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Q5T1R4

- ZEP3_HUMAN

UniProt

Q5T1R4 - ZEP3_HUMAN

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Protein

Transcription factor HIVEP3

Gene

HIVEP3

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

Functioni

Plays a role of transcription factor; binds to recognition signal sequences (Rss heptamer) for somatic recombination of immunoglobulin and T-cell receptor gene segments; Binds also to the kappa-B motif of gene such as S100A4, involved in cell progression and differentiation. Kappa-B motif is a gene regulatory element found in promoters and enhancers of genes involved in immunity, inflammation, and growth and that responds to viral antigens, mitogens, and cytokines. Involvement of HIVEP3 in cell growth is strengthened by the fact that its down-regulation promotes cell cycle progression with ultimate formation of multinucleated giant cells. Strongly inhibits TNF-alpha-induced NF-kappa-B activation; Interferes with nuclear factor NF-kappa-B by several mechanisms: as transcription factor, by competing for Kappa-B motif and by repressing transcription in the nucleus; through a non transcriptional process, by inhibiting nuclear translocation of RELA by association with TRAF2, an adapter molecule in the tumor necrosis factor signaling, which blocks the formation of IKK complex. Interaction with TRAF proteins inhibits both NF-Kappa-B-mediated and c-Jun N-terminal kinase/JNK-mediated responses that include apoptosis and proinflammatory cytokine gene expression. Positively regulates the expression of IL2 in T-cell. Essential regulator of adult bone formation.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri192 – 21423C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri220 – 24223C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri643 – 66523C2H2-type 3; degeneratePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1754 – 177623C2H2-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1782 – 180625C2H2-type 5PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. DNA binding Source: Ensembl
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. positive regulation of transcription, DNA-templated Source: MGI
  2. skeletal muscle cell differentiation Source: Ensembl
  3. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription factor HIVEP3
Alternative name(s):
Human immunodeficiency virus type I enhancer-binding protein 3
Kappa-B and V(D)J recombination signal sequences-binding protein
Kappa-binding protein 1
Short name:
KBP-1
Zinc finger protein ZAS3
Gene namesi
Name:HIVEP3
Synonyms:KBP1, KIAA1555, KRC, ZAS3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:13561. HIVEP3.

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29299.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 24062406Transcription factor HIVEP3PRO_0000331627Add
BLAST

Post-translational modificationi

Phosphorylated on threonine and serine residues.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ5T1R4.
PaxDbiQ5T1R4.
PRIDEiQ5T1R4.

PTM databases

PhosphoSiteiQ5T1R4.

Expressioni

Inductioni

By 12-O-tetradecanoylphorbol-13 acetate (TPA).

Gene expression databases

BgeeiQ5T1R4.
CleanExiHS_HIVEP3.
GenevestigatoriQ5T1R4.

Organism-specific databases

HPAiHPA005728.

Interactioni

Subunit structurei

Interacts with TRAF1 AND TRAF2 as well as with JUN. Forms a multimeric complex with RUNX2 and E3 ubiquitin ligase WWP1 (By similarity).By similarity

Protein-protein interaction databases

BioGridi121861. 6 interactions.
STRINGi9606.ENSP00000247584.

Structurei

3D structure databases

ProteinModelPortaliQ5T1R4.
SMRiQ5T1R4. Positions 191-247, 1753-1809.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati1964 – 196741
Repeati1970 – 197342
Repeati1993 – 199643
Repeati1998 – 200144
Repeati2067 – 207045
Repeati2079 – 208246

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni192 – 24251ZAS1Add
BLAST
Regioni211 – 1074864No DNA binding activity or transactivation activity, but complete prevention of TRAF-dependent NF-Kappa-B activation; associates with TRAF2 and JUNBy similarityAdd
BLAST
Regioni264 – 28724Acidic 1Add
BLAST
Regioni862 – 88322Acidic 2Add
BLAST
Regioni1754 – 180653ZAS2Add
BLAST
Regioni1817 – 187256Acidic 3Add
BLAST
Regioni2053 – 2148966 X 4 AA tandem repeats of S-P-X-[RK]Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1442 – 146625Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi903 – 9097Nuclear localization signalSequence Analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi308 – 33427Ser-richAdd
BLAST
Compositional biasi378 – 41437Ser-richAdd
BLAST
Compositional biasi797 – 81923Ser-richAdd
BLAST
Compositional biasi844 – 88037Glu/Pro-richAdd
BLAST
Compositional biasi916 – 94833Ser-richAdd
BLAST
Compositional biasi1907 – 193630Ser-richAdd
BLAST

