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UniProtKB/Swiss-Prot entry P29590


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PML_HUMAN
Primary accession number P29590
Secondary accession numbers P29591 P29592 P29593 Q00755 Q96S41
Integrated into Swiss-Prot on April 1, 1993
Sequence was last modified on November 25, 2008 (Sequence version 3)
Annotations were last modified on    November 25, 2008 (Entry version 114)
Name and origin of the protein
Protein name Probable transcription factor PML
Synonyms Tripartite motif-containing protein 19
RING finger protein 71
Gene name
Name: PML
Synonyms: MYL, RNF71, TRIM19
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS PML-1; PML-2 AND PML-3), AND CHROMOSOMAL TRANSLOCATION WITH RARA.
PubMed=1720570 [NCBI, ExPASy, EBI, Israel, Japan]
Goddard A.D., Borrow J., Freemont P.S., Solomon E.;
"Characterization of a zinc finger gene disrupted by the t(15;17) in acute promyelocytic leukemia.";
Science 254:1371-1374(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PML-X).
PubMed=1311253 [NCBI, ExPASy, EBI, Israel, Japan]
Kastner P., Perez A., Lutz Y., Rochette-Egly C., Gaub M.P., Durand B., Lanotte M., Berger R., Chambon P.;
"Structure, localization and transcriptional properties of two classes of retinoic acid receptor alpha fusion proteins in acute promyelocytic leukemia (APL): structural similarities with a new family of oncoproteins.";
EMBO J. 11:629-642(1992).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PML-3B).
DOI=10.1016/0092-8674(91)90112-C; PubMed=1652368 [NCBI, ExPASy, EBI, Israel, Japan]
Kakizuka A., Miller W.H. Jr., Umenono K., Warrell R.P. Jr., Frankel S.R., Murty V.V., Dmitrovsky E., Evans R.M.;
"Chromosomal translocation t(15;17) in human acute promyelocytic leukemia fuses RAR alpha with a novel putative transcription factor, PML.";
Cell 66:663-674(1991).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PML-3B).
Goddard A.D., Solomon E.;
Submitted (JAN-1992) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PML-1).
DOI=10.1093/emboj/20.9.2140; PubMed=11331580 [NCBI, ExPASy, EBI, Israel, Japan]
Reymond A., Meroni G., Fantozzi A., Merla G., Cairo S., Luzi L., Riganelli D., Zanaria E., Messali S., Cainarca S., Guffanti A., Minucci S., Pelicci P.G., Ballabio A.;
"The tripartite motif family identifies cell compartments.";
EMBO J. 20:2140-2151(2001).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature04601; PubMed=16572171 [NCBI, ExPASy, EBI, Israel, Japan]
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
"Analysis of the DNA sequence and duplication history of human chromosome 15.";
Nature 440:671-675(2006).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 419-466, AND CHROMOSOMAL TRANSLOCATION WITH RARA.
PubMed=1312695 [NCBI, ExPASy, EBI, Israel, Japan]
Tong J.H., Dong S., Geng J.P., Huang W., Wang Z.Y., Sun G.L., Chen S.J., Chen Z., Larsen C.-J., Berger R.;
"Molecular rearrangements of the MYL gene in acute promyelocytic leukemia (APL, M3) define a breakpoint cluster region as well as some molecular variants.";
Oncogene 7:311-316(1992).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 454-503, AND CHROMOSOMAL TRANSLOCATION WITH RARA.
PubMed=12691149 [NCBI, ExPASy, EBI, Israel, Japan]
Fujita K., Oba R., Harada H., Mori H., Niikura H., Isoyama K., Omine M.;
"Cytogenetics, FISH and RT-PCR analysis of acute promyelocytic leukemia: structure of the fusion point in a case lacking classic t(15;17) translocation.";
Leuk. Lymphoma 44:111-115(2003).
[9]
SUMOYLATION AT LYS-65; LYS-160 AND LYS-490, MUTAGENESIS OF LYS-65; LYS-133; LYS-150; LYS-160 AND LYS-490, SUBCELLULAR LOCATION, AND FUNCTION.
DOI=10.1074/jbc.273.41.26675; PubMed=9756909 [NCBI, ExPASy, EBI, Israel, Japan]
Kamitani T., Kito K., Nguyen H.P., Wada H., Fukuda-Kamitani T., Yeh E.T.H.;
"Identification of three major sentrinization sites in PML.";
J. Biol. Chem. 273:26675-26682(1998).
[10]
INTERACTION WITH TRIM27.
PubMed=9570750 [NCBI, ExPASy, EBI, Israel, Japan]
Cao T., Duprez E., Borden K.L., Freemont P.S., Etkin L.D.;
"Ret finger protein is a normal component of PML nuclear bodies and interacts directly with PML.";
J. Cell Sci. 111:1319-1329(1998).
[11]
INTERACTION WITH LASSA VIRUS Z PROTEIN.
PubMed=9420283 [NCBI, ExPASy, EBI, Israel, Japan]
Borden K.L., Campbell-Dwyer E.J., Salvato M.S.;
"An arenavirus RING (zinc-binding) protein binds the oncoprotein promyelocyte leukemia protein (PML) and relocates PML nuclear bodies to the cytoplasm.";
J. Virol. 72:758-766(1998).
[12]
INTERACTION WITH SIRT1.
DOI=10.1093/emboj/21.10.2383; PubMed=12006491 [NCBI, ExPASy, EBI, Israel, Japan]
Langley E., Pearson M., Faretta M., Bauer U.-M., Frye R.A., Minucci S., Pelicci P.G., Kouzarides T.;
"Human SIR2 deacetylates p53 and antagonizes PML/p53-induced cellular senescence.";
EMBO J. 21:2383-2396(2002).
[13]
INTERACTION WITH TOPBP1.
DOI=10.1128/MCB.23.12.4247-4256.2003; PubMed=12773567 [NCBI, ExPASy, EBI, Israel, Japan]
Xu Z.-X., Timanova-Atanasova A., Zhao R.-X., Chang K.-S.;
"PML colocalizes with and stabilizes the DNA damage response protein TopBP1.";
Mol. Cell. Biol. 23:4247-4256(2003).
[14]
INTERACTION WITH SIAH1, AND DEGRADATION.
DOI=10.1074/jbc.M306407200; PubMed=14645235 [NCBI, ExPASy, EBI, Israel, Japan]
Fanelli M., Fantozzi A., De Luca P., Caprodossi S., Matsuzawa S., Lazar M.A., Pelicci P.G., Minucci S.;
"The coiled-coil domain is the structural determinant for mammalian homologues of Drosophila Sina-mediated degradation of promyelocytic leukemia protein and other tripartite motif proteins by the proteasome.";
J. Biol. Chem. 279:5374-5379(2004).
[15]
FUNCTION, INTERACTION WITH ELF4, AND SUBCELLULAR LOCATION.
DOI=10.1074/jbc.M312439200; PubMed=14976184 [NCBI, ExPASy, EBI, Israel, Japan]
Suico M.A., Yoshida H., Seki Y., Uchikawa T., Lu Z., Shuto T., Matsuzaki K., Nakao M., Li J.-D., Kai H.;
"Myeloid Elf-1-like factor, an ETS transcription factor, up-regulates lysozyme transcription in epithelial cells through interaction with promyelocytic leukemia protein.";
J. Biol. Chem. 279:19091-19098(2004).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; SER-403; SER-518; SER-527; SER-530; SER-535; SER-560; SER-561; SER-562 AND SER-565, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-505 AND SER-512, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0611217104; PubMed=17287340 [NCBI, ExPASy, EBI, Israel, Japan]
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403; THR-409; SER-518; SER-527 AND SER-530, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[19]
STRUCTURE BY NMR OF 49-104.
PubMed=7729428 [NCBI, ExPASy, EBI, Israel, Japan]
Borden K.L.B., Boddy M.N., Lally J., O'Reilly N.J., Martin S., Howe K., Solomon E., Freemont P.S.;
"The solution structure of the RING finger domain from the acute promyelocytic leukaemia proto-oncoprotein PML.";
EMBO J. 14:1532-1541(1995).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M79462; AAA60388.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M79463; AAA60351.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M79464; AAA60390.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X63131; CAA44841.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M73778; AAA60125.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M80185; AAA60352.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF230401; AAG50180.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC013486; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
AC108137; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
X64800; CAA46026.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB067754; BAB62809.1; ALT_TERM; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A40044; A40044.
I38054; I38054.
S19244; S19244.
S42516; S42516.
S44381; S44381.
RefSeq NP_002666.1; -.
NP_150241.2; -.
NP_150242.1; -.
NP_150243.2; -.
NP_150247.2; -.
NP_150249.1; -.
NP_150250.2; -.
NP_150252.1; -.
NP_150253.2; -.
UniGene Hs.526464
3D structure databases
PDB
1BOR; NMR; -; A=49-104.[ExPASy / RCSB / EBI]
PDBsum 1BOR; -.
ModBase P29590.
Protein-protein interaction databases
IntAct P29590; -.
PTM databases
PhosphoSite P29590; -.
Organism-specific databases
HGNC HGNC:9113; PML.
GenAtlas PML.
HPA CAB010194; -.
CAB016304; -.
HPA008312; -.
MIM 102578; gene. [NCBI / EBI]
Orphanet 520; Acute promyelocytic leukaemia.
PharmGKB PA33439; -.
GeneCards P29590.
Gene expression databases
ArrayExpress P29590; -.
CleanEx HS_PML; -.
GermOnline ENSG00000140464; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0005626; Cellular component: insoluble fraction (inferred from direct assay from UniProtKB).
GO:0031965; Cellular component: nuclear membrane (inferred from direct assay from UniProtKB).
GO:0005730; Cellular component: nucleolus (inferred from direct assay from UniProtKB).
GO:0016605; Cellular component: PML body (inferred from direct assay from UniProtKB).
GO:0003677; Molecular function: DNA binding (inferred from electronic annotation from UniProtKB-KW).
GO:0042803; Molecular function: protein homodimerization activity (inferred from physical interaction from UniProtKB).
GO:0032184; Molecular function: SUMO polymer binding (inferred from physical interaction from UniProtKB).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from InterPro).
GO:0006977; Biological process: DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest (inferred from sequence or structural similarity from UniProtKB).
GO:0042771; Biological process: DNA damage response, signal transduction by p53 class mediator resulting in induction of apoptosis (inferred from sequence or structural similarity from UniProtKB).
GO:0044419; Biological process: interspecies interaction between organisms (inferred from electronic annotation from UniProtKB-KW).
GO:0051457; Biological process: maintenance of protein location in nucleus (inferred from direct assay from MGI).
GO:0016525; Biological process: negative regulation of angiogenesis (inferred from mutant phenotype from UniProtKB).
GO:0030308; Biological process: negative regulation of cell growth (inferred from direct assay from UniProtKB).
GO:0008285; Biological process: negative regulation of cell proliferation (inferred from mutant phenotype from UniProtKB).
GO:0016481; Biological process: negative regulation of transcription (inferred from direct assay from UniProtKB).
GO:0006461; Biological process: protein complex assembly (inferred from direct assay from UniProtKB).
GO:0006355; Biological process: regulation of transcription, DNA-dependent (inferred from electronic annotation from UniProtKB-KW).
GO:0034097; Biological process: response to cytokine stimulus (inferred from direct assay from UniProtKB).
GO:0001666; Biological process: response to hypoxia (inferred from direct assay from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR000315; Znf_B-box.
IPR001841; Znf_RING.
IPR013083; Znf_RING/FYVE/PHD.
Graphical view of domain structure.
Gene3D G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
Pfam PF00643; zf-B_box; 2.
PF00097; zf-C3HC4; 1.
Pfam graphical view of domain structure.
SMART SM00336; BBOX; 1.
SM00184; RING; 1.
SMART graphical view of domain structure.
PROSITE PS50119; ZF_BBOX; 2.
PS00518; ZF_RING_1; 1.
PS50089; ZF_RING_2; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P29590.
ProtoNet P29590.
Genome annotation databases
Ensembl ENSG00000140464; Homo sapiens. [Contig view]
GeneID 5371; -.
KEGG hsa:5371; -.
Phylogenomic databases
HOGENOM P29590; -.
HOVERGEN P29590; -.
Other
LinkHub P29590; -.
NextBio 20820; -.
SOURCE PML; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Activator; Alternative splicing; Chromosomal rearrangement; Coiled coil; Cytoplasm; DNA-binding; Host-virus interaction; Metal-binding; Nucleus; Phosphoprotein; Proto-oncogene; Repeat; Transcription; Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   882  882     Probable transcription factor PML. PRO_0000056001
ZN_FING   57    92  36     RING-type. 
ZN_FING   124   166  43     B box-type 1; atypical. 
ZN_FING   183   236  54     B box-type 2. 
REGION   476   490  15     Nuclear localization signal. 
COILED   228   253  26     Potential. 
COMPBIAS   3    46  44     Pro-rich. 
METAL   57    57        Zinc 1. 
METAL   60    60        Zinc 1. 
METAL   72    72        Zinc 2. 
