Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q5VUA4

- ZN318_HUMAN

UniProt

Q5VUA4 - ZN318_HUMAN

(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)

Protein

Zinc finger protein 318

Gene

ZNF318

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

Functioni

Repressed AR-mediated transcriptional activation. May act as a transcriptional regulator during spermatogenesis and, in particular, during meiotic division By similarity.By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1063 – 109735Matrin-type 1Add
BLAST
Zinc fingeri1136 – 116631Matrin-type 2Add
BLAST

GO - Molecular functioni

  1. nucleic acid binding Source: InterPro
  2. zinc ion binding Source: InterPro

GO - Biological processi

  1. meiotic nuclear division Source: UniProtKB-KW
  2. regulation of transcription, DNA-templated Source: UniProtKB-KW
  3. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Meiosis, Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Zinc finger protein 318
Alternative name(s):
Endocrine regulatory protein
Gene namesi
Name:ZNF318
ORF Names:HRIHFB2436
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:13578. ZNF318.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134923137.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 22792279Zinc finger protein 318PRO_0000191807Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei79 – 791Phosphoserine1 Publication
Modified residuei81 – 811Phosphoserine1 Publication
Modified residuei136 – 1361Phosphoserine2 Publications
Modified residuei173 – 1731Phosphoserine2 Publications
Modified residuei214 – 2141Phosphoserine2 Publications
Modified residuei464 – 4641Phosphoserine1 Publication
Modified residuei527 – 5271Phosphoserine2 Publications
Modified residuei1037 – 10371Phosphoserine1 Publication
Modified residuei1243 – 12431Phosphoserine3 Publications
Modified residuei1420 – 14201Phosphoserine1 Publication
Modified residuei1713 – 17131Phosphoserine1 Publication
Modified residuei1896 – 18961Phosphoserine2 Publications
Modified residuei2101 – 21011Phosphoserine2 Publications
Modified residuei2189 – 21891Phosphoserine1 Publication
Modified residuei2192 – 21921Phosphoserine1 Publication
Modified residuei2243 – 22431Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ5VUA4.
PaxDbiQ5VUA4.
PRIDEiQ5VUA4.

PTM databases

PhosphoSiteiQ5VUA4.

Expressioni

Tissue specificityi

Expressed in endocrine tissue.1 Publication

Gene expression databases

BgeeiQ5VUA4.
CleanExiHS_ZNF318.
GenevestigatoriQ5VUA4.

Organism-specific databases

HPAiHPA027022.
HPA027031.

Interactioni

Subunit structurei

Interacts with the N-terminal domain of AR.By similarity

Protein-protein interaction databases

BioGridi117299. 16 interactions.
IntActiQ5VUA4. 2 interactions.
STRINGi9606.ENSP00000354964.

Structurei

3D structure databases

ProteinModelPortaliQ5VUA4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili315 – 34329Sequence AnalysisAdd
BLAST
Coiled coili876 – 980105Sequence AnalysisAdd
BLAST
Coiled coili1768 – 179225Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi41 – 10363Pro-richAdd
BLAST
Compositional biasi1201 – 1327127Lys-richAdd
BLAST
Compositional biasi1433 – 1541109Pro-richAdd
BLAST

Sequence similaritiesi

Contains 2 matrin-type zinc fingers.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1063 – 109735Matrin-type 1Add
BLAST
Zinc fingeri1136 – 116631Matrin-type 2Add
BLAST

Keywords - Domaini

Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG87509.
GeneTreeiENSGT00390000000614.
HOGENOMiHOG000043103.
HOVERGENiHBG107139.
InParanoidiQ5VUA4.
OMAiQTKIRPN.
OrthoDBiEOG71P298.
PhylomeDBiQ5VUA4.
TreeFamiTF350583.

