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Protein

Histone H4 transcription factor

Gene

HINFP

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

Functioni

Transcriptional repressor that binds to the consensus sequence 5'-CGGACGTT-3' and to the RB1 promoter. Transcriptional activator that promotes histone H4 gene transcription at the G1/S phase transition in conjunction with NPAT. Also activates transcription of the ATM and PRKDC genes. Autoregulates its expression by associating with its own promoter.7 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri15 – 3925C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri129 – 15325C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri169 – 19325C2H2-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri199 – 22123C2H2-type 4; degeneratePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri229 – 25123C2H2-type 5PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri255 – 27824C2H2-type 6PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri284 – 30623C2H2-type 7PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri312 – 33726C2H2-type 8PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri345 – 36824C2H2-type 9PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • chromatin binding Source: Ensembl
  • DNA binding Source: UniProtKB
  • enzyme binding Source: UniProtKB
  • histone binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: Ensembl
  • transcriptional repressor activity, RNA polymerase II core promoter proximal region sequence-specific binding Source: Ensembl
  • transcription coactivator activity Source: UniProtKB
  • transcription factor activity, sequence-specific DNA binding Source: UniProtKB
  • transcription regulatory region DNA binding Source: UniProtKB

GO - Biological processi

  • DNA damage checkpoint Source: UniProtKB
  • DNA repair Source: UniProtKB
  • establishment of protein localization Source: UniProtKB
  • G1/S transition of mitotic cell cycle Source: UniProtKB
  • in utero embryonic development Source: UniProtKB
  • myoblast differentiation Source: UniProtKB
  • negative regulation of gene expression Source: UniProtKB
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • positive regulation of gene expression Source: UniProtKB
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • regulation of gene expression Source: UniProtKB
  • regulation of transcription, DNA-templated Source: UniProtKB
  • regulation of transcription involved in G1/S transition of mitotic cell cycle Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

SignaLinkiQ9BQA5.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H4 transcription factor
Alternative name(s):
Histone nuclear factor P
Short name:
HiNF-P
MBD2-interacting zinc finger protein
Methyl-CpG-binding protein 2-interacting zinc finger protein
Gene namesi
Name:HINFP
Synonyms:MIZF, ZNF743
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:17850. HINFP.

Subcellular locationi

GO - Cellular componenti

  • Cajal body Source: UniProtKB
  • nucleoplasm Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi381 – 3811Y → A: Abolishes DNA-Binding. 1 Publication

Organism-specific databases

PharmGKBiPA164720597.

Polymorphism and mutation databases

BioMutaiHINFP.
DMDMi322510032.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 517517Histone H4 transcription factorPRO_0000047218Add
BLAST

Post-translational modificationi

Ubiquitinated. Ubiquitination may lead to proteasome-mediated degradation.1 Publication

Keywords - PTMi

Ubl conjugation

Proteomic databases

PaxDbiQ9BQA5.
PRIDEiQ9BQA5.

PTM databases

PhosphoSiteiQ9BQA5.

Expressioni

Tissue specificityi

Ubiquitous. Highly expressed in brain, heart, skeletal muscle, spleen, kidney, small intestine, placenta and liver.1 Publication

Gene expression databases

BgeeiQ9BQA5.
ExpressionAtlasiQ9BQA5. baseline and differential.
GenevisibleiQ9BQA5. HS.

Organism-specific databases

HPAiHPA061008.

Interactioni

Subunit structurei

Binds MBD2 and a histone deacetylase complex. Interacts with NPAT.2 Publications

GO - Molecular functioni

  • enzyme binding Source: UniProtKB
  • histone binding Source: UniProtKB

Protein-protein interaction databases

BioGridi117469. 36 interactions.
IntActiQ9BQA5. 5 interactions.
MINTiMINT-210289.
STRINGi9606.ENSP00000318085.

