter Source: NTNU_SB
  4. transcription from RNA polymerase II promoter Source: ProtInc
  5. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Ligase, Repressor

Keywords - Biological processi

Host-virus interaction, Transcription, Transcription regulation, Ubl conjugation pathway

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Transcriptional repressor NF-X1 (EC:6.3.2.-)
Alternative name(s):
Nuclear transcription factor, X box-binding protein 1
Gene namesi
Name:NFX1
Synonyms:NFX2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:7803. NFX1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. nucleoplasm Source: HPA
  3. nucleus Source: HPA
  4. plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi20 – 201F → A: Reduces PABPC1 and PABC4 binding. 1 Publication

Organism-specific databases

PharmGKBiPA31608.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11201120Transcriptional repressor NF-X1PRO_0000055979Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei50 – 501Phosphoserine1 Publication

Post-translational modificationi

Isoform 3 is polyubiquitinated in the presence of HPV16 E6 protein; which leads to proteasomal degradation. Isoform 1 is not polyubiquitinated.

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ12986.
PaxDbiQ12986.
PRIDEiQ12986.

PTM databases

PhosphoSiteiQ12986.

Expressioni

Inductioni

By IFNG/IFN-gamma.

Gene expression databases

BgeeiQ12986.
CleanExiHS_NFX1.
GenevestigatoriQ12986.

Interactioni

Subunit structurei

Isoform 1 and isoform 3 interact with human papillomavirus (HPV) type-16 E6 oncoprotein. Isoform 1 interacts with PABPC1 and PABPC4.2 Publications

Protein-protein interaction databases

BioGridi110865. 40 interactions.
IntActiQ12986. 2 interactions.
STRINGi9606.ENSP00000368856.

Structurei

3D structure databases

ProteinModelPortaliQ12986.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini994 – 106269R3HPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni9 – 2618Interaction with PABPC1 and PABC4Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1084 – 10896Poly-Pro

Domaini

The RING-type zinc finger domain interacts with an ubiquitin-conjugating enzyme (E2) and facilitates ubiquitination.

Sequence similaritiesi

Belongs to the NFX1 family.Curated
Contains 8 NF-X1-type zinc fingers.Curated
Contains 1 R3H domain.PROSITE-ProRule annotation
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri358 – 40952RING-type; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri453 – 47119NF-X1-type 1Add
BLAST
Zinc fingeri506 – 52520NF-X1-type 2Add
BLAST
Zinc fingeri567 – 58620NF-X1-type 3Add
BLAST
Zinc fingeri632 – 65524NF-X1-type 4Add
BLAST
Zinc fingeri694 – 71320NF-X1-type 5Add
BLAST
Zinc fingeri721 – 74020NF-X1-type 6Add
BLAST
Zinc fingeri832 – 85423NF-X1-type 7Add
BLAST
Zinc fingeri863 – 88422NF-X1-type 8Add
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00400000022083.
HOGENOMiHOG000006942.
HOVERGENiHBG003827.
InParanoidiQ12986.
KOiK12236.
OMAiRYCPCGQ.
OrthoDBiEOG7NCV2M.
PhylomeDBiQ12986.
TreeFamiTF105889.

Family and domain databases

Gene3Di3.30.1370.50. 1 hit.
InterProiIPR001374. R3H_ss-bd.
IPR019786. Zinc_finger_PHD-type_CS.
IPR000967. Znf_NFX1.
IPR019787. Znf_PHD-finger.
IPR001841. Znf_RING.
[Graphical view]
PfamiPF01424. R3H. 1 hit.
PF01422. zf-NF-X1. 5 hits.
[Graphical view]
SMARTiSM00393. R3H. 1 hit.
SM00184. RING. 1 hit.
SM00438. ZnF_NFX. 9 hits.
[Graphical view]
SUPFAMiSSF82708. SSF82708. 1 hit.
PROSITEiPS51061. R3H. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q12986-1) [UniParc]FASTAAdd to Basket

Also known as: NFX-123

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

        10         20         30         40         50
MAEAPPVSGT FKFNTDAAEF IPQEKKNSGL NCGTQRRLDS NRIGRRNYSS
60 70 80 90 100
PPPCHLSRQV PYDEISAVHQ HSYHPSGSKP KSQQTSFQSS PCNKSPKSHG
110 120 130 140 150
LQNQPWQKLR NEKHHIRVKK AQSLAEQTSD TAGLESSTRS ESGTDLREHS
160 170 180 190 200
PSESEKEVVG ADPRGAKPKK ATQFVYSYGR GPKVKGKLKC EWSNRTTPKP
210 220 230 240 250
EDAGPESTKP VGVFHPDSSE ASSRKGVLDG YGARRNEQRR YPQKRPPWEV
260 270 280 290 300
EGARPRPGRN PPKQEGHRHT NAGHRNNMGP IPKDDLNERP AKSTCDSENL
310 320 330 340 350
AVINKSSRRV DQEKCTVRRQ DPQVVSPFSR GKQNHVLKNV ETHTGSLIEQ
360 370 380 390 400
LTTEKYECMV CCELVRVTAP VWSCQSCYHV FHLNCIKKWA RSPASQADGQ
410 420 430 440 450
SGWRCPACQN VSAHVPNTYT CFCGKVKNPE WSRNEIPHSC GEVCRKKQPG
460 470 480 490 500
QDCPHSCNLL CHPGPCPPCP AFMTKTCECG RTRHTVRCGQ AVSVHCSNPC
510 520 530 540 550
ENILNCGQHQ CAELCHGGQC QPCQIILNQV CYCGSTSRDV LCGTDVGKSD
560 570 580 590 600
GFGDFSCLKI CGKDLKCGNH TCSQVCHPQP CQQCPRLPQL VRCCPCGQTP
610 620 630 640 650
LSQLLELGSS SRKTCMDPVP SCGKVCGKPL PCGSLDFIHT CEKLCHEGDC
660 670 680 690 700
GPCSRTSVIS CRCSFRTKEL PCTSLKSEDA TFMCDKRCNK KRLCGRHKCN
710 720 730 740 750
EICCVDKEHK CPLICGRKLR CGLHRCEEPC HRGNCQTCWQ ASFDELTCHC
760 770 780 790 800
GASVIYPPVP CGTRPPECTQ TCARVHECDH PVYHSCHSEE KCPPCTFLTQ
810 820 830 840 850
KWCMGKHEFR SNIPCHLVDI SCGLPCSATL PCGMHKCQRL CHKGECLVDE
860 870 880 890 900
PCKQPCTTPR ADCGHPCMAP CHTSSPCPVT ACKAKVELQC ECGRRKEMVI
910 920 930 940 950
CSEASSTYQR IAAISMASKI TDMQLGGSVE ISKLITKKEV HQARLECDEE
960 970 980 990 1000
CSALERKKRL AEAFHISEDS DPFNIRSSGS KFSDSLKEDA RKDLKFVSDV
1010 1020 1030 1040 1050
EKEMETLVEA VNKGKNSKKS HSFPPMNRDH RRIIHDLAQV YGLESVSYDS
1060 1070 1080 1090 1100
EPKRNVVVTA IRGKSVCPPT TLTGVLEREM QARPPPPIPH HRHQSDKNPG
1110 1120
SSNLQKITKE PIIDYFDVQD
Length:1,120
Mass (Da):124,395
Last modified:May 20, 2008 - v2
Checksum:iF2203BE1DB6437E6
GO
Isoform 2 (identifier: Q12986-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1014-1024: GKNSKKSHSFP → VEVETSHWTFL
     1025-1120: Missing.

Show »
Length:1,024
Mass (Da):113,623
Checksum:i4228E14EEF42E3BC
GO
Isoform 3 (identifier: Q12986-3) [UniParc]FASTAAdd to Basket

Also known as: NFX-91

The sequence of this isoform differs from the canonical sequence as follows:
     809-833: FRSNIPCHLVDISCGLPCSATLPCG → QSHYWASTQKKRSHYMKKIPAHACL
     834-1120: Missing.

Show »
Length:833
Mass (Da):92,679
Checksum:iAD2A1E26911EA705
GO

Sequence cautioni

The sequence AAA69517.1 differs from that shown. Reason: Frameshift at positions 78, 202 and 284. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti179 – 1791G → A in AAA69517. 1 PublicationCurated
Sequence conflicti186 – 1861G → E in AAA69517. 1 PublicationCurated
Sequence conflicti312 – 3121Q → P in AAA69517. 1 PublicationCurated
Sequence conflicti419 – 4202YT → FS in AAA69517. 1 PublicationCurated
Sequence conflicti560 – 5601I → T in AAA69517. 1 PublicationCurated
Sequence conflicti653 – 6531C → V in AAA69517. 1 PublicationCurated
Sequence conflicti678 – 6781E → EA in BAF84332. (PubMed:14702039)Curated
Sequence conflicti714 – 7141I → N in AAA69517. 1 PublicationCurated
Sequence conflicti786 – 7861C → G in AAA69517. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti731 – 7311H → Y.
Corresponds to variant rs5017299 [ dbSNP | Ensembl ].
VAR_043380
Natural varianti760 – 7601P → S.
Corresponds to variant rs2860036 [ dbSNP | Ensembl ].
VAR_043381
Natural varianti1086 – 10861P → Q.
Corresponds to variant rs2274866 [ dbSNP | Ensembl ].
VAR_043382

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei809 – 83325FRSNI…TLPCG → QSHYWASTQKKRSHYMKKIP AHACL in isoform 3. CuratedVSP_033682Add
BLAST
Alternative sequencei834 – 1120287Missing in isoform 3. CuratedVSP_033683Add
BLAST
Alternative sequencei1014 – 102411GKNSKKSHSFP → VEVETSHWTFL in isoform 2. 2 PublicationsVSP_033684Add
BLAST
Alternative sequencei1025 – 112096Missing in isoform 2. 2 PublicationsVSP_033685Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF332009 mRNA. Translation: AAK16545.1.
AK291643 mRNA. Translation: BAF84332.1.
AL356472, AL356218 Genomic DNA. Translation: CAH72745.1.
AL356472, AL356218 Genomic DNA. Translation: CAH72746.1.
AL356472 Genomic DNA. Translation: CAH72747.3.
AL356218, AL356472 Genomic DNA. Translation: CAI13304.1.
AL356218, AL356472 Genomic DNA. Translation: CAI13305.1.
CH471071 Genomic DNA. Translation: EAW58510.1.
CH471071 Genomic DNA. Translation: EAW58511.1.
BC012151 mRNA. Translation: AAH12151.1.
U15306 mRNA. Translation: AAA69517.1. Frameshift.
CCDSiCCDS6538.1. [Q12986-1]
CCDS6539.1. [Q12986-2]
CCDS6540.1. [Q12986-3]
PIRiI38869.
RefSeqiNP_002495.2. NM_002504.4. [Q12986-1]
NP_667344.1. NM_147133.2. [Q12986-2]
XP_005251531.1. XM_005251474.2.
UniGeneiHs.413074.

Genome annotation databases

EnsembliENST00000318524; ENSP00000317695; ENSG00000086102. [Q12986-3]
ENST00000379521; ENSP00000368836; ENSG00000086102. [Q12986-2]
ENST00000379540; ENSP00000368856; ENSG00000086102. [Q12986-1]
GeneIDi4799.
KEGGihsa:4799.
UCSCiuc003zso.3. human. [Q12986-3]
uc003zsp.2. human. [Q12986-2]
uc003zsq.3. human. [Q12986-1]

Polymorphism databases

DMDMi189047116.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF332009 mRNA. Translation: AAK16545.1.
AK291643 mRNA. Translation: BAF84332.1.
AL356472, AL356218 Genomic DNA. Translation: CAH72745.1.
AL356472, AL356218 Genomic DNA. Translation: CAH72746.1.
AL356472 Genomic DNA. Translation: CAH72747.3.
AL356218, AL356472 Genomic DNA. Translation: CAI13304.1.
AL356218, AL356472 Genomic DNA. Translation: CAI13305.1.
CH471071 Genomic DNA. Translation: EAW58510.1.
CH471071 Genomic DNA. Translation: EAW58511.1.
BC012151 mRNA. Translation: AAH12151.1.
U15306 mRNA. Translation: AAA69517.1. Frameshift.
CCDSiCCDS6538.1. [Q12986-1]
CCDS6539.1. [Q12986-2]
CCDS6540.1. [Q12986-3]
PIRiI38869.
RefSeqiNP_002495.2. NM_002504.4. [Q12986-1]
NP_667344.1. NM_147133.2. [Q12986-2]
XP_005251531.1. XM_005251474.2.
UniGeneiHs.413074.

3D structure databases

ProteinModelPortaliQ12986.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110865. 40 interactions.
IntActiQ12986. 2 interactions.
STRINGi9606.ENSP00000368856.

PTM databases

PhosphoSiteiQ12986.

Polymorphism databases

DMDMi189047116.

Proteomic databases

MaxQBiQ12986.
PaxDbiQ12986.
PRIDEiQ12986.

Protocols and materials databases

DNASUi4799.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000318524; ENSP00000317695; ENSG00000086102. [Q12986-3]
ENST00000379521; ENSP00000368836; ENSG00000086102. [Q12986-2]
ENST00000379540; ENSP00000368856; ENSG00000086102. [Q12986-1]
GeneIDi4799.
KEGGihsa:4799.
UCSCiuc003zso.3. human. [Q12986-3]
uc003zsp.2. human. [Q12986-2]
uc003zsq.3. human. [Q12986-1]

Organism-specific databases

CTDi4799.
GeneCardsiGC09P033280.
HGNCiHGNC:7803. NFX1.
MIMi603255. gene.
neXtProtiNX_Q12986.
PharmGKBiPA31608.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00400000022083.
HOGENOMiHOG000006942.
HOVERGENiHBG003827.
InParanoidiQ12986.
KOiK12236.
OMAiRYCPCGQ.
OrthoDBiEOG7NCV2M.
PhylomeDBiQ12986.
TreeFamiTF105889.

Miscellaneous databases

ChiTaRSiNFX1. human.
GeneWikiiNFX1.
GenomeRNAii4799.
NextBioi18492.
PROiQ12986.
SOURCEiSearch...

Gene expression databases

BgeeiQ12986.
CleanExiHS_NFX1.
GenevestigatoriQ12986.

Family and domain databases

Gene3Di3.30.1370.50. 1 hit.
InterProiIPR001374. R3H_ss-bd.
IPR019786. Zinc_finger_PHD-type_CS.
IPR000967. Znf_NFX1.
IPR019787. Znf_PHD-finger.
IPR001841. Znf_RING.
[Graphical view]
PfamiPF01424. R3H. 1 hit.
PF01422. zf-NF-X1. 5 hits.
[Graphical view]
SMARTiSM00393. R3H. 1 hit.
SM00184. RING. 1 hit.
SM00438. ZnF_NFX. 9 hits.
[Graphical view]
SUPFAMiSSF82708. SSF82708. 1 hit.
PROSITEiPS51061. R3H. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Li J.M., Sah J.H., Zhou Z.M.
    Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Testis.
  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] (ISOFORM 2).
    Tissue: Placenta.
  3. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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).
    Tissue: Eye.
  6. "A novel cysteine-rich sequence-specific DNA-binding protein interacts with the conserved X-box motif of the human major histocompatibility complex class II genes via a repeated Cys-His domain and functions as a transcriptional repressor."
    Song Z., Krishna S., Thanos D., Strominger J.L., Ono S.J.
    J. Exp. Med. 180:1763-1774(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 48-1120 (ISOFORM 1).
  7. "RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent ubiquitination."
    Lorick K.L., Jensen J.P., Fang S., Ong A.M., Hatakeyama S., Weissman A.M.
    Proc. Natl. Acad. Sci. U.S.A. 96:11364-11369(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS AN E2-DEPENDENT UBIQUITIN-PROTEIN LIGASE.
  8. "Identification of a novel telomerase repressor that interacts with the human papillomavirus type-16 E6/E6-AP complex."
    Gewin L., Myers H., Kiyono T., Galloway D.A.
    Genes Dev. 18:2269-2282(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HPV16 E6, FUNCTION.
  9. "NFX1-123 and poly(A) binding proteins synergistically augment activation of telomerase in human papillomavirus type 16 E6-expressing cells."
    Katzenellenbogen R.A., Egelkrout E.M., Vliet-Gregg P., Gewin L.C., Gafken P.R., Galloway D.A.
    J. Virol. 81:3786-3796(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PABPC1 AND PABPC4, MUTAGENESIS OF PHE-20.
  10. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "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].
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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.

Entry informationi

Entry nameiNFX1_HUMAN
AccessioniPrimary (citable) accession number: Q12986
Secondary accession number(s): A8K6H8
, Q5VXW6, Q96EL5, Q9BXI1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 20, 2008
Last modified: February 4, 2015
This is version 145 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: 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. 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.