METAL   74    74        Zinc 2. 
METAL   77    77        Zinc 1. 
METAL   80    80        Zinc 1. 
METAL   88    88        Zinc 2. 
METAL   91    91        Zinc 2. 
SITE   394   395  2     Breakpoint for translocation to form PML-RARA oncogene in type A APL. 
SITE   552   553  2     Breakpoint for translocation to form PML-RARA oncogene in type B APL. 
MOD_RES   8     8        Phosphoserine. 
MOD_RES   403   403        Phosphoserine. 
MOD_RES   409   409        Phosphothreonine. 
MOD_RES   504   504        Phosphoserine (By similarity). 
MOD_RES   505   505        Phosphoserine. 
MOD_RES   512   512        Phosphoserine. 
MOD_RES   518   518        Phosphoserine. 
MOD_RES   527   527        Phosphoserine. 
MOD_RES   530   530        Phosphoserine. 
MOD_RES   535   535        Phosphoserine. 
MOD_RES   560   560        Phosphoserine. 
MOD_RES   561   561        Phosphoserine. 
MOD_RES   562   562        Phosphoserine. 
MOD_RES   565   565        Phosphoserine. 
CROSSLNK   65    65        Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO). 
CROSSLNK   160   160        Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO). 
CROSSLNK   490   490        Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO). 
VAR_SEQ   404   466        Missing (in some isoforms). VSP_005737
VAR_SEQ   553   560        EERVVVIS -> GRERNALW (in isoform PML-3B). VSP_005742
VAR_SEQ   561   882        Missing (in isoform PML-3B). VSP_005743
VAR_SEQ   571   882        SSRELDDSSSESSDLQLEGPSTLRVLDENLADPQAEDRPL VFFDLKIDNETQKISQLAAVNRESKFRVVIQPEAFFSIYS KAVSLEVGLQHFLSFLSSMRRPILACYKLWGPGLPNFFRA LEDINRLWEFQEAISGFLAALPLIRERVPGASSFKLKNLA QTYLARNMSERSAMAAVLAMRDLCRLLEVSPGPQLAQHVY PFSSLQCFASLQPLVQAAVLPRAEARLLALHNVSFMELLS AHRRDRQGGLKKYSRYLSLQTTTLPPAQPAFNLQALGTYF EGLLEGPALARAEGVSTPLAGRGLAERASQQS -> CMEPMETAEPQSSPAHSSPAHSSPVQSLLRAQGASSLPCG TYHPPAWPPHQPAEQAATPDAEPHSEPPDHQERPAVHRGI RYLLYRAQRAIRLRHALRLHPQLHRAPIRTWSPHVVQAST PAITGPLNHPANAQEHPAQLQRGISPPHRIRGAVRSRSRS LRGSSHLSQWLNNFFALPFSSMASQLDMSSVVGAGEGRAQ TLGAVVPPGDSVRGSMEASQVQVPLEASPITFPPPCAPER PPISPVPGARQAGL (in isoform PML-3). VSP_005741
VAR_SEQ   571   611        SSRELDDSSSESSDLQLEGPSTLRVLDENLADPQAE DRPLV -> VSGPEVQPRTPASPHFRSQGAQPQQVTLRLALRLGN FPVRH (in isoform PML-2). VSP_005739
VAR_SEQ   612   882        Missing (in isoform PML-2). VSP_005740
VAR_SEQ   621   633        TQKISQLAAVNRE -> SGFSWGYPHPFLI (in isoform PML-X). VSP_005744
VAR_SEQ   634   882        Missing (in isoform PML-X). VSP_005745
VAR_SEQ   648   664        Missing (in some isoforms). VSP_005738
MUTAGEN   65    65        K->R: Loss of one sumoylation. No effect on nuclear body formation. Loss of 2 sumoylations; when associated with R-490 with or without R-133 or R-150. No effect on nuclear body formation; when associated with R-490. No sumoylation nor nuclear body formation; when associated with R-160 and R-490. 
MUTAGEN   68    68        K->R: No effect on sumoylation levels. 
MUTAGEN   133   133        K->R: Loss of 2 sumoylations; when associated with R-65 and R-490. 
MUTAGEN   150   150        K->R: Loss of 2 sumoylations; when associated with R-65 and R-490. 
MUTAGEN   160   160        K->R: Loss of 2 sumoylations; when asociated with or without R-65. No sumoylation nor nuclear body formation; when associated with or without R-65 and R-490. 
MUTAGEN   490   490        K->R: Loss of 2 sumoylations; when associated with R-65 with or without R-133. No effect on nuclear body formation; when associated with R-65. No sumoylation nor nuclear body formation; when associated with R-65 and R-160. 
CONFLICT   419   419        P -> A (in Ref. 1; AAA60351/AAA60388/AAA60390 and 3; AAA60352). 
CONFLICT   645   645        F -> L (in Ref. 1; AAA60388 and 5; AAG50180). 
STRAND   58    60  3      
STRAND   82    87  6      
STRAND   93    96  4      
Sequence information
Length: 882 AA [This is the length of the unprocessed precursor] Molecular weight: 97551 Da [This is the MW of the unprocessed precursor] CRC64: D50968A977E34287 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MEPAPARSPR PQQDPARPQE PTMPPPETPS EGRQPSPSPS PTERAPASEE EFQFLRCQQC 

        70         80         90        100        110        120 
QAEAKCPKLL PCLHTLCSGC LEASGMQCPI CQAPWPLGAD TPALDNVFFE SLQRRLSVYR 

       130        140        150        160        170        180 
QIVDAQAVCT RCKESADFWC FECEQLLCAK CFEAHQWFLK HEARPLAELR NQSVREFLDG 

       190        200        210        220        230        240 
TRKTNNIFCS NPNHRTPTLT SIYCRGCSKP LCCSCALLDS SHSELKCDIS AEIQQRQEEL 

       250        260        270        280        290        300 
DAMTQALQEQ DSAFGAVHAQ MHAAVGQLGR ARAETEELIR ERVRQVVAHV RAQERELLEA 

       310        320        330        340        350        360 
VDARYQRDYE EMASRLGRLD AVLQRIRTGS ALVQRMKCYA SDQEVLDMHG FLRQALCRLR 

       370        380        390        400        410        420 
QEEPQSLQAA VRTDGFDEFK VRLQDLSSCI TQGKDAAVSK KASPEAASTP RDPIDVDLPE 

       430        440        450        460        470        480 
EAERVKAQVQ ALGLAEAQPM AVVQSVPGAH PVPVYAFSIK GPSYGEDVSN TTTAQKRKCS 

       490        500        510        520        530        540 
QTQCPRKVIK MESEEGKEAR LARSSPEQPR PSTSKAVSPP HLDGPPSPRS PVIGSEVFLP 

       550        560        570        580        590        600 
NSNHVASGAG EAEERVVVIS SSEDSDAENS SSRELDDSSS ESSDLQLEGP STLRVLDENL 

       610        620        630        640        650        660 
ADPQAEDRPL VFFDLKIDNE TQKISQLAAV NRESKFRVVI QPEAFFSIYS KAVSLEVGLQ 

       670        680        690        700        710        720 
HFLSFLSSMR RPILACYKLW GPGLPNFFRA LEDINRLWEF QEAISGFLAA LPLIRERVPG 

       730        740        750        760        770        780 
ASSFKLKNLA QTYLARNMSE RSAMAAVLAM RDLCRLLEVS PGPQLAQHVY PFSSLQCFAS 

       790        800        810        820        830        840 
LQPLVQAAVL PRAEARLLAL HNVSFMELLS AHRRDRQGGL KKYSRYLSLQ TTTLPPAQPA 

       850        860        870        880 
FNLQALGTYF EGLLEGPALA RAEGVSTPLA GRGLAERASQ QS 

P29590 in FASTA format

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