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P15822 (ZEP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 149. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:HIVEP1
Synonyms:ZNF40
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2718 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2 Ref.7 Ref.8 Ref.9

Subunit structure

Interacts with CIRH1A. Ref.13

Subcellular location

Isoform 1: Nucleus Ref.2 Ref.9 Ref.13.

Isoform 2: Cytoplasm. Nucleus Ref.2 Ref.9 Ref.13.

Isoform 3: Cytoplasm. Nucleus Ref.2 Ref.9 Ref.13.

Induction

By mitogens and phorbol ester.

Domain

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 similarities

Contains 5 C2H2-type zinc fingers.

Sequence caution

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.

Ontologies

Binary interactions

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P15822-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P15822-2)

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
Isoform 3 (identifier: P15822-3)

Also known as: GAAP-2;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 27182718Zinc finger protein 40
PRO_0000047369

Regions

Zinc finger406 – 42823C2H2-type 1
Zinc finger434 – 45623C2H2-type 2
Zinc finger959 – 98628C2H2-type 3
Zinc finger2088 – 211023C2H2-type 4
Zinc finger2116 – 214025C2H2-type 5
Compositional bias803 – 8064Poly-Ser

Amino acid modifications

Modified residue4291Phosphothreonine Ref.11
Modified residue4921Phosphoserine Ref.14
Modified residue4951Phosphoserine Ref.14
Modified residue10361Phosphoserine Ref.11
Modified residue17351Phosphoserine Ref.11
Modified residue17491Phosphoserine Ref.14 Ref.15
Modified residue17531Phosphoserine Ref.14 Ref.15

Natural variations

Alternative sequence1 – 20172017Missing in isoform 2.
VSP_037714
Alternative sequence1 – 20022002Missing in isoform 3.
VSP_037715
Alternative sequence2003 – 202422AITTH…KSSLS → MGQKFQKKSYRLVLKELRNP LL in isoform 3.
VSP_037716
Alternative sequence2018 – 20247KWKSSLS → MGQKFQK in isoform 2.
VSP_037717
Natural variant1871T → M.
Corresponds to variant rs2228209 [ dbSNP | Ensembl ].
VAR_057383
Natural variant3621P → L.
Corresponds to variant rs34221818 [ dbSNP | Ensembl ].
VAR_057384
Natural variant7161T → A.
Corresponds to variant rs2228210 [ dbSNP | Ensembl ].
VAR_057385
Natural variant8281V → I.
Corresponds to variant rs2228218 [ dbSNP | Ensembl ].
VAR_057386
Natural variant8731T → A. Ref.4 Ref.5
Corresponds to variant rs6900196 [ dbSNP | Ensembl ].
VAR_057387
Natural variant10741N → S. Ref.1
Corresponds to variant rs2228220 [ dbSNP | Ensembl ].
VAR_057388
Natural variant11701K → N. Ref.1
Corresponds to variant rs34258344 [ dbSNP | Ensembl ].
VAR_057389
Natural variant15201A → G. Ref.4
Corresponds to variant rs2228212 [ dbSNP | Ensembl ].
VAR_057390
Natural variant16091M → I. Ref.5
Corresponds to variant rs2228213 [ dbSNP | Ensembl ].
VAR_057391
Natural variant19151Q → R. Ref.1
Corresponds to variant rs1126472 [ dbSNP | Ensembl ].
VAR_057392
Natural variant24441T → M.
Corresponds to variant rs2228214 [ dbSNP | Ensembl ].
VAR_059892
Natural variant26921A → G. Ref.1 Ref.5
Corresponds to variant rs1042054 [ dbSNP | Ensembl ].
VAR_059893

Experimental info

Sequence conflict5151P → N in CAA35798. Ref.1
Sequence conflict12271V → I in CAA35798. Ref.1
Sequence conflict14361N → G in CAA35798. Ref.1
Sequence conflict16601V → E in AAA17534. Ref.5
Sequence conflict18831I → L in CAA35798. Ref.1
Sequence conflict20671F → C in AAV85766. Ref.6
Sequence conflict20801V → I in CAA35798. Ref.1
Sequence conflict21491V → I in CAA35798. Ref.1
Sequence conflict23881S → P in AAV85766. Ref.6

