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Protein

Transcription factor HIVEP3

Gene

HIVEP3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Zinc fingeri192 – 214C2H2-type 1PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri220 – 242C2H2-type 2PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri640 – 670CCHC HIVEP-typePROSITE-ProRule annotationAdd BLAST31
Zinc fingeri1754 – 1776C2H2-type 3PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri1782 – 1806C2H2-type 4PROSITE-ProRule annotationAdd BLAST25

GO - Molecular functioni

GO - Biological processi

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
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:13561. HIVEP3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi59269.
OpenTargetsiENSG00000127124.
PharmGKBiPA29299.

Polymorphism and mutation databases

BioMutaiHIVEP3.
DMDMi74756245.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003316271 – 2406Transcription factor HIVEP3Add BLAST2406

Post-translational modificationi

Phosphorylated on threonine and serine residues.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ5T1R4.
MaxQBiQ5T1R4.
PaxDbiQ5T1R4.
PeptideAtlasiQ5T1R4.
PRIDEiQ5T1R4.

PTM databases

iPTMnetiQ5T1R4.
PhosphoSitePlusiQ5T1R4.

Expressioni

Inductioni

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

Gene expression databases

BgeeiENSG00000127124.
CleanExiHS_HIVEP3.
GenevisibleiQ5T1R4. HS.

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. 8 interactors.
STRINGi9606.ENSP00000247584.

Structurei

3D structure databases

ProteinModelPortaliQ5T1R4.
SMRiQ5T1R4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati1964 – 196714
Repeati1970 – 197324
Repeati1993 – 199634
Repeati1998 – 200144
Repeati2067 – 207054
Repeati2079 – 208264

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni192 – 242ZAS1Add BLAST51
Regioni211 – 1074No DNA binding activity or transactivation activity, but complete prevention of TRAF-dependent NF-Kappa-B activation; associates with TRAF2 and JUNBy similarityAdd BLAST864
Regioni264 – 287Acidic 1Add BLAST24
Regioni862 – 883Acidic 2Add BLAST22
Regioni1754 – 1806ZAS2Add BLAST53
Regioni1817 – 1872Acidic 3Add BLAST56
Regioni2053 – 21486 X 4 AA tandem repeats of S-P-X-[RK]Add BLAST96

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili1442 – 1466Sequence analysisAdd BLAST25

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi903 – 909Nuclear localization signalSequence analysis7

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi308 – 334Ser-richAdd BLAST27
Compositional biasi378 – 414Ser-richAdd BLAST37
Compositional biasi797 – 819Ser-richAdd BLAST23
Compositional biasi844 – 880Glu/Pro-richAdd BLAST37
Compositional biasi916 – 948Ser-richAdd BLAST33
Compositional biasi1907 – 1936Ser-richAdd BLAST30

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 4 C2H2-type zinc fingers.PROSITE-ProRule annotation
Contains 1 CCHC HIVEP-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri192 – 214C2H2-type 1PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri220 – 242C2H2-type 2PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri640 – 670CCHC HIVEP-typePROSITE-ProRule annotationAdd BLAST31
Zinc fingeri1754 – 1776C2H2-type 3PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri1782 – 1806C2H2-type 4PROSITE-ProRule annotationAdd BLAST25

Keywords - Domaini

Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1721. Eukaryota.
COG5048. LUCA.
GeneTreeiENSGT00530000063161.
HOGENOMiHOG000155774.
HOVERGENiHBG095595.
InParanoidiQ5T1R4.
KOiK09239.
OMAiMERIPGE.
OrthoDBiEOG091G00EA.
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]
PROSITEiPS51811. ZF_CCHC_HIVEP. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 4 hits.
PS50157. ZINC_FINGER_C2H2_2. 4 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

