SubmitCancel

Skip Header

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

Q9Y2X9

- ZN281_HUMAN

UniProt

Q9Y2X9 - ZN281_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 281

Gene
ZNF281, GZP1, ZBP99
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Transcription repressor that plays a role in regulation of embryonic stem cells (ESCs) differentiation. Required for ESCs differentiation and acts by mediating autorepression of NANOG in ESCs: binds to the NANOG promoter and promotes association of NANOG protein to its own promoter and recruits the NuRD complex, which deacetylates histones. Not required for establishement and maintenance of ESCs By similarity. Represses the transcription of a number of genes including GAST, ODC1 and VIM. Binds to the G-rich box in the enhancer region of these genes.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri261 – 28323C2H2-type 1Add
BLAST
Zinc fingeri289 – 31123C2H2-type 2Add
BLAST
Zinc fingeri317 – 33923C2H2-type 3Add
BLAST
Zinc fingeri345 – 36723C2H2-type 4; atypicalAdd
BLAST

GO - Molecular functioni

  1. core promoter binding Source: UniProtKB
  2. metal ion binding Source: UniProtKB-KW
  3. protein binding Source: UniProtKB
  4. sequence-specific DNA binding Source: UniProtKB
  5. sequence-specific DNA binding transcription factor activity Source: UniProtKB
  6. transcription corepressor activity Source: UniProtKB
  7. transcription regulatory region DNA binding Source: UniProtKB

GO - Biological processi

  1. embryonic body morphogenesis Source: UniProtKB
  2. negative regulation of gene expression Source: UniProtKB
  3. negative regulation of transcription, DNA-templated Source: UniProtKB
  4. positive regulation of transcription, DNA-templated Source: UniProtKB
  5. stem cell differentiation Source: UniProtKB
  6. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Differentiation, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Zinc finger protein 281
Alternative name(s):
GC-box-binding zinc finger protein 1
Transcription factor ZBP-99
Zinc finger DNA-binding protein 99
Gene namesi
Name:ZNF281
Synonyms:GZP1, ZBP99
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:13075. ZNF281.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA37651.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 895895Zinc finger protein 281PRO_0000047505Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei395 – 3951Phosphoserine1 Publication
Modified residuei484 – 4841Phosphoserine1 Publication
Modified residuei785 – 7851Phosphoserine1 Publication
Modified residuei807 – 8071Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9Y2X9.
PaxDbiQ9Y2X9.
PRIDEiQ9Y2X9.

PTM databases

PhosphoSiteiQ9Y2X9.

Expressioni

Gene expression databases

ArrayExpressiQ9Y2X9.
BgeeiQ9Y2X9.
CleanExiHS_ZNF281.
GenevestigatoriQ9Y2X9.

Organism-specific databases

HPAiHPA051228.

Interactioni

Protein-protein interaction databases

BioGridi117074. 20 interactions.
IntActiQ9Y2X9. 8 interactions.
STRINGi9606.ENSP00000294740.

Structurei

3D structure databases

ProteinModelPortaliQ9Y2X9.
SMRiQ9Y2X9. Positions 223-366.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi4 – 3734Gly-richAdd
BLAST
Compositional biasi90 – 967Poly-Pro
Compositional biasi141 – 1488Poly-His

Sequence similaritiesi

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri261 – 28323C2H2-type 1Add
BLAST
Zinc fingeri289 – 31123C2H2-type 2Add
BLAST
Zinc fingeri317 – 33923C2H2-type 3Add
BLAST
Zinc fingeri345 – 36723C2H2-type 4; atypicalAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG5048.
HOGENOMiHOG000293204.
HOVERGENiHBG055321.
InParanoidiQ9Y2X9.
OMAiQKDIEPR.
OrthoDBiEOG7VDXNJ.
PhylomeDBiQ9Y2X9.
TreeFamiTF331779.