Secondary structure

........... 2718
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 28, 2009. Version 3.
Checksum: 64C1C1CF06AC25ED

FASTA2,718296,865
        10         20         30         40         50         60 
MPRTKQIHPR NLRDKIEEAQ KELNGAEVSK KEILQAGVKG TSESLKGVKR KKIVAENHLK 

        70         80         90        100        110        120 
KIPKSPLRNP LQAKHKQNTE ESSFAVLHSA SESHKKQNYI PVKNGKQFTK QNGETPGIIA 

       130        140        150        160        170        180 
EASKSEESVS PKKPLFLQQP SELRRWRSEG ADPAKFSDLD EQCDSSSLSS KTRTDNSECI 

       190        200        210        220        230        240 
SSHCGTTSPS YTNTAFDVLL KAMEPELSTL SQKGSPCAIK TEKLRPNKTA RSPPKLKNSS 

       250        260        270        280        290        300 
MDAPNQTSQE LVAESQSSCT SYTVHMSAAQ KNEQGAMQSA SHLYHQHEHF VPKSNQHNQQ 

       310        320        330        340        350        360 
LPGCSGFTGS LTNLQNQENA KLEQVYNIAV TSSVGLTSPS SRSQVTPQNQ QMDSASPLSI 

       370        380        390        400        410        420 
SPANSTQSPP MPIYNSTHVA SVVNQSVEQM CNLLLKDQKP KKQGKYICEY CNRACAKPSV 

       430        440        450        460        470        480 
LLKHIRSHTG ERPYPCVTCG FSFKTKSNLY KHKKSHAHTI KLGLVLQPDA GGLFLSHESP 

       490        500        510        520        530        540 
KALSIHSDVE DSGESEEEGA TDERQHDLGA MELQPVHIIK RMSNAETLLK SSFTPSSPEN 

       550        560        570        580        590        600 
VIGDFLLQDR SAESQAVTEL PKVVVHHVTV SPLRTDSPKA MDPKPELSSA QKQKDLQVTN 

       610        620        630        640        650        660 
VQPLSANMSQ GGVSRLETNE NSHQKGDMNP LEGKQDSHVG TVHAQLQRQQ ATDYSQEQQG 

       670        680        690        700        710        720 
KLLSPRSLGS TDSGYFSRSE SADQTVSPPT PFARRLPSTE QDSGRSNGPS AALVTTSTPS 

       730        740        750        760        770        780 
ALPTGEKALL LPGQMRPPLA TKTLEERISK LISDNEALVD DKQLDSVKPR RTSLSRRGSI 

       790        800        810        820        830        840 
DSPKSYIFKD SFQFDLKPVG RRTSSSSDIP KSPFTPTEKS KQVFLLSVPS LDCLPITRSN 

       850        860        870        880        890        900 
SMPTTGYSAV PANIIPPPHP LRGSQSFDDK IGTFYDDVFV SGPNAPVPQS GHPRTLVRQA 

       910        920        930        940        950        960 
AIEDSSANES HVLGTGQSLD ESHQGCHAAG EAMSVRSKAL AQGPHIEKKK SHQGRGTMFE 

       970        980        990       1000       1010       1020 
CETCRNRYRK LENFENHKKF YCSELHGPKT KVAMREPEHS PVPGGLQPQI LHYRVAGSSG 

      1030       1040       1050       1060       1070       1080 
IWEQTPQIRK RRKMKSVGDD EELQQNESGT SPKSSEGLQF QNALGCNPSL PKHNVTIRSD 

      1090       1100       1110       1120       1130       1140 
QQHKNIQLQN SHIHLVARGP EQTMDPKLST IMEQQISSAA QDKIELQRHG TGISVIQHTN 

      1150       1160       1170       1180       1190       1200 
SLSRPNSFDK PEPFERASPV SFQELNRTGK SGSLKVIGIS QEESHPSRDG SHPHQLALSD 