Domaini

The ZAS2 domain binds DNA as dimers, tetramers, and multiple of tetramers and readily forms highly ordred DNA-protein structures.By similarity

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri192 – 21423C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri220 – 24223C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri643 – 66523C2H2-type 3; degeneratePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1754 – 177623C2H2-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1782 – 180625C2H2-type 5PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG296349.
GeneTreeiENSGT00530000063161.
HOGENOMiHOG000155774.
HOVERGENiHBG095595.
InParanoidiQ5T1R4.
KOiK09239.
OMAiMERIPGE.
OrthoDBiEOG7V1FPQ.
PhylomeDBiQ5T1R4.
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. 5 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Note: Additional isoforms can be generated by alternative splicing or polyadenylation. HIVEP3L transcript may lack exon 7 leading to a premature codon stop.1 Publication

Isoform 1 (identifier: Q5T1R4-1) [UniParc]FASTAAdd to Basket

Also known as: HIVEP3S

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
MDPEQSVKGT KKAEGSPRKR LTKGEAIQTS VSSSVPYPGS GTAATQESPA
60 70 80 90 100
QELLAPQPFP GPSSVLREGS QEKTGQQQKP PKRPPIEASV HISQLPQHPL
110 120 130 140 150
TPAFMSPGKP EHLLEGSTWQ LVDPMRPGPS GSFVAPGLHP QSQLLPSHAS
160 170 180 190 200
IIPPEDLPGV PKVFVPRPSQ VSLKPTEEAH KKERKPQKPG KYICQYCSRP
210 220 230 240 250
CAKPSVLQKH IRSHTGERPY PCGPCGFSFK TKSNLYKHRK SHAHRIKAGL
260 270 280 290 300
ASGMGGEMYP HGLEMERIPG EEFEEPTEGE STDSEEETSA TSGHPAELSP
310 320 330 340 350
RPKQPLLSSG LYSSGSHSSS HERCSLSQSS TAQSLEDPPP FVEPSSEHPL
360 370 380 390 400
SHKPEDTHTI KQKLALRLSE RKKVIDEQAF LSPGSKGSTE SGYFSRSESA
410 420 430 440 450
EQQVSPPNTN AKSYAEIIFG KCGRIGQRTA MLTATSTQPL LPLSTEDKPS
460 470 480 490 500
LVPLSVPRTQ VIEHITKLIT INEAVVDTSE IDSVKPRRSS LSRRSSMESP
510 520 530 540 550
KSSLYREPLS SHSEKTKPEQ SLLSLQHPPS TAPPVPLLRS HSMPSAACTI
560 570 580 590 600
STPHHPFRGS YSFDDHITDS EALSHSSHVF TSHPRMLKRQ PAIELPLGGE
610 620 630 640 650
YSSEEPGPSS KDTASKPSDE VEPKESELTK KTKKGLKTKG VIYECNICGA
660 670 680 690 700
RYKKRDNYEA HKKYYCSELQ IAKPISAGTH TSPEAEKSQI EHEPWSQMMH
710 720 730 740 750
YKLGTTLELT PLRKRRKEKS LGDEEEPPAF ESTKSQFGSP GPSDAARNLP
760 770 780 790 800
LESTKSPAEP SKSVPSLEGP TGFQPRTPKP GSGSESGKER RTTSKEISVI
810 820 830 840 850
QHTSSFEKSD SLEQPSGLEG EDKPLAQFPS PPPAPHGRSA HSLQPKLVRQ
860 870 880 890 900
PNIQVPEILV TEEPDRPDTE PEPPPKEPEK TEEFQWPQRS QTLAQLPAEK
910 920 930 940 950
LPPKKKRLRL AEMAQSSGES SFESSVPLSR SPSQESNVSL SGSSRSASFE