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. 4 hits.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 3 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. Align

Isoform 1 (identifier: Q9Y2X9-1) [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

MKIGSGFLSG GGGTGSSGGS GSGGGGSGGG GGGGSSGRRA EMEPTFPQGM    50
VMFNHRLPPV TSFTRPAGSA APPPQCVLSS STSAAPAAEP PPPPAPDMTF 100
KKEPAASAAA FPSQRTSWGF LQSLVSIKQE KPADPEEQQS HHHHHHHHYG 150
GLFAGAEERS PGLGGGEGGS HGVIQDLSIL HQHVQQQPAQ HHRDVLLSSS 200
SRTDDHHGTE EPKQDTNVKK AKRPKPESQG IKAKRKPSAS SKPSLVGDGE 250
GAILSPSQKP HICDHCSAAF RSSYHLRRHV LIHTGERPFQ CSQCSMGFIQ 300
KYLLQRHEKI HSREKPFGCD QCSMKFIQKY HMERHKRTHS GEKPYKCDTC 350
QQYFSRTDRL LKHRRTCGEV IVKGATSAEP GSSNHTNMGN LAVLSQGNTS 400
SSRRKTKSKS IAIENKEQKT GKTNESQISN NINMQSYSVE MPTVSSSGGI 450
IGTGIDELQK RVPKLIFKKG SRKNTDKNYL NFVSPLPDIV GQKSLSGKPS 500
GSLGIVSNNS VETIGLLQST SGKQGQISSN YDDAMQFSKK RRYLPTASSN 550
SAFSINVGHM VSQQSVIQSA GVSVLDNEAP LSLIDSSALN AEIKSCHDKS 600
GIPDEVLQSI LDQYSNKSES QKEDPFNIAE PRVDLHTSGE HSELVQEENL 650
SPGTQTPSND KASMLQEYSK YLQQAFEKST NASFTLGHGF QFVSLSSPLH 700
NHTLFPEKQI YTTSPLECGF GQSVTSVLPS SLPKPPFGML FGSQPGLYLS 750
ALDATHQQLT PSQELDDLID SQKNLETSSA FQSSSQKLTS QKEQKNLESS 800
TGFQIPSQEL ASQIDPQKDI EPRTTYQIEN FAQAFGSQFK SGSRVPMTFI 850
TNSNGEVDHR VRTSVSDFSG YTNMMSDVSE PCSTRVKTPT SQSYR 895
Length:895
Mass (Da):96,915
Last modified:November 1, 1999 - v1
Checksum:i556FAAEA8D095FB7
GO
Isoform 2 (identifier: Q9Y2X9-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     49-84: Missing.

Note: Gene prediction based on EST data.

Show »
Length:859
Mass (Da):93,232
Checksum:i180A44DE154DD4FD
GO

Sequence cautioni

The sequence CAB70967.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti527 – 5271I → T in a breast cancer sample; somatic mutation. 1 Publication
VAR_035576

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei49 – 8436Missing in isoform 2. VSP_054815Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti63 – 631F → L in BAG51134. 1 Publication
Sequence conflicti206 – 2061H → Y in AAH51905. 1 Publication
Sequence conflicti482 – 4821F → L in BAG51134. 1 Publication
Sequence conflicti635 – 6351L → I in BAG51134. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF125158 mRNA. Translation: AAD21084.1.
AJ132591 mRNA. Translation: CAB70967.1. Different initiation.
AJ132592 mRNA. Translation: CAB70968.1.
AK022916 mRNA. Translation: BAG51134.1.
AC104461 Genomic DNA. No translation available.
BC051905 mRNA. Translation: AAH51905.1.
BC060820 mRNA. Translation: AAH60820.1.
CCDSiCCDS1402.1. [Q9Y2X9-1]
CCDS60384.1. [Q9Y2X9-2]
PIRiJC7089.
RefSeqiNP_001268222.1. NM_001281293.1. [Q9Y2X9-1]
NP_001268223.1. NM_001281294.1. [Q9Y2X9-2]
NP_036614.1. NM_012482.4. [Q9Y2X9-1]
UniGeneiHs.59757.
Hs.703449.
Hs.735801.

Genome annotation databases

EnsembliENST00000294740; ENSP00000294740; ENSG00000162702.
ENST00000367352; ENSP00000356321; ENSG00000162702.
ENST00000367353; ENSP00000356322; ENSG00000162702.
GeneIDi23528.
KEGGihsa:23528.
UCSCiuc001gve.3. human. [Q9Y2X9-1]

Polymorphism databases

DMDMi13124664.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF125158 mRNA. Translation: AAD21084.1 .
AJ132591 mRNA. Translation: CAB70967.1 . Different initiation.
AJ132592 mRNA. Translation: CAB70968.1 .
AK022916 mRNA. Translation: BAG51134.1 .
AC104461 Genomic DNA. No translation available.
BC051905 mRNA. Translation: AAH51905.1 .
BC060820 mRNA. Translation: AAH60820.1 .
CCDSi CCDS1402.1. [Q9Y2X9-1 ]
CCDS60384.1. [Q9Y2X9-2 ]
PIRi JC7089.
RefSeqi NP_001268222.1. NM_001281293.1. [Q9Y2X9-1 ]
NP_001268223.1. NM_001281294.1. [Q9Y2X9-2 ]
NP_036614.1. NM_012482.4. [Q9Y2X9-1 ]
UniGenei Hs.59757.
Hs.703449.
Hs.735801.

3D structure databases

ProteinModelPortali Q9Y2X9.
SMRi Q9Y2X9. Positions 223-366.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 117074. 20 interactions.
IntActi Q9Y2X9. 8 interactions.
STRINGi 9606.ENSP00000294740.

PTM databases

PhosphoSitei Q9Y2X9.

Polymorphism databases

DMDMi 13124664.

Proteomic databases

MaxQBi Q9Y2X9.
PaxDbi Q9Y2X9.
PRIDEi Q9Y2X9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000294740 ; ENSP00000294740 ; ENSG00000162702 .
ENST00000367352 ; ENSP00000356321 ; ENSG00000162702 .
ENST00000367353 ; ENSP00000356322 ; ENSG00000162702 .
GeneIDi 23528.
KEGGi hsa:23528.
UCSCi uc001gve.3. human. [Q9Y2X9-1 ]

Organism-specific databases

CTDi 23528.
GeneCardsi GC01M200375.
HGNCi HGNC:13075. ZNF281.
HPAi HPA051228.
neXtProti NX_Q9Y2X9.
PharmGKBi PA37651.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5048.
HOGENOMi HOG000293204.
HOVERGENi HBG055321.
InParanoidi Q9Y2X9.
OMAi QKDIEPR.
OrthoDBi EOG7VDXNJ.
PhylomeDBi Q9Y2X9.
TreeFami TF331779.

Miscellaneous databases

GeneWikii ZNF281.
GenomeRNAii 23528.
NextBioi 35462517.
PROi Q9Y2X9.

Gene expression databases

ArrayExpressi Q9Y2X9.
Bgeei Q9Y2X9.
CleanExi HS_ZNF281.
Genevestigatori Q9Y2X9.

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. 4 hits.
[Graphical view ]
PROSITEi PS00028. ZINC_FINGER_C2H2_1. 3 hits.
PS50157. ZINC_FINGER_C2H2_2. 4 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "ZBP-99 defines a conserved family of transcription factors and regulates ornithine decarboxylase gene expression."
    Law D.J., Du M., Law G.L., Merchant J.L.
    Biochem. Biophys. Res. Commun. 262:113-120(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION.
  2. "Identification of human GC-box-binding zinc finger protein, a new Krueppel-like zinc finger protein, by the yeast one-hybrid screening with a GC-rich target sequence."
    Lisowsky T., Loguercio Polosa P., Sagliano A., Roberti M., Gadaleta M.N., Cantatore P.
    FEBS Lett. 453:369-374(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Liver.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  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 1).
    Tissue: Placenta and Skin.
  6. "ZBP-89 represses vimentin gene transcription by interacting with the transcriptional activator, Sp1."
    Zhang X., Diab I.H., Zehner Z.E.
    Nucleic Acids Res. 31:2900-2914(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-395; SER-785 AND SER-807, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  8. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-484, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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].
  11. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: VARIANT [LARGE SCALE ANALYSIS] THR-527.

Entry informationi

Entry nameiZN281_HUMAN
AccessioniPrimary (citable) accession number: Q9Y2X9
Secondary accession number(s): A6NF48
, B3KMX2, Q5RKW5, Q9NY92
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: November 1, 1999
Last modified: September 3, 2014
This is version 127 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi