Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P15822

- ZEP1_HUMAN

UniProt

P15822 - ZEP1_HUMAN

Protein

Zinc finger protein 40

Gene

HIVEP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 154 (01 Oct 2014)
      Sequence version 3 (28 Jul 2009)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    This protein specifically binds to the DNA sequence 5'-GGGACTTTCC-3' which is found in the enhancer elements of numerous viral promoters such as those of SV40, CMV, or HIV-1. In addition, related sequences are found in the enhancer elements of a number of cellular promoters, including those of the class I MHC, interleukin-2 receptor, and interferon-beta genes. It may act in T-cell activation. Involved in activating HIV-1 gene expression. Isoform 2 and isoform 3 also bind to the IPCS (IRF1 and p53 common sequence) DNA sequence in the promoter region of interferon regulatory factor 1 and p53 genes and are involved in transcription regulation of these genes. Isoform 2 does not activate HIV-1 gene expression. Isoform 2 and isoform 3 may be involved in apoptosis.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri406 – 42823C2H2-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri434 – 45623C2H2-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri959 – 98628C2H2-type 3PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri2088 – 211023C2H2-type 4PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri2116 – 214025C2H2-type 5PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: ProtInc
    2. metal ion binding Source: UniProtKB-KW
    3. protein binding Source: UniProtKB

    GO - Biological processi

    1. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
    2. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Zinc finger protein 40
    Alternative name(s):
    Cirhin interaction protein
    Short name:
    CIRIP
    Gate keeper of apoptosis-activating protein
    Short name:
    GAAP
    Human immunodeficiency virus type I enhancer-binding protein 1
    Short name:
    HIV-EP1
    Major histocompatibility complex-binding protein 1
    Short name:
    MBP-1
    Positive regulatory domain II-binding factor 1
    Short name:
    PRDII-BF1
    Gene namesi
    Name:HIVEP1
    Synonyms:ZNF40
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:4920. HIVEP1.

    Subcellular locationi

    Isoform 3 : Cytoplasm 1 Publication. Nucleus 1 Publication

    GO - Cellular componenti

    1. mitochondrion Source: HPA
    2. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA29297.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 27182718Zinc finger protein 40PRO_0000047369Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei429 – 4291Phosphothreonine1 Publication
    Modified residuei492 – 4921Phosphoserine1 Publication
    Modified residuei495 – 4951Phosphoserine1 Publication
    Modified residuei1036 – 10361Phosphoserine1 Publication
    Modified residuei1735 – 17351Phosphoserine1 Publication
    Modified residuei1749 – 17491Phosphoserine2 Publications
    Modified residuei1753 – 17531Phosphoserine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP15822.
    PaxDbiP15822.
    PRIDEiP15822.

    PTM databases

    PhosphoSiteiP15822.

    Expressioni

    Inductioni

    By mitogens and phorbol ester.

    Gene expression databases

    ArrayExpressiP15822.
    BgeeiP15822.
    CleanExiHS_HIVEP1.
    GenevestigatoriP15822.

    Organism-specific databases

    HPAiHPA050724.

    Interactioni

    Subunit structurei

    Interacts with CIRH1A.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ATXN1P542536EBI-722264,EBI-930964
    CACNA1AO005552EBI-722264,EBI-766279
    CIRH1AQ969X63EBI-722264,EBI-2602591

    Protein-protein interaction databases

    BioGridi109343. 37 interactions.
    IntActiP15822. 55 interactions.
    MINTiMINT-1188428.
    STRINGi9606.ENSP00000368698.

    Structurei

    Secondary structure

    1
    2718
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni2091 – 20933
    Helixi2100 – 210910
    Beta strandi2119 – 21224
    Beta strandi2124 – 21274
    Helixi2128 – 21369
    Beta strandi2137 – 21404

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BBONMR-A2087-2143[»]
    3ZNFNMR-A2114-2143[»]
    4ZNFNMR-A2114-2143[»]
    ProteinModelPortaliP15822.
    SMRiP15822. Positions 405-461, 2087-2143.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP15822.

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi803 – 8064Poly-Ser

    Domaini

    Contains two sets of 2 zinc-fingers, which are widely separated and recognize the same DNA sequence. There is a fifth zinc-finger in-between.

    Sequence similaritiesi

    Contains 5 C2H2-type zinc fingers.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri406 – 42823C2H2-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri434 – 45623C2H2-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri959 – 98628C2H2-type 3PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri2088 – 211023C2H2-type 4PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri2116 – 214025C2H2-type 5PROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG296349.
    HOGENOMiHOG000169307.
    HOVERGENiHBG018160.
    KOiK09239.
    OMAiPPLATKT.
    OrthoDBiEOG7GJ6C1.
    PhylomeDBiP15822.
    TreeFamiTF331837.

    Family and domain databases

    Gene3Di3.30.160.60. 4 hits.
    InterProiIPR007087. Znf_C2H2.
    IPR015880. Znf_C2H2-like.
    IPR013087. Znf_C2H2/integrase_DNA-bd.
    [Graphical view]
    SMARTiSM00355. ZnF_C2H2. 5 hits.
    [Graphical view]
    PROSITEiPS00028. ZINC_FINGER_C2H2_1. 4 hits.
    PS50157. ZINC_FINGER_C2H2_2. 4 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P15822-1) [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

    MPRTKQIHPR NLRDKIEEAQ KELNGAEVSK KEILQAGVKG TSESLKGVKR     50
    KKIVAENHLK KIPKSPLRNP LQAKHKQNTE ESSFAVLHSA SESHKKQNYI 100
    PVKNGKQFTK QNGETPGIIA EASKSEESVS PKKPLFLQQP SELRRWRSEG 150
    ADPAKFSDLD EQCDSSSLSS KTRTDNSECI SSHCGTTSPS YTNTAFDVLL 200
    KAMEPELSTL SQKGSPCAIK TEKLRPNKTA RSPPKLKNSS MDAPNQTSQE 250
    LVAESQSSCT SYTVHMSAAQ KNEQGAMQSA SHLYHQHEHF VPKSNQHNQQ 300
    LPGCSGFTGS LTNLQNQENA KLEQVYNIAV TSSVGLTSPS SRSQVTPQNQ 350
    QMDSASPLSI SPANSTQSPP MPIYNSTHVA SVVNQSVEQM CNLLLKDQKP 400
    KKQGKYICEY CNRACAKPSV LLKHIRSHTG ERPYPCVTCG FSFKTKSNLY 450
    KHKKSHAHTI KLGLVLQPDA GGLFLSHESP KALSIHSDVE DSGESEEEGA 500
    TDERQHDLGA MELQPVHIIK RMSNAETLLK SSFTPSSPEN VIGDFLLQDR 550
    SAESQAVTEL PKVVVHHVTV SPLRTDSPKA MDPKPELSSA QKQKDLQVTN 600
    VQPLSANMSQ GGVSRLETNE NSHQKGDMNP LEGKQDSHVG TVHAQLQRQQ 650
    ATDYSQEQQG KLLSPRSLGS TDSGYFSRSE SADQTVSPPT PFARRLPSTE 700
    QDSGRSNGPS AALVTTSTPS ALPTGEKALL LPGQMRPPLA TKTLEERISK 750
    LISDNEALVD DKQLDSVKPR RTSLSRRGSI DSPKSYIFKD SFQFDLKPVG 800
    RRTSSSSDIP KSPFTPTEKS KQVFLLSVPS LDCLPITRSN SMPTTGYSAV 850
    PANIIPPPHP LRGSQSFDDK IGTFYDDVFV SGPNAPVPQS GHPRTLVRQA 900
    AIEDSSANES HVLGTGQSLD ESHQGCHAAG EAMSVRSKAL AQGPHIEKKK 950
    SHQGRGTMFE CETCRNRYRK LENFENHKKF YCSELHGPKT KVAMREPEHS 1000
    PVPGGLQPQI LHYRVAGSSG IWEQTPQIRK RRKMKSVGDD EELQQNESGT 1050
    SPKSSEGLQF QNALGCNPSL PKHNVTIRSD QQHKNIQLQN SHIHLVARGP 1100
    EQTMDPKLST IMEQQISSAA QDKIELQRHG TGISVIQHTN SLSRPNSFDK 1150
    PEPFERASPV SFQELNRTGK SGSLKVIGIS QEESHPSRDG SHPHQLALSD 1200
    ALRGELQESS RKSPSERHVL GQPSRLVRQH NIQVPEILVT EEPDRDLEAQ 1250
    CHDQEKSEKF SWPQRSETLS KLPTEKLPPK KKRLRLAEIE HSSTESSFDS 1300
    TLSRSLSRES SLSHTSSFSA SLDIEDVSKT EASPKIDFLN KAEFLMIPAG 1350
    LNTLNVPGCH REMRRTASEQ INCTQTSMEV SDLRSKSFDC GSITPPQTTP 1400
    LTELQPPSSP SRVGVTGHVP LLERRRGPLV RQISLNIAPD SHLSPVHPTS 1450
    FQNTALPSVN AVPYQGPQLT STSLAEFSAN TLHSQTQVKD LQAETSNSSS 1500
    TNVFPVQQLC DINLLNQIHA PPSHQSTQLS LQVSTQGSKP DKNSVLSGSS 1550
    KSEDCFAPKY QLHCQVFTSG PSCSSNPVHS LPNQVISDPV GTDHCVTSAT 1600
    LPTKLIDSMS NSHPLLPPEL RPLGSQVQKV PSSFMLPIRL QSSVPAYCFA 1650
    TLTSLPQILV TQDLPNQPIC QTNHSVVPIS EEQNSVPTLQ KGHQNALPNP 1700
    EKEFLCENVF SEMSQNSSLS ESLPITQKIS VGRLSPQQES SASSKRMLSP 1750
    ANSLDIAMEK HQKRAKDENG AVCATDVRPL EALSSRVNEA SKQKKPILVR 1800
    QVCTTEPLDG VMLEKDVFSQ PEISNEAVNL TNVLPADNSS TGCSKFVVIE 1850
    PISELQEFEN IKSSTSLTLT VRSSPAPSEN THISPLKCTD NNQERKSPGV 1900
    KNQGDKVNIQ EQSQQPVTSL SLFNIKDTQQ LAFPSLKTTT NFTWCYLLRQ 1950
    KSLHLPQKDQ KTSAYTDWTV SASNPNPLGL PTKVALALLN SKQNTGKSLY 2000
    CQAITTHSKS DLLVYSSKWK SSLSKRALGN QKSTVVEFSN KDASEINSEQ 2050
    DKENSLIKSE PRRIKIFDGG YKSNEEYVYV RGRGRGKYIC EECGIRCKKP 2100
    SMLKKHIRTH TDVRPYHCTY CNFSFKTKGN LTKHMKSKAH SKKCVDLGVS 2150
    VGLIDEQDTE ESDEKQRFSY ERSGYDLEES DGPDEDDNEN EDDDEDSQAE 2200
    SVLSATPSVT ASPQHLPSRS SLQDPVSTDE DVRITDCFSG VHTDPMDVLP 2250
    RALLTRMTVL STAQSDYNRK TLSPGKARQR AARDENDTIP SVDTSRSPCH 2300
    QMSVDYPESE EILRSSMAGK AVAITQSPSS VRLPPAAAEH SPQTAAGMPS 2350
    VASPHPDPQE QKQQITLQPT PGLPSPHTHL FSHLPLHSQQ QSRTPYNMVP 2400
    VGGIHVVPAG LTYSTFVPLQ AGPVQLTIPA VSVVHRTLGT HRNTVTEVSG 2450
    TTNPAGVAEL SSVVPCIPIG QIRVPGLQNL STPGLQSLPS LSMETVNIVG 2500
    LANTNMAPQV HPPGLALNAV GLQVLTANPS SQSSPAPQAH IPGLQILNIA 2550
    LPTLIPSVSQ VAVDAQGAPE MPASQSKACE TQPKQTSVAS ANQVSRTESP 2600
    QGLPTVQREN AKKVLNPPAP AGDHARLDGL SKMDTEKAAS ANHVKPKPEL 2650
    TSIQGQPAST SQPLLKAHSE VFTKPSGQQT LSPDRQVPRP TALPRRQPTV 2700
    HFSDVSSDDD EDRLVIAT 2718
    Length:2,718
    Mass (Da):296,865
    Last modified:July 28, 2009 - v3
    Checksum:i64C1C1CF06AC25ED
    GO
    Isoform 2 (identifier: P15822-2) [UniParc]FASTAAdd to Basket

    Also known as: Delta 2, GAAP-1

    The sequence of this isoform differs from the canonical sequence as follows:
         1-2017: Missing.
         2018-2024: KWKSSLS → MGQKFQK

    Show »
    Length:701
    Mass (Da):75,714
    Checksum:i001EB17FE50AC810
    GO
    Isoform 3 (identifier: P15822-3) [UniParc]FASTAAdd to Basket

    Also known as: GAAP-2

    The sequence of this isoform differs from the canonical sequence as follows:
         1-2002: Missing.
         2003-2024: AITTHSKSDLLVYSSKWKSSLS → MGQKFQKKSYRLVLKELRNPLL

    Show »
    Length:716
    Mass (Da):77,538
    Checksum:i1F340537E16FCFF1
    GO

    Sequence cautioni

    The sequence CAA35798.1 differs from that shown. Reason: Frameshift at several positions.
    The sequence CAH73909.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAH73982.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAI14768.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAI21070.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti515 – 5151P → N in CAA35798. (PubMed:2106471)Curated
    Sequence conflicti1227 – 12271V → I in CAA35798. (PubMed:2106471)Curated
    Sequence conflicti1436 – 14361N → G in CAA35798. (PubMed:2106471)Curated
    Sequence conflicti1660 – 16601V → E in AAA17534. (PubMed:2108316)Curated
    Sequence conflicti1883 – 18831I → L in CAA35798. (PubMed:2106471)Curated
    Sequence conflicti2067 – 20671F → C in AAV85766. 1 PublicationCurated
    Sequence conflicti2080 – 20801V → I in CAA35798. (PubMed:2106471)Curated
    Sequence conflicti2149 – 21491V → I in CAA35798. (PubMed:2106471)Curated
    Sequence conflicti2388 – 23881S → P in AAV85766. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti187 – 1871T → M.
    Corresponds to variant rs2228209 [ dbSNP | Ensembl ].
    VAR_057383
    Natural varianti362 – 3621P → L.
    Corresponds to variant rs34221818 [ dbSNP | Ensembl ].
    VAR_057384
    Natural varianti716 – 7161T → A.
    Corresponds to variant rs2228210 [ dbSNP | Ensembl ].
    VAR_057385
    Natural varianti828 – 8281V → I.
    Corresponds to variant rs2228218 [ dbSNP | Ensembl ].
    VAR_057386
    Natural varianti873 – 8731T → A.2 Publications
    Corresponds to variant rs6900196 [ dbSNP | Ensembl ].
    VAR_057387
    Natural varianti1074 – 10741N → S.1 Publication
    Corresponds to variant rs2228220 [ dbSNP | Ensembl ].
    VAR_057388
    Natural varianti1170 – 11701K → N.1 Publication
    Corresponds to variant rs34258344 [ dbSNP | Ensembl ].
    VAR_057389
    Natural varianti1520 – 15201A → G.1 Publication
    Corresponds to variant rs2228212 [ dbSNP | Ensembl ].
    VAR_057390
    Natural varianti1609 – 16091M → I.1 Publication
    Corresponds to variant rs2228213 [ dbSNP | Ensembl ].
    VAR_057391
    Natural varianti1915 – 19151Q → R.1 Publication
    Corresponds to variant rs1126472 [ dbSNP | Ensembl ].
    VAR_057392
    Natural varianti2444 – 24441T → M.
    Corresponds to variant rs2228214 [ dbSNP | Ensembl ].
    VAR_059892
    Natural varianti2692 – 26921A → G.2 Publications
    Corresponds to variant rs1042054 [ dbSNP | Ensembl ].
    VAR_059893

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 20172017Missing in isoform 2. 1 PublicationVSP_037714Add
    BLAST
    Alternative sequencei1 – 20022002Missing in isoform 3. 1 PublicationVSP_037715Add
    BLAST
    Alternative sequencei2003 – 202422AITTH…KSSLS → MGQKFQKKSYRLVLKELRNP LL in isoform 3. 1 PublicationVSP_037716Add
    BLAST
    Alternative sequencei2018 – 20247KWKSSLS → MGQKFQK in isoform 2. 1 PublicationVSP_037717

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X51435 mRNA. Translation: CAA35798.1. Frameshift.
    AL391828
    , AL137221, AL157373, Z98050 Genomic DNA. Translation: CAH73909.1. Sequence problems.
    AL157373
    , AL137221, AL391828, Z98050 Genomic DNA. Translation: CAH73982.1. Sequence problems.
    AL137221
    , AL157373, AL391828, Z98050 Genomic DNA. Translation: CAI14768.1. Sequence problems.
    Z98050
    , AL137221, AL157373, AL391828 Genomic DNA. Translation: CAI21070.1. Sequence problems.
    BC140816 mRNA. Translation: AAI40817.1.
    M32019 mRNA. Translation: AAA17534.1.
    AY673640 mRNA. Translation: AAV85766.1.
    CCDSiCCDS43426.1. [P15822-1]
    PIRiA34203.
    RefSeqiNP_002105.3. NM_002114.3.
    UniGeneiHs.567284.

    Genome annotation databases

    EnsembliENST00000379388; ENSP00000368698; ENSG00000095951. [P15822-1]
    GeneIDi3096.
    KEGGihsa:3096.
    UCSCiuc003nac.3. human. [P15822-1]

    Polymorphism databases

    DMDMi254763385.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X51435 mRNA. Translation: CAA35798.1 . Frameshift.
    AL391828
    , AL137221 , AL157373 , Z98050 Genomic DNA. Translation: CAH73909.1 . Sequence problems.
    AL157373
    , AL137221 , AL391828 , Z98050 Genomic DNA. Translation: CAH73982.1 . Sequence problems.
    AL137221
    , AL157373 , AL391828 , Z98050 Genomic DNA. Translation: CAI14768.1 . Sequence problems.
    Z98050
    , AL137221 , AL157373 , AL391828 Genomic DNA. Translation: CAI21070.1 . Sequence problems.
    BC140816 mRNA. Translation: AAI40817.1 .
    M32019 mRNA. Translation: AAA17534.1 .
    AY673640 mRNA. Translation: AAV85766.1 .
    CCDSi CCDS43426.1. [P15822-1 ]
    PIRi A34203.
    RefSeqi NP_002105.3. NM_002114.3.
    UniGenei Hs.567284.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BBO NMR - A 2087-2143 [» ]
    3ZNF NMR - A 2114-2143 [» ]
    4ZNF NMR - A 2114-2143 [» ]
    ProteinModelPortali P15822.
    SMRi P15822. Positions 405-461, 2087-2143.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109343. 37 interactions.
    IntActi P15822. 55 interactions.
    MINTi MINT-1188428.
    STRINGi 9606.ENSP00000368698.

    Chemistry

    ChEMBLi CHEMBL2909.

    PTM databases

    PhosphoSitei P15822.

    Polymorphism databases

    DMDMi 254763385.

    Proteomic databases

    MaxQBi P15822.
    PaxDbi P15822.
    PRIDEi P15822.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000379388 ; ENSP00000368698 ; ENSG00000095951 . [P15822-1 ]
    GeneIDi 3096.
    KEGGi hsa:3096.
    UCSCi uc003nac.3. human. [P15822-1 ]

    Organism-specific databases

    GeneCardsi GC06P012009.
    HGNCi HGNC:4920. HIVEP1.
    HPAi HPA050724.
    MIMi 194540. gene.
    neXtProti NX_P15822.
    PharmGKBi PA29297.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG296349.
    HOGENOMi HOG000169307.
    HOVERGENi HBG018160.
    KOi K09239.
    OMAi PPLATKT.
    OrthoDBi EOG7GJ6C1.
    PhylomeDBi P15822.
    TreeFami TF331837.

    Miscellaneous databases

    ChiTaRSi HIVEP1. human.
    EvolutionaryTracei P15822.
    GeneWikii HIVEP1.
    GenomeRNAii 3096.
    NextBioi 12285.
    PROi P15822.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P15822.
    Bgeei P15822.
    CleanExi HS_HIVEP1.
    Genevestigatori P15822.