960 970 980 990 1000
RDDHGKAEAP SPSSDMRPKP LGTHMLTVPS HHPHAREMRR SASEQSPNVS
1010 1020 1030 1040 1050
HSAHMTETRS KSFDYGSLSL TGPSAPAPVA PPARVAPPER RKCFLVRQAS
1060 1070 1080 1090 1100
LSRPPESELE VAPKGRQESE EPQPSSSKPS AKSSLSQISS AATSHGGPPG
1110 1120 1130 1140 1150
GKGPGQDRPP LGPTVPYTEA LQVFHHPVAQ TPLHEKPYLP PPVSLFSFQH
1160 1170 1180 1190 1200
LVQHEPGQSP EFFSTQAMSS LLSSPYSMPP LPPSLFQAPP LPLQPTVLHP
1210 1220 1230 1240 1250
GQLHLPQLMP HPANIPFRQP PSFLPMPYPT SSALSSGFFL PLQSQFALQL
1260 1270 1280 1290 1300
PGDVESHLPQ IKTSLAPLAT GSAGLSPSTE YSSDIRLPPV APPASSSAPT
1310 1320 1330 1340 1350
SAPPLALPAC PDTMVSLVVP VRVQTNMPSY GSAMYTTLSQ ILVTQSQGSS
1360 1370 1380 1390 1400
ATVALPKFEE PPSKGTTVCG ADVHEVGPGP SGLSEEQSRA FPTPYLRVPV
1410 1420 1430 1440 1450
TLPERKGTSL SSESILSLEG SSSTAGGSKR VLSPAGSLEL TMETQQQKRV
1460 1470 1480 1490 1500
KEEEASKADE KLELVKPCSV VLTSTEDGKR PEKSHLGNQG QGRRELEMLS
1510 1520 1530 1540 1550
SLSSDPSDTK EIPPLPHPAL SHGTAPGSEA LKEYPQPSGK PHRRGLTPLS
1560 1570 1580 1590 1600
VKKEDSKEQP DLPSLAPPSS LPLSETSSRP AKSQEGTDSK KVLQFPSLHT
1610 1620 1630 1640 1650
TTNVSWCYLN YIKPNHIQHA DRRSSVYAGW CISLYNPNLP GVSTKAALSL
1660 1670 1680 1690 1700
LRSKQKVSKE TYTMATAPHP EAGRLVPSSS RKPRMTEVHL PSLVSPEGQK
1710 1720 1730 1740 1750
DLARVEKEEE RRGEPEEDAP ASQRGEPARI KIFEGGYKSN EEYVYVRGRG
1760 1770 1780 1790 1800
RGKYVCEECG IRCKKPSMLK KHIRTHTDVR PYVCKHCHFA FKTKGNLTKH
1810 1820 1830 1840 1850
MKSKAHSKKC QETGVLEELE AEEGTSDDLF QDSEGREGSE AVEEHQFSDL
1860 1870 1880 1890 1900
EDSDSDSDLD EDEDEDEEES QDELSRPSSE APPPGPPHAL RADSSPILGP
1910 1920 1930 1940 1950
QPPDAPASGT EATRGSSVSE AERLTASSCS MSSQSMPGLP WLGPAPLGSV
1960 1970 1980 1990 2000
EKDTGSALSY KPVSPRRPWS PSKEAGSRPP LARKHSLTKN DSSPQRCSPA
2010 2020 2030 2040 2050
REPQASAPSP PGLHVDPGRG MGALPCGSPR LQLSPLTLCP LGRELAPRAH
2060 2070 2080 2090 2100
VLSKLEGTTD PGLPRYSPTR RWSPGQAESP PRSAPPGKWA LAGPGSPSAG
2110 2120 2130 2140 2150
EHGPGLGLDP RVLFPPAPLP HKLLSRSPET CASPWQKAES RSPSCSPGPA
2160 2170 2180 2190 2200
HPLSSRPFSA LHDFHGHILA RTEENIFSHL PLHSQHLTRA PCPLIPIGGI
2210 2220 2230 2240 2250
QMVQARPGAH PTLLPGPTAA WVSGFSGGGS DLTGAREAQE RGRWSPTESS
2260 2270 2280 2290 2300
SASVSPVAKV SKFTLSSELE GGDYPKERER TGGGPGRPPD WTPHGTGAPA
2310 2320 2330 2340 2350
EPTPTHSPCT PPDTLPRPPQ GRRAAQSWSP RLESPRAPTN PEPSATPPLD
2360 2370 2380 2390 2400
RSSSVGCLAE ASARFPARTR NLSGEPRTRQ DSPKPSGSGE PRAHPHQPED

RVPPNA
Length:2,406
Mass (Da):259,465
Last modified:December 21, 2004 - v1
Checksum:iAFCCFDAF87014A7D
GO
Isoform 2 (identifier: Q5T1R4-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     2136-2136: Missing.