Structurei

3D structure databases

ProteinModelPortaliQ9BQA5.
SMRiQ9BQA5. Positions 14-47, 171-372.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni373 – 517145Interaction with NPATAdd
BLAST
Regioni374 – 40734Required for activation of histone H4 transcription and contributes to DNA-bindingAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi49 – 568Poly-Glu
Compositional biasi440 – 4445Poly-Glu

Sequence similaritiesi

Contains 9 C2H2-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri15 – 3925C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri129 – 15325C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri169 – 19325C2H2-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri199 – 22123C2H2-type 4; degeneratePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri229 – 25123C2H2-type 5PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri255 – 27824C2H2-type 6PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri284 – 30623C2H2-type 7PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri312 – 33726C2H2-type 8PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri345 – 36824C2H2-type 9PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG3608. Eukaryota.
ENOG410XQF8. LUCA.
GeneTreeiENSGT00530000063079.
HOGENOMiHOG000232129.
InParanoidiQ9BQA5.
OMAiHSKEPAY.
OrthoDBiEOG75QR47.
PhylomeDBiQ9BQA5.
TreeFamiTF350923.

Family and domain databases

Gene3Di3.30.160.60. 5 hits.
InterProiIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
SMARTiSM00355. ZnF_C2H2. 10 hits.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 7 hits.
PS50157. ZINC_FINGER_C2H2_2. 6 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9BQA5-1) [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

        10         20         30         40         50
MPPPGKVPRK ENLWLQCEWG SCSFVCSTME KFFEHVTQHL QQHLHGSGEE
60 70 80 90 100
EEEEEEDDPL EEEFSCLWQE CGFCSLDSSA DLIRHVYFHC YHTKLKQWGL
110 120 130 140 150
QALQSQADLG PCILDFQSRN VIPDIPDHFL CLWEHCENSF DNPEWFYRHV
160 170 180 190 200
EAHSLCCEYE AVGKDNPVVL CGWKGCTCTF KDRSKLREHL RSHTQEKVVA
210 220 230 240 250
CPTCGGMFAN NTKFLDHIRR QTSLDQQHFQ CSHCSKRFAT ERLLRDHMRN
260 270 280 290 300
HVNHYKCPLC DMTCPLPSSL RNHMRFRHSE DRPFKCDCCD YSCKNLIDLQ
310 320 330 340 350
KHLDTHSEEP AYRCDFENCT FSARSLCSIK SHYRKVHEGD SEPRYKCHVC
360 370 380 390 400
DKCFTRGNNL TVHLRKKHQF KWPSGHPRFR YKEHEDGYMR LQLVRYESVE
410 420 430 440 450
LTQQLLRQPQ EGSGLGTSLN ESSLQGIILE TVPGEPGRKE EEEEGKGSEG
460 470 480 490 500
TALSASQDNP SSVIHVVNQT NAQGQQEIVY YVLSEAPGEP PPAPEPPSGG
510
IMEKLQGIAE EPEIQMV
Length:517
Mass (Da):59,678
Last modified:February 8, 2011 - v2
Checksum:i2CE1910737B0B6EB
GO
Isoform 2 (identifier: Q9BQA5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     381-419: YKEHEDGYMR...QEGSGLGTSL → LGHFCIPLPG...CGCSWFATRV
     420-517: Missing.

Note: No experimental confirmation available.
Show »
Length:419
Mass (Da):48,993
Checksum:i31245BA4887EEC8C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti62 – 621E → G in BAG62976 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti4 – 41P → S.1 Publication
Corresponds to variant rs17850972 [ dbSNP | Ensembl ].
VAR_026547
Natural varianti78 – 781S → C.1 Publication
Corresponds to variant rs17850974 [ dbSNP | Ensembl ].
VAR_026548
Natural varianti352 – 3521K → R.
Corresponds to variant rs34118252 [ dbSNP | Ensembl ].
VAR_038793
Natural varianti493 – 4931A → V.1 Publication
Corresponds to variant rs100803 [ dbSNP | Ensembl ].
VAR_019424

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei381 – 41939YKEHE…LGTSL → LGHFCIPLPGFAALYAPTSP GTRNMKMAICGCSWFATRV in isoform 2. 1 PublicationVSP_044719Add
BLAST
Alternative sequencei420 – 51798Missing in isoform 2. 1 PublicationVSP_044720Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK056362 mRNA. Translation: BAG51688.1.
AK301452 mRNA. Translation: BAG62976.1.
AP002956 Genomic DNA. No translation available.
AP003391 Genomic DNA. No translation available.
CH471065 Genomic DNA. Translation: EAW67461.1.
BC001073 mRNA. Translation: AAH01073.1.
BC001945 mRNA. Translation: AAH01945.1.
BC012856 mRNA. Translation: AAH12856.1.
BC017234 mRNA. Translation: AAH17234.1.
AL080201 mRNA. Translation: CAB45773.1.
CCDSiCCDS58188.1. [Q9BQA5-2]
CCDS8414.1. [Q9BQA5-1]
PIRiT12509.
RefSeqiNP_001230188.1. NM_001243259.1. [Q9BQA5-2]
NP_056332.2. NM_015517.4. [Q9BQA5-1]
NP_945322.1. NM_198971.2. [Q9BQA5-1]
XP_011541047.1. XM_011542745.1. [Q9BQA5-1]
UniGeneiHs.504091.

Genome annotation databases

EnsembliENST00000350777; ENSP00000318085; ENSG00000172273. [Q9BQA5-1]
ENST00000527410; ENSP00000436815; ENSG00000172273. [Q9BQA5-2]
GeneIDi25988.
KEGGihsa:25988.
UCSCiuc001pvq.4. human. [Q9BQA5-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK056362 mRNA. Translation: BAG51688.1.
AK301452 mRNA. Translation: BAG62976.1.
AP002956 Genomic DNA. No translation available.
AP003391 Genomic DNA. No translation available.
CH471065 Genomic DNA. Translation: EAW67461.1.
BC001073 mRNA. Translation: AAH01073.1.
BC001945 mRNA. Translation: AAH01945.1.
BC012856 mRNA. Translation: AAH12856.1.
BC017234 mRNA. Translation: AAH17234.1.
AL080201 mRNA. Translation: CAB45773.1.
CCDSiCCDS58188.1. [Q9BQA5-2]
CCDS8414.1. [Q9BQA5-1]
PIRiT12509.
RefSeqiNP_001230188.1. NM_001243259.1. [Q9BQA5-2]
NP_056332.2. NM_015517.4. [Q9BQA5-1]
NP_945322.1. NM_198971.2. [Q9BQA5-1]
XP_011541047.1. XM_011542745.1. [Q9BQA5-1]
UniGeneiHs.504091.

3D structure databases

ProteinModelPortaliQ9BQA5.
SMRiQ9BQA5. Positions 14-47, 171-372.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117469. 36 interactions.
IntActiQ9BQA5. 5 interactions.
MINTiMINT-210289.
STRINGi9606.ENSP00000318085.

PTM databases

PhosphoSiteiQ9BQA5.

Polymorphism and mutation databases

BioMutaiHINFP.
DMDMi322510032.

Proteomic databases

PaxDbiQ9BQA5.
PRIDEiQ9BQA5.

Protocols and materials databases

DNASUi25988.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000350777; ENSP00000318085; ENSG00000172273. [Q9BQA5-1]
ENST00000527410; ENSP00000436815; ENSG00000172273. [Q9BQA5-2]
GeneIDi25988.
KEGGihsa:25988.
UCSCiuc001pvq.4. human. [Q9BQA5-1]

Organism-specific databases

CTDi25988.
GeneCardsiHINFP.
HGNCiHGNC:17850. HINFP.
HPAiHPA061008.
MIMi607099. gene.
neXtProtiNX_Q9BQA5.
PharmGKBiPA164720597.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3608. Eukaryota.
ENOG410XQF8. LUCA.
GeneTreeiENSGT00530000063079.
HOGENOMiHOG000232129.
InParanoidiQ9BQA5.
OMAiHSKEPAY.
OrthoDBiEOG75QR47.
PhylomeDBiQ9BQA5.
TreeFamiTF350923.

Enzyme and pathway databases

SignaLinkiQ9BQA5.

Miscellaneous databases

GeneWikiiMIZF.
GenomeRNAii25988.
NextBioi47680.
PROiQ9BQA5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BQA5.
ExpressionAtlasiQ9BQA5. baseline and differential.
GenevisibleiQ9BQA5. HS.

Family and domain databases

Gene3Di3.30.160.60. 5 hits.
InterProiIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
SMARTiSM00355. ZnF_C2H2. 10 hits.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 7 hits.
PS50157. ZINC_FINGER_C2H2_2. 6 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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] (ISOFORMS 1 AND 2).
    Tissue: Synovium.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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), VARIANTS SER-4; CYS-78 AND VAL-493.
    Tissue: Eye and Lung.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 356-517 (ISOFORM 1).
    Tissue: Testis.
  6. "Involvement of a novel zinc finger protein, MIZF, in transcriptional repression by interacting with a methyl-CpG-binding protein, MBD2."
    Sekimata M., Takahashi A., Murakami-Sekimata A., Homma Y.
    J. Biol. Chem. 276:42632-42638(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH MBD2.
  7. "Identification of HiNF-P, a key activator of cell cycle-controlled histone H4 genes at the onset of S phase."
    Mitra P., Xie R.-L., Medina R., Hovhannisyan H., Zaidi S.K., Wei Y., Harper J.W., Stein J.L., van Wijnen A.J., Stein G.S.
    Mol. Cell. Biol. 23:8110-8123(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
  8. "Sequence-specific transcriptional repression by an MBD2-interacting zinc finger protein MIZF."
    Sekimata M., Homma Y.
    Nucleic Acids Res. 32:590-597(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "HiNF-P directly links the cyclin E/CDK2/p220NPAT pathway to histone H4 gene regulation at the G1/S phase cell cycle transition."
    Miele A., Braastad C.D., Holmes W.F., Mitra P., Medina R., Xie R.-L., Zaidi S.K., Ye X., Wei Y., Harper J.W., van Wijnen A.J., Stein J.L., Stein G.S.
    Mol. Cell. Biol. 25:6140-6153(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NPAT, SUBCELLULAR LOCATION.
  10. "The histone gene transcription factor HiNF-P stabilizes its cell cycle regulatory co-activator p220NPAT."
    Medina R., van Wijnen A.J., Stein G.S., Stein J.L.
    Biochemistry 45:15915-15920(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION.
  11. "The HiNF-P/p220NPAT cell cycle signaling pathway controls nonhistone target genes."
    Medina R., van der Deen M., Miele-Chamberland A., Xie R.-L., van Wijnen A.J., Stein J.L., Stein G.S.
    Cancer Res. 67:10334-10342(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "HiNF-P is a bifunctional regulator of cell cycle controlled histone H4 gene transcription."
    Mitra P., Xie R.-L., Harper J.W., Stein J.L., Stein G.S., van Wijnen A.J.
    J. Cell. Biochem. 101:181-191(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "The histone gene cell cycle regulator HiNF-P is a unique zinc finger transcription factor with a novel conserved auxiliary DNA-binding motif."
    Medina R., Buck T., Zaidi S.K., Miele-Chamberland A., Lian J.B., Stein J.L., van Wijnen A.J., Stein G.S.
    Biochemistry 47:11415-11423(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, REGION, MUTAGENESIS OF TYR-381.

Entry informationi

Entry nameiHINFP_HUMAN
AccessioniPrimary (citable) accession number: Q9BQA5
Secondary accession number(s): B3KPH6
, B4DWB4, E9PQF4, Q96E65, Q9Y4M7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: February 8, 2011
Last modified: April 13, 2016
This is version 129 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 11
    Human chromosome 11: 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

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 one 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.