Family and domain databases

InterProiIPR015880. Znf_C2H2-like.
IPR003604. Znf_U1.
[Graphical view]
SMARTiSM00355. ZnF_C2H2. 2 hits.
SM00451. ZnF_U1. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q5VUA4-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MYRSSARSSV SSHRPKDDGG GGPRSGRSSG SSSGPARRSS PPPPPSGSSS
60 70 80 90 100
RTPARRPRSP SGHRGRRASP SPPRGRRVSP SPPRARRGSP SPPRGRRLFP
110 120 130 140 150
PGPAGFRGSS RGESRADYAR DGRGDHPGDS GSRRRSPGLC SDSLEKSLRI
160 170 180 190 200
TVGNDHFCVS TPERRRLSDR LGSPVDNLED MDRDDLTDDS VFTRSSQCSR
210 220 230 240 250
GLERYISQEE GPLSPFLGQL DEDYRTKETF LHRSDYSPHI SCHDELLRGT
260 270 280 290 300
ERNREKLKGY SIRSEERSRE AKRPRYDDTV KINSMGGDHP SFTSGTRNYR
310 320 330 340 350
QRRRSPSPRF LDPEFRELDL ARRKREEEEE RSRSLSQELV GVDGGGTGCS
360 370 380 390 400
IPGLSGVLTA SEPGYSLHRP EEVSVMPKKS ILKKRIEVDI MEPSMQLESF
410 420 430 440 450
SSSTSSSQDH PLYSGHPSLP LSGAIAAFAS EIENKGTMVE TALKEPQGNL
460 470 480 490 500
YQWGPLPGIP KDNSPLREKF GSFLCHKDNL DLKAEGPERH TDFLLPHERA
510 520 530 540 550
SQDGSGFSRI LSMLADSTST QEKRRRSFPD IEDEEKFLYG DEEEDLKAES
560 570 580 590 600
VPKPLGSSES EVMRQKASSL PSSAPAVKLE SLEETNPEYA KIHDLLKTIG
610 620 630 640 650
LDIGVAEISQ LAARTQERLH GKKPSLRSSA DRRSSVDRYF SADHCSSVDH
660 670 680 690 700
RFSADRCSSV DHCFSADRRS SDPHRLESRE AHHSNTHSPE VSHPHPPSPV
710 720 730 740 750
DPYLLTKNSP PFLKSDHPVG HISGPEVVGS GFQSSVAVRC MLPSAPSAPI
760 770 780 790 800
RLPHTAALSQ FHMPRASQFA AARIPPNYQG PAIPPASFDA YRHYMAYAAS
810 820 830 840 850
RWPMYPTSQP SNHPVPEPHR IMPITKQATR SRPNLRVIPT VTPDKPKQKE
860 870 880 890 900
SLRGSIPAAQ VPVQVSIPSL IRYNPEKISD EKNRASQKQK VIEEREKLKN
910 920 930 940 950
DREARQKKMY YLRTELERLH KQQGEMLRKK RREKDGHKDP LLVEVSRLQD
960 970 980 990 1000
NIMKDIAELR QEAEEAEKKQ SELDKVAQIL GINIFDKSQK SLSDSREPTE
1010 1020 1030 1040 1050
KPGKAEKSKS PEKVSSFSNS SSNKESKVNN EKFRTKSPKP AESPQSATKQ
1060 1070 1080 1090 1100
LDQPTAAYEY YDAGNHWCKD CNTICGTMFD FFTHMHNKKH TQTLDPYNRP
1110 1120 1130 1140 1150
WASKTQSEAK QDAIKRTDKI TVPAKGSEFL VPISGFYCQL CEEFLGDPIS
1160 1170 1180 1190 1200
GEQHVKGHQH NEKYKKYVDE NPLYEERRNL DRQAGLAVVL ETERRRQSEL
1210 1220 1230 1240 1250
KRKLSEKPKE EKKEKKAKAV KEVKEDDKVS EKLEDQLSEG RNSPEKAENK
1260 1270 1280 1290 1300
RNTGIKLQLK EEVKKESPTS SSFGKFSWKK PEKEEEKSSL VTPSISKEEI
1310 1320 1330 1340 1350
LESSKDKEDG KTEAGKAKPI KIKLSGKTVV AHTSPWMPVV TTSTQTKIRP
1360 1370 1380 1390 1400
NLPIPSTVLR KSCSATMSKP APLNTFLSIK SSGTTAKPLP VVKESSADLL
1410 1420 1430 1440 1450
LPPDIISKAF GGEEVILKGS PEEKVVLAEK SEPSHLPEQI LPPPPPPPPP
1460 1470 1480 1490 1500
PPPPPPVIPH PAAPSAAQAN AILAPVKSNP VVSQTLSPGF VGPNILNPVL
1510 1520 1530 1540 1550
PVAIMASAQP AAIPSDETAP GVSESDRDQT LFSVLVRPPP PLSSVFSEQA
1560 1570 1580 1590 1600
KKLEKRNSCL ATANAKDLYD IFYSSGGKGA PETKGAPETK LSGGPLANGE
1610 1620 1630 1640 1650
NSNLSRTKSS DTSSTSPLNS SASQEELHQD EGLVAAPIVS NSEKPIAKTL
1660 1670 1680 1690 1700
VALGKWSVVE HVGPKSTGST YGFLQPLTRL CQSRPYETIT PKTDTLAIWT
1710 1720 1730 1740 1750
SSSFQSDTSR DISPEKSELD LGEPGPPGVE PPPQLLDIQC KESQKLVEIH
1760 1770 1780 1790 1800
LRESVNQDKE SQELRKSEDC RESEIETNTE LKERVKELSE GIVDEGVSTS
1810 1820 1830 1840 1850
IGPHSIDDSN LNHGNRYMWE GEVKQPNLLM IDKEAEQSNK LMTGSETPSK
1860 1870 1880 1890 1900
VVIKLSPQAC SFTKAKLDSF LSEARSLLNP QDTPVKISAP ELLLHSPARS
1910 1920 1930 1940 1950
AMCLTGSPQE QGVSVVSEEG LENSAPESAS RTSRYRSLKL KRERSKDFQV
1960 1970 1980 1990 2000
KKIYELAVWD ENKKRPETWE SPEKPKTEAL ELQDVHPELT VTIESKALED
2010 2020 2030 2040 2050
FEATDLKVEE LTALGNLGDM PVDFCTTRVS PAHRSPTVLC QKVCEENSVS
2060 2070 2080 2090 2100
PIGCNSSDPA DFEPIPSFSG FPLDSPKTLV LDFETEGERN SPNPRSVRIP
2110 2120 2130 2140 2150
SPNILKTGLT ENVDRGLGGL EGTHQALDLL AGGMMPEEVK ESSQLDKQES
2160 2170 2180 2190 2200
LGLELKTINS AGLGPSPCLP DLVDFVTRTS GVQKDKLCSP LSEPGDPSKC
2210 2220 2230 2240 2250
SSLELGPLQL EISNASTTEV AILQVDDDSG DPLNLVKAPV SRSPPREQVI
2260 2270
EDNMVPQGMP EQETTVGAIQ DHTESSVHN
Length:2,279
Mass (Da):251,112
Last modified:January 15, 2008 - v2
Checksum:iCC8F7D54710E2450
GO
Isoform 2 (identifier: Q5VUA4-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1093-1117: TLDPYNRPWASKTQSEAKQDAIKRT → GQFQKSSDFQKEGLQQTFLPPERQG
     1118-2279: Missing.