Show »
Length:2,405
Mass (Da):259,336
Checksum:i2FC59B5BAB2DE97D
GO

Sequence cautioni

The sequence BAB13381.2 differs from that shown. Reason: Erroneous initiation.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti44 – 441A → P in AAK01082. (PubMed:11161801)Curated
Sequence conflicti94 – 952QL → HV in AAK01082. (PubMed:11161801)Curated
Sequence conflicti123 – 1231D → S in AAK01082. (PubMed:11161801)Curated
Sequence conflicti127 – 1271P → L in AAK01082. (PubMed:11161801)Curated
Sequence conflicti133 – 1342FV → LL in AAK01082. (PubMed:11161801)Curated
Sequence conflicti589 – 5891R → P in AAK01082. (PubMed:11161801)Curated
Sequence conflicti901 – 9011L → A in AAK01082. (PubMed:11161801)Curated
Sequence conflicti961 – 9611S → D in AAK01082. (PubMed:11161801)Curated
Sequence conflicti1034 – 10352RV → GE in AAK01082. (PubMed:11161801)Curated
Sequence conflicti1048 – 10492QA → SP in AAK01082. (PubMed:11161801)Curated
Sequence conflicti1110 – 11101P → A in AAK01082. (PubMed:11161801)Curated
Sequence conflicti1180 – 11801P → L in BAB13381. (PubMed:10997877)Curated
Sequence conflicti1180 – 11801P → L in AAI52564. (PubMed:15489334)Curated
Sequence conflicti1279 – 12791T → Q in AAK01082. (PubMed:11161801)Curated
Sequence conflicti1524 – 15241T → Q in AAK01082. (PubMed:11161801)Curated
Sequence conflicti2376 – 23761P → S in AAK01082. (PubMed:11161801)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti35 – 351V → I.
Corresponds to variant rs2146315 [ dbSNP | Ensembl ].
VAR_042910
Natural varianti484 – 4841V → M in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_042911
Natural varianti575 – 5751H → R.3 Publications
Corresponds to variant rs2810566 [ dbSNP | Ensembl ].
VAR_042912
Natural varianti1087 – 10871Q → H.
Corresponds to variant rs17363472 [ dbSNP | Ensembl ].
VAR_042913
Natural varianti2023 – 20231A → P.3 Publications
Corresponds to variant rs2483689 [ dbSNP | Ensembl ].
VAR_042914
Natural varianti2109 – 21091D → A.3 Publications
Corresponds to variant rs2991344 [ dbSNP | Ensembl ].
VAR_042915
Natural varianti2272 – 22721G → R.1 Publication
Corresponds to variant rs11809423 [ dbSNP | Ensembl ].
VAR_042916
Natural varianti2339 – 23391T → A.3 Publications
Corresponds to variant rs9439043 [ dbSNP | Ensembl ].
VAR_042917

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei2136 – 21361Missing in isoform 2. 2 PublicationsVSP_033279

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF278765 mRNA. Translation: AAK01082.1.
AB046775 mRNA. Translation: BAB13381.2. Different initiation.
AL445933 Genomic DNA. Translation: CAI14537.1.
AL445933 Genomic DNA. Translation: CAI14538.1.
BC152563 mRNA. Translation: AAI52564.1.
CCDSiCCDS44124.1. [Q5T1R4-2]
CCDS463.1. [Q5T1R4-1]
RefSeqiNP_001121186.1. NM_001127714.2. [Q5T1R4-2]
NP_078779.2. NM_024503.4. [Q5T1R4-1]
XP_006710871.1. XM_006710808.1. [Q5T1R4-1]
UniGeneiHs.403972.
Hs.648369.

Genome annotation databases

EnsembliENST00000247584; ENSP00000247584; ENSG00000127124. [Q5T1R4-1]
ENST00000372583; ENSP00000361664; ENSG00000127124. [Q5T1R4-1]
ENST00000372584; ENSP00000361665; ENSG00000127124. [Q5T1R4-2]
GeneIDi59269.
KEGGihsa:59269.
UCSCiuc001cgz.4. human. [Q5T1R4-1]
uc001cha.4. human. [Q5T1R4-2]

Polymorphism databases

DMDMi74756245.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF278765 mRNA. Translation: AAK01082.1 .
AB046775 mRNA. Translation: BAB13381.2 . Different initiation.
AL445933 Genomic DNA. Translation: CAI14537.1 .
AL445933 Genomic DNA. Translation: CAI14538.1 .
BC152563 mRNA. Translation: AAI52564.1 .
CCDSi CCDS44124.1. [Q5T1R4-2 ]
CCDS463.1. [Q5T1R4-1 ]
RefSeqi NP_001121186.1. NM_001127714.2. [Q5T1R4-2 ]
NP_078779.2. NM_024503.4. [Q5T1R4-1 ]
XP_006710871.1. XM_006710808.1. [Q5T1R4-1 ]
UniGenei Hs.403972.
Hs.648369.

3D structure databases

ProteinModelPortali Q5T1R4.
SMRi Q5T1R4. Positions 191-247, 1753-1809.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 121861. 6 interactions.
STRINGi 9606.ENSP00000247584.

PTM databases

PhosphoSitei Q5T1R4.

Polymorphism databases

DMDMi 74756245.

Proteomic databases

MaxQBi Q5T1R4.
PaxDbi Q5T1R4.
PRIDEi Q5T1R4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000247584 ; ENSP00000247584 ; ENSG00000127124 . [Q5T1R4-1 ]
ENST00000372583 ; ENSP00000361664 ; ENSG00000127124 . [Q5T1R4-1 ]
ENST00000372584 ; ENSP00000361665 ; ENSG00000127124 . [Q5T1R4-2 ]
GeneIDi 59269.
KEGGi hsa:59269.
UCSCi uc001cgz.4. human. [Q5T1R4-1 ]
uc001cha.4. human. [Q5T1R4-2 ]

Organism-specific databases

CTDi 59269.
GeneCardsi GC01M041985.
HGNCi HGNC:13561. HIVEP3.
HPAi HPA005728.
MIMi 606649. gene.
neXtProti NX_Q5T1R4.
PharmGKBi PA29299.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG296349.
GeneTreei ENSGT00530000063161.
HOGENOMi HOG000155774.
HOVERGENi HBG095595.
InParanoidi Q5T1R4.
KOi K09239.
OMAi MERIPGE.
OrthoDBi EOG7V1FPQ.
PhylomeDBi Q5T1R4.
TreeFami TF331837.

Miscellaneous databases

ChiTaRSi HIVEP3. human.
GeneWikii HIVEP3.
GenomeRNAii 59269.
NextBioi 65146.
PROi Q5T1R4.
SOURCEi Search...

Gene expression databases

Bgeei Q5T1R4.
CleanExi HS_HIVEP3.
Genevestigatori Q5T1R4.

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. 5 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Structure of the human zinc finger protein HIVEP3: molecular cloning, expression, exon-intron structure, and comparison with paralogous genes HIVEP1 and HIVEP2."
    Hicar M.D., Liu Y., Allen C.E., Wu L.-C.
    Genomics 71:89-100(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ALTERNATIVE SPLICING, DOMAIN, VARIANTS ARG-575; PRO-2023; ALA-2109; ARG-2272 AND ALA-2339.
    Tissue: Brain.
  2. "Prediction of the coding sequences of unidentified human genes. XVIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.
    DNA Res. 7:273-281(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANTS ARG-575; PRO-2023; ALA-2109 AND ALA-2339.
    Tissue: Brain.
  3. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
    Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
    DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  4. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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 2), VARIANTS ARG-575; PRO-2023; ALA-2109 AND ALA-2339.
  6. Cited for: VARIANT [LARGE SCALE ANALYSIS] MET-484.

Entry informationi

Entry nameiZEP3_HUMAN
AccessioniPrimary (citable) accession number: Q5T1R4
Secondary accession number(s): A7YY91
, Q5T1R5, Q9BZS0, Q9HCL7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: December 21, 2004
Last modified: October 29, 2014
This is version 104 of the entry and version 1 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 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3