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 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti44A → P in AAK01082 (PubMed:11161801).Curated1
Sequence conflicti94 – 95QL → HV in AAK01082 (PubMed:11161801).Curated2
Sequence conflicti123D → S in AAK01082 (PubMed:11161801).Curated1
Sequence conflicti127P → L in AAK01082 (PubMed:11161801).Curated1
Sequence conflicti133 – 134FV → LL in AAK01082 (PubMed:11161801).Curated2
Sequence conflicti589R → P in AAK01082 (PubMed:11161801).Curated1
Sequence conflicti901L → A in AAK01082 (PubMed:11161801).Curated1
Sequence conflicti961S → D in AAK01082 (PubMed:11161801).Curated1
Sequence conflicti1034 – 1035RV → GE in AAK01082 (PubMed:11161801).Curated2
Sequence conflicti1048 – 1049QA → SP in AAK01082 (PubMed:11161801).Curated2
Sequence conflicti1110P → A in AAK01082 (PubMed:11161801).Curated1
Sequence conflicti1180P → L in BAB13381 (PubMed:10997877).Curated1
Sequence conflicti1180P → L in AAI52564 (PubMed:15489334).Curated1
Sequence conflicti1279T → Q in AAK01082 (PubMed:11161801).Curated1
Sequence conflicti1524T → Q in AAK01082 (PubMed:11161801).Curated1
Sequence conflicti2376P → S in AAK01082 (PubMed:11161801).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04291035V → I.Corresponds to variant rs2146315dbSNPEnsembl.1
Natural variantiVAR_042911484V → M in a colorectal cancer sample; somatic mutation. 1 PublicationCorresponds to variant rs780211835dbSNPEnsembl.1
Natural variantiVAR_042912575H → R.3 PublicationsCorresponds to variant rs2810566dbSNPEnsembl.1
Natural variantiVAR_0429131087Q → H.Corresponds to variant rs17363472dbSNPEnsembl.1
Natural variantiVAR_0429142023A → P.3 PublicationsCorresponds to variant rs2483689dbSNPEnsembl.1
Natural variantiVAR_0429152109D → A.3 PublicationsCorresponds to variant rs2991344dbSNPEnsembl.1
Natural variantiVAR_0429162272G → R.1 PublicationCorresponds to variant rs11809423dbSNPEnsembl.1
Natural variantiVAR_0429172339T → A.3 PublicationsCorresponds to variant rs9439043dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0332792136Missing in isoform 2. 2 Publications1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_011540186.1. XM_011541884.2. [Q5T1R4-1]
XP_016857481.1. XM_017001992.1. [Q5T1R4-1]
XP_016857482.1. XM_017001993.1. [Q5T1R4-1]
XP_016857483.1. XM_017001994.1. [Q5T1R4-2]
UniGeneiHs.403972.
Hs.648369.

Genome annotation databases

EnsembliENST00000372583; ENSP00000361664; ENSG00000127124. [Q5T1R4-1]
ENST00000372584; ENSP00000361665; ENSG00000127124. [Q5T1R4-2]
GeneIDi59269.
KEGGihsa:59269.
UCSCiuc001cgz.5. human. [Q5T1R4-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_011540186.1. XM_011541884.2. [Q5T1R4-1]
XP_016857481.1. XM_017001992.1. [Q5T1R4-1]
XP_016857482.1. XM_017001993.1. [Q5T1R4-1]
XP_016857483.1. XM_017001994.1. [Q5T1R4-2]
UniGeneiHs.403972.
Hs.648369.

3D structure databases

ProteinModelPortaliQ5T1R4.
SMRiQ5T1R4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121861. 8 interactors.
STRINGi9606.ENSP00000247584.

PTM databases

iPTMnetiQ5T1R4.
PhosphoSitePlusiQ5T1R4.

Polymorphism and mutation databases

BioMutaiHIVEP3.
DMDMi74756245.

Proteomic databases

EPDiQ5T1R4.
MaxQBiQ5T1R4.
PaxDbiQ5T1R4.
PeptideAtlasiQ5T1R4.
PRIDEiQ5T1R4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000372583; ENSP00000361664; ENSG00000127124. [Q5T1R4-1]
ENST00000372584; ENSP00000361665; ENSG00000127124. [Q5T1R4-2]
GeneIDi59269.
KEGGihsa:59269.
UCSCiuc001cgz.5. human. [Q5T1R4-1]

Organism-specific databases

CTDi59269.
DisGeNETi59269.
GeneCardsiHIVEP3.
HGNCiHGNC:13561. HIVEP3.
HPAiHPA005728.
MIMi606649. gene.
neXtProtiNX_Q5T1R4.
OpenTargetsiENSG00000127124.
PharmGKBiPA29299.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1721. Eukaryota.
COG5048. LUCA.
GeneTreeiENSGT00530000063161.
HOGENOMiHOG000155774.
HOVERGENiHBG095595.
InParanoidiQ5T1R4.
KOiK09239.
OMAiMERIPGE.
OrthoDBiEOG091G00EA.
PhylomeDBiQ5T1R4.
TreeFamiTF331837.

Miscellaneous databases

ChiTaRSiHIVEP3. human.
GeneWikiiHIVEP3.
GenomeRNAii59269.
PROiQ5T1R4.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000127124.
CleanExiHS_HIVEP3.
GenevisibleiQ5T1R4. HS.

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]
PROSITEiPS51811. ZF_CCHC_HIVEP. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 4 hits.
PS50157. ZINC_FINGER_C2H2_2. 4 hits.
[Graphical view]
ProtoNetiSearch...

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: November 2, 2016
This is version 120 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

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.