      1210       1220       1230       1240       1250       1260 
ALRGELQESS RKSPSERHVL GQPSRLVRQH NIQVPEILVT EEPDRDLEAQ CHDQEKSEKF 

      1270       1280       1290       1300       1310       1320 
SWPQRSETLS KLPTEKLPPK KKRLRLAEIE HSSTESSFDS TLSRSLSRES SLSHTSSFSA 

      1330       1340       1350       1360       1370       1380 
SLDIEDVSKT EASPKIDFLN KAEFLMIPAG LNTLNVPGCH REMRRTASEQ INCTQTSMEV 

      1390       1400       1410       1420       1430       1440 
SDLRSKSFDC GSITPPQTTP LTELQPPSSP SRVGVTGHVP LLERRRGPLV RQISLNIAPD 

      1450       1460       1470       1480       1490       1500 
SHLSPVHPTS FQNTALPSVN AVPYQGPQLT STSLAEFSAN TLHSQTQVKD LQAETSNSSS 

      1510       1520       1530       1540       1550       1560 
TNVFPVQQLC DINLLNQIHA PPSHQSTQLS LQVSTQGSKP DKNSVLSGSS KSEDCFAPKY 

      1570       1580       1590       1600       1610       1620 
QLHCQVFTSG PSCSSNPVHS LPNQVISDPV GTDHCVTSAT LPTKLIDSMS NSHPLLPPEL 

      1630       1640       1650       1660       1670       1680 
RPLGSQVQKV PSSFMLPIRL QSSVPAYCFA TLTSLPQILV TQDLPNQPIC QTNHSVVPIS 

      1690       1700       1710       1720       1730       1740 
EEQNSVPTLQ KGHQNALPNP EKEFLCENVF SEMSQNSSLS ESLPITQKIS VGRLSPQQES 

      1750       1760       1770       1780       1790       1800 
SASSKRMLSP ANSLDIAMEK HQKRAKDENG AVCATDVRPL EALSSRVNEA SKQKKPILVR 

      1810       1820       1830       1840       1850       1860 
QVCTTEPLDG VMLEKDVFSQ PEISNEAVNL TNVLPADNSS TGCSKFVVIE PISELQEFEN 

      1870       1880       1890       1900       1910       1920 
IKSSTSLTLT VRSSPAPSEN THISPLKCTD NNQERKSPGV KNQGDKVNIQ EQSQQPVTSL 

      1930       1940       1950       1960       1970       1980 
SLFNIKDTQQ LAFPSLKTTT NFTWCYLLRQ KSLHLPQKDQ KTSAYTDWTV SASNPNPLGL 

      1990       2000       2010       2020       2030       2040 
PTKVALALLN SKQNTGKSLY CQAITTHSKS DLLVYSSKWK SSLSKRALGN QKSTVVEFSN 

      2050       2060       2070       2080       2090       2100 
KDASEINSEQ DKENSLIKSE PRRIKIFDGG YKSNEEYVYV RGRGRGKYIC EECGIRCKKP 

      2110       2120       2130       2140       2150       2160 
SMLKKHIRTH TDVRPYHCTY CNFSFKTKGN LTKHMKSKAH SKKCVDLGVS VGLIDEQDTE 

      2170       2180       2190       2200       2210       2220 
ESDEKQRFSY ERSGYDLEES DGPDEDDNEN EDDDEDSQAE SVLSATPSVT ASPQHLPSRS 

      2230       2240       2250       2260       2270       2280 
SLQDPVSTDE DVRITDCFSG VHTDPMDVLP RALLTRMTVL STAQSDYNRK TLSPGKARQR 

      2290       2300       2310       2320       2330       2340 
AARDENDTIP SVDTSRSPCH QMSVDYPESE EILRSSMAGK AVAITQSPSS VRLPPAAAEH 

      2350       2360       2370       2380       2390       2400 
SPQTAAGMPS VASPHPDPQE QKQQITLQPT PGLPSPHTHL FSHLPLHSQQ QSRTPYNMVP 

      2410       2420       2430       2440       2450       2460 
VGGIHVVPAG LTYSTFVPLQ AGPVQLTIPA VSVVHRTLGT HRNTVTEVSG TTNPAGVAEL 

      2470       2480       2490       2500       2510       2520 
SSVVPCIPIG QIRVPGLQNL STPGLQSLPS LSMETVNIVG LANTNMAPQV HPPGLALNAV 

      2530       2540       2550       2560       2570       2580 
GLQVLTANPS SQSSPAPQAH IPGLQILNIA LPTLIPSVSQ VAVDAQGAPE MPASQSKACE 

      2590       2600       2610       2620       2630       2640 
TQPKQTSVAS ANQVSRTESP QGLPTVQREN AKKVLNPPAP AGDHARLDGL SKMDTEKAAS 

      2650       2660       2670       2680       2690       2700 
ANHVKPKPEL TSIQGQPAST SQPLLKAHSE VFTKPSGQQT LSPDRQVPRP TALPRRQPTV 

      2710 
HFSDVSSDDD EDRLVIAT 

« Hide

Isoform 2 (Delta 2) (GAAP-1) [UniParc].

Checksum: 001EB17FE50AC810
Show »

FASTA70175,714
Isoform 3 (GAAP-2) [UniParc].

Checksum: 1F340537E16FCFF1
Show »

FASTA71677,538

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X51435 mRNA. Translation: CAA35798.1. Frameshift.
AL391828 expand/collapse EMBL AC list , AL137221, AL157373, Z98050 Genomic DNA. Translation: CAH73909.1. Sequence problems.
AL157373 expand/collapse EMBL AC list , AL137221, AL391828, Z98050 Genomic DNA. Translation: CAH73982.1. Sequence problems.
AL137221 expand/collapse EMBL AC list , AL157373, AL391828, Z98050 Genomic DNA. Translation: CAI14768.1. Sequence problems.
Z98050 expand/collapse EMBL AC list , 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.
PIRA34203.
RefSeqNP_002105.2. NM_002114.2.
UniGeneHs.567284.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BBONMR-A2087-2143[»]
3ZNFNMR-A2114-2143[»]
4ZNFNMR-A2114-2143[»]
ProteinModelPortalP15822.
SMRP15822. Positions 405-461, 2087-2143.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109343. 38 interactions.
IntActP15822. 55 interactions.
MINTMINT-1188428.
STRING9606.ENSP00000368698.

Chemistry

ChEMBLCHEMBL2909.

PTM databases

PhosphoSiteP15822.

Polymorphism databases

DMDM254763385.

Proteomic databases

PaxDbP15822.
PRIDEP15822.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000379388; ENSP00000368698; ENSG00000095951. [P15822-1]
GeneID3096.
KEGGhsa:3096.
UCSCuc003nac.3. human. [P15822-1]

Organism-specific databases

CTD3096.
GeneCardsGC06P012009.
HGNCHGNC:4920. HIVEP1.
HPAHPA050724.
MIM194540. gene.
neXtProtNX_P15822.
PharmGKBPA29297.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG296349.
HOGENOMHOG000169307.
HOVERGENHBG018160.
KOK09239.
OMAPPLATKT.
OrthoDBEOG7GJ6C1.
PhylomeDBP15822.
TreeFamTF331837.

Gene expression databases

ArrayExpressP15822.
BgeeP15822.
CleanExHS_HIVEP1.
GenevestigatorP15822.

Family and domain databases

Gene3D3.30.160.60. 4 hits.
InterProIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
SMARTSM00355. ZnF_C2H2. 5 hits.
[Graphical view]
PROSITEPS00028. ZINC_FINGER_C2H2_1. 4 hits.
PS50157. ZINC_FINGER_C2H2_2. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHIVEP1. human.
EvolutionaryTraceP15822.
GeneWikiHIVEP1.
GenomeRNAi3096.
NextBio12285.
PROP15822.
SOURCESearch...

Entry information

Entry nameZEP1_HUMAN
AccessionPrimary (citable) accession number: P15822
Secondary accession number(s): B2RTU3 expand/collapse secondary AC list , Q14122, Q5MPB1, Q5VW60
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: July 28, 2009
Last modified: April 16, 2014
This is version 149 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM