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P31947 (1433S_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 153. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
14-3-3 protein sigma
Alternative name(s):
Epithelial cell marker protein 1
Stratifin
Gene names
Name:SFN
Synonyms:HME1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length248 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. When bound to KRT17, regulates protein synthesis and epithelial cell growth by stimulating Akt/mTOR pathway. May also regulate MDM2 autoubiquitination and degradation and thereby activate p53/TP53. Ref.10

p53-regulated inhibitor of G2/M progression. Ref.10

Subunit structure

Homodimer. Interacts with KRT17 and SAMSN1 By similarity. Found in a complex with XPO7, EIF4A1, ARHGAP1, VPS26A, VPS29, VPS35 and SFN. Interacts with GAB2. Interacts with SRPK2. Interacts with COPS6. Interacts with RFWD2; this interaction leads to proteasomal degradation. Ref.8 Ref.11 Ref.14 Ref.17

Subcellular location

Cytoplasm. Nucleus By similarity. Secreted. Note: May be secreted by a non-classical secretory pathway.

Tissue specificity

Present mainly in tissues enriched in stratified squamous keratinizing epithelium.

Post-translational modification

Ubiquitinated. Ubiquitination by RFFL induces proteasomal degradation and indirectly regulates p53/TP53 activation. Ref.10

Sequence similarities

Belongs to the 14-3-3 family.

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   PTMPhosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic process

Traceable author statement. Source: Reactome

establishment of skin barrier

Inferred from sequence or structural similarity. Source: UniProtKB

intrinsic apoptotic signaling pathway

Traceable author statement. Source: Reactome

intrinsic apoptotic signaling pathway in response to DNA damage

Inferred from direct assay PubMed 11574543. Source: HGNC

keratinocyte differentiation

Inferred from electronic annotation. Source: Ensembl

keratinocyte proliferation

Inferred from electronic annotation. Source: Ensembl

membrane organization

Traceable author statement. Source: Reactome

negative regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from direct assay PubMed 11574543. Source: HGNC

negative regulation of protein kinase activity

Traceable author statement Ref.2. Source: ProtInc

negative regulation of protein serine/threonine kinase activity

Traceable author statement Ref.2. Source: GOC

positive regulation of cell growth

Inferred from electronic annotation. Source: Ensembl

positive regulation of epidermal cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of protein export from nucleus

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway

Traceable author statement. Source: Reactome

regulation of cyclin-dependent protein serine/threonine kinase activity

Inferred from electronic annotation. Source: Ensembl

regulation of epidermal cell division

Inferred from sequence or structural similarity. Source: UniProtKB

release of cytochrome c from mitochondria

Inferred from direct assay PubMed 11574543. Source: HGNC

signal transduction

Traceable author statement Ref.2. Source: ProtInc

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

cytoplasmic vesicle membrane

Traceable author statement. Source: Reactome

cytosol

Traceable author statement. Source: Reactome

extracellular space

Traceable author statement Ref.2. Source: ProtInc

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 11574543Ref.11. Source: UniProtKB

protein kinase C inhibitor activity

Traceable author statement Ref.2. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P31947-1)

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.
Isoform 2 (identifier: P31947-2)

The sequence of this isoform differs from the canonical sequence as follows:
     85-116: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 24824814-3-3 protein sigma
PRO_0000058643

Sites

Site561Interaction with phosphoserine on interacting protein
Site1291Interaction with phosphoserine on interacting protein

Amino acid modifications

Modified residue51Phosphoserine Ref.15
Modified residue2481Phosphoserine Ref.9 Ref.12 Ref.13 Ref.15

Natural variations

Alternative sequence85 – 11632Missing in isoform 2.
VSP_021768
Natural variant1551M → I.
Corresponds to variant rs11542705 [ dbSNP | Ensembl ].
VAR_048095

Experimental info

Sequence conflict771K → M in CAG46703. Ref.4
Sequence conflict1201Y → H in AAA59546. Ref.2
Sequence conflict2421A → V in AAA59546. Ref.2

Secondary structure

....................... 248
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: 7F4B44E3AA59ECE6

FASTA24827,774
        10         20         30         40         50         60 
MERASLIQKA KLAEQAERYE DMAAFMKGAV EKGEELSCEE RNLLSVAYKN VVGGQRAAWR 

        70         80         90        100        110        120 
VLSSIEQKSN EEGSEEKGPE VREYREKVET ELQGVCDTVL GLLDSHLIKE AGDAESRVFY 

       130        140        150        160        170        180 
LKMKGDYYRY LAEVATGDDK KRIIDSARSA YQEAMDISKK EMPPTNPIRL GLALNFSVFH 

       190        200        210        220        230        240 
YEIANSPEEA ISLAKTTFDE AMADLHTLSE DSYKDSTLIM QLLRDNLTLW TADNAGEEGG 


EAPQEPQS 

« Hide

Isoform 2 [UniParc].