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Show »
Length:1,117
Mass (Da):124,880
Checksum:i65866465A953CF07
GO

Sequence cautioni

The sequence AAH98434.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence starting in position 1214.
The sequence AAD47387.1 differs from that shown. Reason: Frameshift at positions 4 and 44.
The sequence AAD17298.1 differs from that shown. Reason: Erroneous initiation.
The sequence AAH98434.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti62 – 621G → R in AAD47387. 1 PublicationCurated
Sequence conflicti75 – 751G → V in AAD47387. 1 PublicationCurated
Sequence conflicti75 – 751G → V in AAD17298. 1 PublicationCurated
Sequence conflicti1034 – 10352RT → CI in AAD47387. 1 PublicationCurated
Sequence conflicti1034 – 10352RT → CI in AAD17298. 1 PublicationCurated
Sequence conflicti1259 – 12591L → F in AAD47387. 1 PublicationCurated
Sequence conflicti1259 – 12591L → F in AAD17298. 1 PublicationCurated
Sequence conflicti1349 – 13491R → G in AAD47387. 1 PublicationCurated
Sequence conflicti1349 – 13491R → G in AAD17298. 1 PublicationCurated
Sequence conflicti2160 – 21601S → F in AAD47387. 1 PublicationCurated
Sequence conflicti2160 – 21601S → F in AAD17298. 1 PublicationCurated
Sequence conflicti2173 – 21731V → D in BAA34799. (PubMed:9853615)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti407 – 4071S → I.
Corresponds to variant rs34541323 [ dbSNP | Ensembl ].
VAR_053759
Natural varianti812 – 8121N → S in a breast cancer sample; somatic mutation. 1 Publication
VAR_036056
Natural varianti870 – 8701L → V.
Corresponds to variant rs9357410 [ dbSNP | Ensembl ].
VAR_053760
Natural varianti1274 – 12741G → R in a breast cancer sample; somatic mutation. 1 Publication
VAR_036057
Natural varianti1292 – 12921T → I.
Corresponds to variant rs10948072 [ dbSNP | Ensembl ].
VAR_053761
Natural varianti1580 – 15801A → T.
Corresponds to variant rs3734684 [ dbSNP | Ensembl ].
VAR_053762
Natural varianti1583 – 15831T → I.
Corresponds to variant rs36107018 [ dbSNP | Ensembl ].
VAR_053763
Natural varianti1797 – 17971V → A.1 Publication
Corresponds to variant rs1459675 [ dbSNP | Ensembl ].
VAR_053764

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1093 – 111725TLDPY…AIKRT → GQFQKSSDFQKEGLQQTFLP PERQG in isoform 2. 1 PublicationVSP_016592Add
BLAST
Alternative sequencei1118 – 22791162Missing in isoform 2. 1 PublicationVSP_016593Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF090114 mRNA. Translation: AAD47387.1. Frameshift.
AF121141 mRNA. Translation: AAD17298.1. Different initiation.
AL590383, AL583834 Genomic DNA. Translation: CAH71374.2.
AL583834, AL590383 Genomic DNA. Translation: CAI14459.2.
BC030687 mRNA. No translation available.
BC098434 mRNA. Translation: AAH98434.1. Sequence problems.
AB015342 mRNA. Translation: BAA34799.1.
CCDSiCCDS4895.2. [Q5VUA4-1]
RefSeqiNP_055160.2. NM_014345.2. [Q5VUA4-1]
UniGeneiHs.509718.