    Family and domain databases

    Gene3Di 3.30.160.60. 4 hits.
    InterProi IPR007087. Znf_C2H2.
    IPR015880. Znf_C2H2-like.
    IPR013087. Znf_C2H2/integrase_DNA-bd.
    [Graphical view ]
    SMARTi SM00355. ZnF_C2H2. 5 hits.
    [Graphical view ]
    PROSITEi PS00028. ZINC_FINGER_C2H2_1. 4 hits.
    PS50157. ZINC_FINGER_C2H2_2. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A DNA-binding protein containing two widely separated zinc finger motifs that recognize the same DNA sequence."
      Fan C.M., Maniatis T.
      Genes Dev. 4:29-42(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS SER-1074; ASN-1170; ARG-1915 AND GLY-2692.
    2. "Transcriptional regulator of genes involved in the control of cell growth or cell proliferation. Use of said regulator as a therapeutic or diagnostic agent."
      Tovey M.
      Patent number CA2448384, 12-DEC-2002
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), FUNCTION (ISOFORMS 2 AND 3), SUBCELLULAR LOCATION (ISOFORMS 2 AND 3).
    3. "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].
    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 ALA-873 AND GLY-1520.
    5. "A large protein containing zinc finger domains binds to related sequence elements in the enhancers of the class I major histocompatibility complex and kappa immunoglobulin genes."
      Baldwin A.S. Jr., LeClair K.P., Singh H., Sharp P.A.
      Mol. Cell. Biol. 10:1406-1414(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 817-2718 (ISOFORM 1), VARIANTS ALA-873; ILE-1609 AND GLY-2692.
    6. Yu B., Mitchell G.A., Richter A.
      Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2035-2718 (ISOFORM 1).
      Tissue: Liver.
    7. "Regulation of human immunodeficiency virus enhancer function by PRDII-BF1 and c-rel gene products."
      Muchardt C., Seeler J.S., Nirula A., Shurland D.L., Gaynor R.B.
      J. Virol. 66:244-250(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION (ISOFORM 2), ALTERNATIVE SPLICING.
    8. "Transcription factor PRDII-BF1 activates human immunodeficiency virus type 1 gene expression."
      Seeler J.S., Muchardt C., Suessle A., Gaynor R.B.
      J. Virol. 68:1002-1009(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION (ISOFORM 1).
    9. "GAAP-1: a transcriptional activator of p53 and IRF-1 possesses pro-apoptotic activity."
      Lallemand C., Palmieri M., Blanchard B., Meritet J.F., Tovey M.G.
      EMBO Rep. 3:153-158(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION (ISOFORM 2), SUBCELLULAR LOCATION (ISOFORM 2), ALTERNATIVE SPLICING.
    10. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-429; SER-1036 AND SER-1735, 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. "Cirhin up-regulates a canonical NF-kappaB element through strong interaction with Cirip/HIVEP1."
      Yu B., Mitchell G.A., Richter A.
      Exp. Cell Res. 315:3086-3098(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH CIRH1A.
    14. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-492; SER-495; SER-1749 AND SER-1753, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1749 AND SER-1753, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "High-resolution three-dimensional structure of a single zinc finger from a human enhancer binding protein in solution."
      Omichinski J.G., Clore G.M., Appella E., Sakaguchi K., Gronenborn A.M.
      Biochemistry 29:9324-9334(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 2114-2143.
    17. "High-resolution solution structure of the double Cys2His2 zinc finger from the human enhancer binding protein MBP-1."
      Omichinski J.G., Clore G.M., Robien M., Sakaguchi K., Appella E., Gronenborn A.M.
      Biochemistry 31:3907-3917(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 2088-2143.

    Entry informationi

    Entry nameiZEP1_HUMAN
    AccessioniPrimary (citable) accession number: P15822
    Secondary accession number(s): B2RTU3
    , Q14122, Q5MPB1, Q5VW60
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: July 28, 2009
    Last modified: October 1, 2014
    This is version 154 of the entry and version 3 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 6
      Human chromosome 6: 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