Checksum: 14CBC2F26014D926
Show »

FASTA21624,336

References

« Hide 'large scale' references
[1]"Complementary DNA cloning of a novel epithelial cell marker protein, HME1, that may be down-regulated in neoplastic mammary cells."
Prasad G.L., Valverius E.M., McDuffie E., Cooper H.L.
Cell Growth Differ. 3:507-513(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Epithelium.
[2]"Molecular cloning and expression of the transformation sensitive epithelial marker stratifin. A member of a protein family that has been involved in the protein kinase C signalling pathway."
Leffers H., Madsen P., Rasmussen H.H., Honore B., Andersen A.H., Walbum E., Vandekerckhove J., Celis J.E.
J. Mol. Biol. 231:982-998(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 19-25; 42-49; 118-122; 130-139; 149-159; 161-181; 196-199; 225-229 AND 231-239.
Tissue: Keratinocyte.
[3]"14-3-3 sigma is a p53-regulated inhibitor of G2/M progression."
Hermeking H., Lengauer C., Polyak K., He T.-C., Zhang L., Thiagalingam S., Kinzler K.W., Vogelstein B.
Mol. Cell 1:3-11(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
[4]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[5]"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].
[6]"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] (ISOFORMS 1 AND 2).
Tissue: Cervix, Lung and Placenta.
[7]"Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes."
Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J.
Electrophoresis 13:960-969(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 42-49 AND 118-122.
Tissue: Keratinocyte.
[8]"Exportin 7 defines a novel general nuclear export pathway."
Mingot J.-M., Bohnsack M.T., Jaekle U., Goerlich D.
EMBO J. 23:3227-3236(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH XPO7; ARHGAP1; EIF4A1; VPS26A; VPS29 AND VPS35.
[9]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"CARPs enhance p53 turnover by degrading 14-3-3sigma and stabilizing MDM2."
Yang W., Dicker D.T., Chen J., El-Deiry W.S.
Cell Cycle 7:670-682(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN MDM2 UBIQUITINATION, UBIQUITINATION BY RFFL.
[11]"Phosphorylation-dependent binding of 14-3-3 terminates signalling by the Gab2 docking protein."
Brummer T., Larance M., Herrera Abreu M.T., Lyons R.J., Timpson P., Emmerich C.H., Fleuren E.D.G., Lehrbach G.M., Schramek D., Guilhaus M., James D.E., Daly R.J.
EMBO J. 27:2305-2316(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GAB2.
[12]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Interaction of Akt-phosphorylated SRPK2 with 14-3-3 mediates cell cycle and cell death in neurons."
Jang S.W., Liu X., Fu H., Rees H., Yepes M., Levey A., Ye K.
J. Biol. Chem. 284:24512-24525(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SRPK2.
[15]"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-5 AND SER-248, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"COP9 signalosome subunit 6 stabilizes COP1, which functions as an E3 ubiquitin ligase for 14-3-3sigma."
Choi H.H., Gully C., Su C.H., Velazquez-Torres G., Chou P.C., Tseng C., Zhao R., Phan L., Shaiken T., Chen J., Yeung S.C., Lee M.H.
Oncogene 30:4791-4801(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH COPS6 AND RFWD2.
[18]"A structural basis for 14-3-3sigma functional specificity."
Wilker E.W., Grant R.A., Artim S.C., Yaffe M.B.
J. Biol. Chem. 280:18891-18898(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH PHOSPHOSERINE PEPTIDE.
[19]"Identification and structural characterization of two 14-3-3 binding sites in the human peptidylarginine deiminase type VI."
Rose R., Rose M., Ottmann C.
J. Struct. Biol. 180:65-72(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 1-231 IN COMPLEX WITH PADI6 PHOSPHOPEPTIDES.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M93010 mRNA. Translation: AAA59546.1.
X57348 mRNA. Translation: CAA40623.1.
AF029081 Genomic DNA. Translation: AAC52029.1.
AF029082 mRNA. Translation: AAC52030.1.
CR541905 mRNA. Translation: CAG46703.1.
CR541926 mRNA. Translation: CAG46724.1.
AL034380 Genomic DNA. Translation: CAB92118.1.
BC000329 mRNA. Translation: AAH00329.1.
BC000995 mRNA. Translation: AAH00995.1.
BC001550 mRNA. Translation: AAH01550.1.
BC002995 mRNA. Translation: AAH02995.1.
BC023552 mRNA. Translation: AAH23552.1.
CCDSCCDS288.1. [P31947-1]
PIRS34753.
S38956.
RefSeqNP_006133.1. NM_006142.3. [P31947-1]
UniGeneHs.523718.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1YWTX-ray2.40A/B1-248[»]
1YZ5X-ray2.80A/B1-248[»]
3IQJX-ray1.15A1-231[»]
3IQUX-ray1.05A1-231[»]
3IQVX-ray1.20A1-231[»]
3LW1X-ray1.28A1-248[»]
3MHRX-ray1.15A1-231[»]
3O8IX-ray2.00A1-231[»]
3P1NX-ray1.40A1-231[»]
3P1OX-ray1.90A1-231[»]
3P1PX-ray1.95A1-231[»]
3P1QX-ray1.70A1-231[»]
3P1RX-ray1.70A1-231[»]
3P1SX-ray1.65A1-231[»]
3SMKX-ray2.10A1-231[»]
3SMLX-ray1.90A1-231[»]
3SMMX-ray2.00A1-231[»]
3SMNX-ray2.00A1-231[»]
3SMOX-ray1.80A1-231[»]
3SPRX-ray1.99A1-231[»]
3T0LX-ray1.60A1-231[»]
3T0MX-ray1.62A1-231[»]
3U9XX-ray1.80A1-231[»]
3UX0X-ray1.75A1-231[»]
4DATX-ray1.40A1-231[»]
4DAUX-ray2.00A1-231[»]
4DHMX-ray1.70A1-231[»]
4DHNX-ray1.80A1-231[»]
4DHOX-ray1.70A1-231[»]
4DHPX-ray1.75A1-231[»]
4DHQX-ray1.75A1-231[»]
4DHRX-ray1.40A1-231[»]
4DHSX-ray1.74A1-231[»]
4DHTX-ray1.80A1-231[»]
4DHUX-ray1.67A1-231[»]
4FL5X-ray1.90A/B1-231[»]
4FR3X-ray1.90A1-231[»]
4HQWX-ray2.35A1-231[»]
4HRUX-ray3.15A1-231[»]
4IEAX-ray1.70A1-231[»]
4JC3X-ray2.05A1-231[»]
4JDDX-ray2.10A1-231[»]
ProteinModelPortalP31947.
SMRP31947. Positions 1-231.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109072. 138 interactions.
DIPDIP-29861N.
IntActP31947. 149 interactions.
MINTMINT-108060.
STRING9606.ENSP00000340989.

Chemistry

BindingDBP31947.
ChEMBLCHEMBL1909482.

PTM databases

PhosphoSiteP31947.

Polymorphism databases

DMDM398953.

2D gel databases

OGPP31947.
SWISS-2DPAGEP31947.

Proteomic databases

MaxQBP31947.
PaxDbP31947.
PeptideAtlasP31947.
PRIDEP31947.

Protocols and materials databases

DNASU2810.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000339276; ENSP00000340989; ENSG00000175793. [P31947-1]
GeneID2810.
KEGGhsa:2810.
UCSCuc001bnc.1. human. [P31947-1]

Organism-specific databases

CTD2810.
GeneCardsGC01P027189.
HGNCHGNC:10773. SFN.
HPACAB006268.
CAB040552.
HPA011105.
MIM601290. gene.
neXtProtNX_P31947.
PharmGKBPA177.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5040.
HOGENOMHOG000240379.
HOVERGENHBG050423.
InParanoidP31947.
KOK06644.
OMAEQKGNEE.
OrthoDBEOG7HHWT3.
PhylomeDBP31947.
TreeFamTF102003.

Enzyme and pathway databases

ReactomeREACT_11123. Membrane Trafficking.
REACT_578. Apoptosis.
SignaLinkP31947.

Gene expression databases

BgeeP31947.
CleanExHS_SFN.
GenevestigatorP31947.

Family and domain databases

Gene3D1.20.190.20. 1 hit.
InterProIPR000308. 14-3-3.
IPR023409. 14-3-3_CS.
IPR023410. 14-3-3_domain.
[Graphical view]
PANTHERPTHR18860. PTHR18860. 1 hit.
PfamPF00244. 14-3-3. 1 hit.
[Graphical view]
PIRSFPIRSF000868. 14-3-3. 1 hit.
PRINTSPR00305. 1433ZETA.
SMARTSM00101. 14_3_3. 1 hit.
[Graphical view]
SUPFAMSSF48445. SSF48445. 1 hit.
PROSITEPS00796. 1433_1. 1 hit.
PS00797. 1433_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP31947.
GeneWikiStratifin.
GenomeRNAi2810.
NextBio11071.
PROP31947.
SOURCESearch...

Entry information

Entry name1433S_HUMAN
AccessionPrimary (citable) accession number: P31947
Secondary accession number(s): Q6FH30, Q6FH51, Q96DH0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: July 9, 2014
This is version 153 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

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