Genome annotation databases

EnsembliENST00000361428; ENSP00000354964; ENSG00000171467. [Q5VUA4-1]
ENST00000605935; ENSP00000475748; ENSG00000171467. [Q5VUA4-2]
GeneIDi24149.
KEGGihsa:24149.
UCSCiuc003oux.3. human. [Q5VUA4-1]

Polymorphism databases

DMDMi166215018.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF090114 mRNA. Translation: AAD47387.1 . Frameshift.
AF121141 mRNA. Translation: AAD17298.1 . Different initiation.
AL590383 , AL583834 Genomic DNA. Translation: CAH71374.2 .
AL583834 , AL590383 Genomic DNA. Translation: CAI14459.2 .
BC030687 mRNA. No translation available.
BC098434 mRNA. Translation: AAH98434.1 . Sequence problems.
AB015342 mRNA. Translation: BAA34799.1 .
CCDSi CCDS4895.2. [Q5VUA4-1 ]
RefSeqi NP_055160.2. NM_014345.2. [Q5VUA4-1 ]
UniGenei Hs.509718.

3D structure databases

ProteinModelPortali Q5VUA4.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 117299. 16 interactions.
IntActi Q5VUA4. 2 interactions.
STRINGi 9606.ENSP00000354964.

PTM databases

PhosphoSitei Q5VUA4.

Polymorphism databases

DMDMi 166215018.

Proteomic databases

MaxQBi Q5VUA4.
PaxDbi Q5VUA4.
PRIDEi Q5VUA4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000361428 ; ENSP00000354964 ; ENSG00000171467 . [Q5VUA4-1 ]
ENST00000605935 ; ENSP00000475748 ; ENSG00000171467 . [Q5VUA4-2 ]
GeneIDi 24149.
KEGGi hsa:24149.
UCSCi uc003oux.3. human. [Q5VUA4-1 ]

Organism-specific databases

CTDi 24149.
GeneCardsi GC06M043346.
HGNCi HGNC:13578. ZNF318.
HPAi HPA027022.
HPA027031.
neXtProti NX_Q5VUA4.
PharmGKBi PA134923137.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG87509.
GeneTreei ENSGT00390000000614.
HOGENOMi HOG000043103.
HOVERGENi HBG107139.
InParanoidi Q5VUA4.
OMAi QTKIRPN.
OrthoDBi EOG71P298.
PhylomeDBi Q5VUA4.
TreeFami TF350583.

Miscellaneous databases

ChiTaRSi ZNF318. human.
GeneWikii ZNF318.
GenomeRNAii 24149.
NextBioi 46851.
PROi Q5VUA4.

Gene expression databases

Bgeei Q5VUA4.
CleanExi HS_ZNF318.
Genevestigatori Q5VUA4.

Family and domain databases

InterProi IPR015880. Znf_C2H2-like.
IPR003604. Znf_U1.
[Graphical view ]
SMARTi SM00355. ZnF_C2H2. 2 hits.
SM00451. ZnF_U1. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A novel cDNA expressed in endocrine tissue."
    Lopez-Egido J.R., Oberg K., Gobl A.E.
    Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, VARIANT ALA-1797.
  2. "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].
  3. "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), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1213 (ISOFORM 1).
    Tissue: Lymph and Testis.
  4. "Selection system for genes encoding nuclear-targeted proteins."
    Ueki N., Oda T., Kondo M., Yano K., Noguchi T., Muramatsu M.-A.
    Nat. Biotechnol. 16:1338-1342(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2056-2279 (ISOFORM 1), SUBCELLULAR LOCATION.
    Tissue: Fetal brain.
  5. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1243, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136; SER-173; SER-214; SER-1896; SER-2189; SER-2192 AND SER-2243, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "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].
  9. "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-173; SER-214 AND SER-1713, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  10. "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-464; SER-527; SER-1243; SER-1420; SER-1896; SER-2101 AND SER-2243, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79; SER-81; SER-136; SER-527; SER-1037; SER-1243 AND SER-2101, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: VARIANTS [LARGE SCALE ANALYSIS] SER-812 AND ARG-1274.

Entry informationi

Entry nameiZN318_HUMAN
AccessioniPrimary (citable) accession number: Q5VUA4
Secondary accession number(s): O94796
, Q4G0E4, Q8NEM6, Q9UNU8, Q9Y2W9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: January 15, 2008
Last modified: October 29, 2014
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3