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Q9H9Z2 (LN28A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein lin-28 homolog A

Short name=Lin-28A
Alternative name(s):
Zinc finger CCHC domain-containing protein 1
Gene names
Name:LIN28A
Synonyms:CSDD1, LIN28, ZCCHC1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length209 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts as a 'translational enhancer', driving specific mRNAs to polysomes and thus increasing the efficiency of protein synthesis. Its association with the translational machinery and target mRNAs results in an increased number of initiation events per molecule of mRNA and, indirectly, in stabilizing the mRNAs. Binds IGF2 mRNA, MYOD1 mRNA, ARBP/36B4 ribosomal protein mRNA and its own mRNA. Essential for skeletal muscle differentiation program through the translational up-regulation of IGF2 expression By similarity. Acts as a suppressor of microRNA (miRNA) biogenesis by specifically binding the precursor let-7 (pre-let-7), a miRNA precursor. Acts by binding pre-let-7 and recruiting ZCCHC11/TUT4 uridylyltransferase, leading to the terminal uridylation of pre-let-7. Uridylated pre-let-7 miRNAs fail to be processed by Dicer and undergo degradation. Degradation of pre-let-7 in embryonic stem (ES) cells contributes to the maintenance of ES cells. In contrast, LIN28A down-regulation in neural stem cells by miR-125, allows the processing of pre-let-7. Specifically recognizes the 5'-GGAG-3' motif in the terminal loop of pre-let-7. Also recognizes and binds non pre-let-7 pre-miRNAs that contain the 5'-GGAG-3' motif in the terminal loop, leading to their terminal uridylation and subsequent degradation. Ref.12 Ref.13

Subunit structure

Monomer. During skeletal muscle differentiation, associated with translation initiation complexes in the polysomal compartment. Directly interacts with EIF3S2. Interaction with NCL is RNA-dependent By similarity. Interacts with ZCCHC11/TUT4. Ref.13

Subcellular location

Cytoplasm. Nucleusnucleolus. Note: Nucleolar localization observed in 10-15% of the nuclei in differentiated myotubes By similarity. Shuttles between the cytoplasm and the nucleus. Localizes to cytoplasmic processing bodies and stress granules. Ref.11 Ref.12

Tissue specificity

Expressed in embryonic stem cells (ES cells), placenta and testis. Ref.7 Ref.8 Ref.9

Developmental stage

Expressed in fetal liver. Expression decreases during differentiation of ES cells or upon induction of neuronal differentiation by retinoic acid. Ref.7 Ref.8 Ref.9

Induction

Can be negatively regulated by the interaction of microRNAs miR-125a and miR-125b with at least two miRNA responsive elements (miREs) in the 3'-UTR of this gene. These interactions may reduce both translation efficiency and mRNA abundance. Negatively regulated by retinoic acid. Ref.6 Ref.10

Domain

The CSD domain is required for function in muscle differentiation By similarity.

The CCHC zinc fingers interact with the GGAG motif at the 3' end of let-7 miRNAs precursors, more generally they bind the 5'-NGNNG-3' consensus motif with micromolar affinity. The CSD domain recognizes the loop at the 5' end. The flexible linker allows accommodating variable sequences and lengths among let-7 family members.

Miscellaneous

Overexpressed in primary tumors (overall frequency approximately 15%), overexpression being linked to repression of let-7 family miRNAs and derepression of let-7 targets. Facilitates cellular transformation in vitro, and overexpression is associated with advanced disease across multiple tumor types.

Sequence similarities

Belongs to the lin-28 family.

Contains 2 CCHC-type zinc fingers.

Contains 1 CSD (cold-shock) domain.

Ontologies

Keywords
   Biological processRNA-mediated gene silencing
   Cellular componentCytoplasm
Nucleus
   DomainRepeat
Zinc-finger
   LigandMetal-binding
RNA-binding
Zinc
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRNA 3'-end processing

Inferred from mutant phenotype Ref.12Ref.13. Source: UniProtKB

germ cell development

Inferred from electronic annotation. Source: Ensembl

miRNA catabolic process

Inferred from mutant phenotype Ref.12Ref.13. Source: UniProtKB

negative regulation of glial cell differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of neuron differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of translation

Inferred from electronic annotation. Source: Ensembl

pre-miRNA processing

Inferred from mutant phenotype Ref.12Ref.13. Source: UniProtKB

regulation of gene silencing by miRNA

Inferred from electronic annotation. Source: Ensembl

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: InterPro

stem cell maintenance

Inferred from mutant phenotype Ref.13. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 18604195PubMed 20014101. Source: MGI

cytoplasmic mRNA processing body

Inferred from direct assay Ref.11. Source: UniProtKB

cytoplasmic stress granule

Inferred from direct assay Ref.11. Source: UniProtKB

nucleolus

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay Ref.11. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: InterPro

RNA binding

Inferred from direct assay Ref.12Ref.13. Source: UniProtKB

mRNA binding

Inferred from electronic annotation. Source: Ensembl

miRNA binding

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction Ref.13. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.15
Chain2 – 209208Protein lin-28 homolog A
PRO_0000253787

Regions

Domain39 – 11274CSD
Zinc finger137 – 15418CCHC-type 1
Zinc finger159 – 17618CCHC-type 2
Region113 – 13624Flexible linker

Amino acid modifications

Modified residue21N-acetylglycine Ref.15 Ref.16
Modified residue31Phosphoserine Ref.15
Modified residue1201Phosphoserine Ref.15
Modified residue2001Phosphoserine Ref.15

Experimental info

Mutagenesis461W → A: Does not affect localization to cytoplasmic processing bodies; when associated with A-55 and A-73. Ref.11
Mutagenesis551F → A: Does not affect localization to cytoplasmic processing bodies; when associated with A-46 and A-73. Ref.11
Mutagenesis731F → A: Does not affect localization to cytoplasmic processing bodies; when associated with A-46 and A-55. Ref.11
Mutagenesis1471H → A: Abolishes ability to suppress pre-let-7 biogenesis and localization to cytoplasmic processing bodies without affecting pre-let-7 binding; when associated with A-169. Ref.11 Ref.12
Mutagenesis1691H → A: Abolishes ability to suppress pre-let-7 biogenesis and localization to cytoplasmic processing bodies without affecting pre-let-7 binding; when associated with A-147. Ref.11 Ref.12

Secondary structure

............... 209
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9H9Z2 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: FA5EF6DD33FABF54

FASTA20922,743
        10         20         30         40         50         60 
MGSVSNQQFA GGCAKAAEEA PEEAPEDAAR AADEPQLLHG AGICKWFNVR MGFGFLSMTA 

        70         80         90        100        110        120 
RAGVALDPPV DVFVHQSKLH MEGFRSLKEG EAVEFTFKKS AKGLESIRVT GPGGVFCIGS 

       130        140        150        160        170        180 
ERRPKGKSMQ KRRSKGDRCY NCGGLDHHAK ECKLPPQPKK CHFCQSISHM VASCPLKAQQ 

       190        200 
GPSAQGKPTY FREEEEEIHS PTLLPEAQN 

« Hide

References

« Hide 'large scale' references
[1]"Conservation of the heterochronic regulator Lin-28, its developmental expression and microRNA complementary sites."
Moss E.G., Tang L.
Dev. Biol. 258:432-442(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]Erratum
Moss E.G., Tang L.
Dev. Biol. 262:361-361(2003)
[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. expand/collapse author list , 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].
Tissue: Teratocarcinoma.
[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. expand/collapse author list , 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].
Tissue: Placenta.
[6]"Expression profiling of mammalian microRNAs uncovers a subset of brain-expressed microRNAs with possible roles in murine and human neuronal differentiation."
Sempere L.F., Freemantle S., Pitha-Rowe I., Moss E.G., Dmitrovsky E., Ambros V.
Genome Biol. 5:R13.1-R13.11(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[7]"The transcriptome profile of human embryonic stem cells as defined by SAGE."
Richards M., Tan S.-P., Tan J.-H., Chan W.-K., Bongso A.
Stem Cells 22:51-64(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[8]"Vascular gene expression and phenotypic correlation during differentiation of human embryonic stem cells."
Gerecht-Nir S., Dazard J.-E., Golan-Mashiach M., Osenberg S., Botvinnik A., Amariglio N., Domany E., Rechavi G., Givol D., Itskovitz-Eldor J.
Dev. Dyn. 232:487-497(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[9]"Depletion of human micro-RNA miR-125b reveals that it is critical for the proliferation of differentiated cells but not for the down-regulation of putative targets during differentiation."
Lee Y.S., Kim H.K., Chung S., Kim K.-S., Dutta A.
J. Biol. Chem. 280:16635-16641(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[10]"Micro-RNA regulation of the mammalian lin-28 gene during neuronal differentiation of embryonal carcinoma cells."
Wu L., Belasco J.G.
Mol. Cell. Biol. 25:9198-9208(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[11]"Localization of the developmental timing regulator Lin28 to mRNP complexes, P-bodies and stress granules."
Balzer E., Moss E.G.
RNA Biol. 4:16-25(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF TRP-46; PHE-55; PHE-73; HIS-147 AND HIS-169.
[12]"Lin28 mediates the terminal uridylation of let-7 precursor MicroRNA."
Heo I., Joo C., Cho J., Ha M., Han J., Kim V.N.
Mol. Cell 32:276-284(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, RNA-BINDING, MUTAGENESIS OF HIS-147 AND HIS-169.
[13]"TUT4 in concert with Lin28 suppresses MicroRNA biogenesis through pre-microRNA uridylation."
Heo I., Joo C., Kim Y.-K., Ha M., Yoon M.-J., Cho J., Yeom K.-H., Han J., Kim V.N.
Cell 138:696-708(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, RNA-BINDING, INTERACTION WITH ZCCHC11.
[14]"Lin28 promotes transformation and is associated with advanced human malignancies."
Viswanathan S.R., Powers J.T., Einhorn W., Hoshida Y., Ng T.L., Toffanin S., O'Sullivan M., Lu J., Phillips L.A., Lockhart V.L., Shah S.P., Tanwar P.S., Mermel C.H., Beroukhim R., Azam M., Teixeira J., Meyerson M., Hughes T.P. expand/collapse author list , Llovet J.M., Radich J., Mullighan C.G., Golub T.R., Sorensen P.H., Daley G.Q.
Nat. Genet. 41:843-848(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: POSSIBLE INVOLVEMENT IN CANCERS.
[15]"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: ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; SER-120 AND SER-200, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[16]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"Solution structure of the zinc-finger domain in LIN-28."
RIKEN structural genomics initiative (RSGI)
Submitted (NOV-2005) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 134-186.
[18]"Structural basis of pre-let-7 miRNA recognition by the zinc knuckles of pluripotency factor Lin28."
Loughlin F.E., Gebert L.F., Towbin H., Brunschweiger A., Hall J., Allain F.H.
Nat. Struct. Mol. Biol. 19:84-89(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 124-186 IN COMPLEX WITH SHORT RNA, CONSENSUS MOTIF.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF521099 mRNA. Translation: AAM77751.1.
AK022519 mRNA. Translation: BAB14075.1.
AL513365 Genomic DNA. Translation: CAI21500.1.
BC028566 mRNA. Translation: AAH28566.1.
CCDSCCDS280.1.
RefSeqNP_078950.1. NM_024674.4.
XP_006710962.1. XM_006710899.1.
XP_006710963.1. XM_006710900.1.
UniGeneHs.86154.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CQFNMR-A137-186[»]
2LI8NMR-A124-186[»]
ProteinModelPortalQ9H9Z2.
SMRQ9H9Z2. Positions 34-186.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122842. 2 interactions.
IntActQ9H9Z2. 2 interactions.
STRING9606.ENSP00000254231.

PTM databases

PhosphoSiteQ9H9Z2.

Polymorphism databases

DMDM74752750.

Proteomic databases

PaxDbQ9H9Z2.
PRIDEQ9H9Z2.

Protocols and materials databases

DNASU79727.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000254231; ENSP00000254231; ENSG00000131914.
ENST00000326279; ENSP00000363314; ENSG00000131914.
GeneID79727.
KEGGhsa:79727.
UCSCuc001bmj.3. human.

Organism-specific databases

CTD79727.
GeneCardsGC01P026737.
HGNCHGNC:15986. LIN28A.
HPACAB020785.
MIM611043. gene.
neXtProtNX_Q9H9Z2.
PharmGKBPA165751523.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG244191.
HOGENOMHOG000047091.
HOVERGENHBG081922.
InParanoidQ9H9Z2.
OMASGICKWF.
OrthoDBEOG72JWJ8.
PhylomeDBQ9H9Z2.
TreeFamTF316240.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
SignaLinkQ9H9Z2.

Gene expression databases

BgeeQ9H9Z2.
CleanExHS_LIN28.
GenevestigatorQ9H9Z2.

Family and domain databases

Gene3D2.40.50.140. 1 hit.
4.10.60.10. 1 hit.
InterProIPR011129. Cold_shock_prot.
IPR002059. CSP_DNA-bd.
IPR012340. NA-bd_OB-fold.
IPR001878. Znf_CCHC.
[Graphical view]
PfamPF00313. CSD. 1 hit.
PF00098. zf-CCHC. 1 hit.
[Graphical view]
PRINTSPR00050. COLDSHOCK.
SMARTSM00357. CSP. 1 hit.
SM00343. ZnF_C2HC. 2 hits.
[Graphical view]
SUPFAMSSF50249. SSF50249. 1 hit.
SSF57756. SSF57756. 1 hit.
PROSITEPS50158. ZF_CCHC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9H9Z2.
GeneWikiLIN28.
GenomeRNAi79727.
NextBio69098.
PROQ9H9Z2.
SOURCESearch...

Entry information

Entry nameLN28A_HUMAN
AccessionPrimary (citable) accession number: Q9H9Z2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: March 1, 2001
Last modified: July 9, 2014
This is version 116 of the entry and version 1 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 chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM