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UniProtKB/Swiss-Prot entry Q9UHD8


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

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Entry information
Entry name SEPT9_HUMAN
Primary accession number Q9UHD8
Secondary accession numbers Q96QF3 Q96QF4 Q96QF5 Q9HA04 Q9UG40 Q9Y5W4
Integrated into Swiss-Prot on December 21, 2004
Sequence was last modified on April 18, 2006 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 79)
Name and origin of the protein
Protein name Septin-9
Synonyms MLL septin-like fusion protein MSF-A
MLL septin-like fusion protein
Ovarian/Breast septin
Ov/Br septin
Septin D1
Gene name
Name: SEPT9
Synonyms: KIAA0991, MSF
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] (ISOFORM 2), VARIANT VAL-576, TISSUE SPECIFICITY, DISEASE, AND CHROMOSOMAL TRANSLOCATION.
DOI=10.1073/pnas.96.11.6428; PubMed=10339604 [NCBI, ExPASy, EBI, Israel, Japan]
Osaka M., Rowley J.D., Zeleznik-Le N.J.;
"MSF (MLL septin-like fusion), a fusion partner gene of MLL, in a therapy-related acute myeloid leukemia with a t(11;17)(q23;q25).";
Proc. Natl. Acad. Sci. U.S.A. 96:6428-6433(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4 AND 5), FUNCTION, AND VARIANTS CYS-76; LEU-145 AND VAL-576.
PubMed=10987277 [NCBI, ExPASy, EBI, Israel, Japan]
Russell S.E.H., McIlhatton M.A., Burrows J.F., Donaghy P.G., Chanduloy S., Petty E.M., Kalikin L.M., Church S.W., McIlroy S., Harkin D.P., Keilty G.W., Cranston A.N., Weissenbach J., Hickey I., Johnston P.G.;
"Isolation and mapping of a human septin gene to a region on chromosome 17q, commonly deleted in sporadic epithelial ovarian tumors.";
Cancer Res. 60:4729-4734(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), VARIANT VAL-576, TISSUE SPECIFICITY, AND ALTERNATIVE SPLICING.
DOI=10.1006/geno.1999.6077; PubMed=10673329 [NCBI, ExPASy, EBI, Israel, Japan]
Kalikin L.M., Sims H.L., Petty E.M.;
"Genomic and expression analyses of alternatively spliced transcripts of the MLL septin-like fusion gene (MSF) that map to a 17q25 region of loss in breast and ovarian tumors.";
Genomics 63:165-172(2000).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT VAL-576.
Zhang W., He L., Wan T., Yuan Z., Zhu X., Cao X.;
"Novel human cell division control protein septin D1.";
Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
TISSUE=Mammary gland;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT VAL-576.
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND VARIANT VAL-576.
TISSUE=Eye, and Skin;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 26-586, AND VARIANT VAL-576.
TISSUE=Brain;
DOI=10.1093/dnares/6.1.63; PubMed=10231032 [NCBI, ExPASy, EBI, Israel, Japan]
Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro.";
DNA Res. 6:63-70(1999).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 353-586, AND VARIANT VAL-576.
TISSUE=Testis;
DOI=10.1186/1471-2164-8-399; PubMed=17974005 [NCBI, ExPASy, EBI, Israel, Japan]
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Blocker H., Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., Ottenwalder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[10]
TISSUE SPECIFICITY, AND ALTERNATIVE SPLICING.
DOI=10.1038/sj.onc.1204752; PubMed=11593400 [NCBI, ExPASy, EBI, Israel, Japan]
McIlhatton M.A., Burrows J.F., Donaghy P.G., Chanduloy S., Johnston P.G., Russell S.E.;
"Genomic organization, complex splicing pattern and expression of a human septin gene on chromosome 17q25.3.";
Oncogene 20:5930-5939(2001).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85, AND MASS SPECTROMETRY.
DOI=10.1021/pr050048h; PubMed=16083285 [NCBI, ExPASy, EBI, Israel, Japan]
Kim J.-E., Tannenbaum S.R., White F.M.;
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells.";
J. Proteome Res. 4:1339-1346(2005).
[12]
INTERACTION WITH ARHGEF18.
DOI=10.1038/sj.onc.1208101; PubMed=15558029 [NCBI, ExPASy, EBI, Israel, Japan]
Nagata K., Inagaki M.;
"Cytoskeletal modification of Rho guanine nucleotide exchange factor activity: identification of a Rho guanine nucleotide exchange factor as a binding partner for Sept9b, a mammalian septin.";
Oncogene 24:65-76(2005).
[13]
INTERACTION WITH RTKN.
DOI=10.1038/sj.onc.1208862; PubMed=16007136 [NCBI, ExPASy, EBI, Israel, Japan]
Ito H., Iwamoto I., Morishita R., Nozawa Y., Narumiya S., Asano T., Nagata K.;
"Possible role of Rho/Rhotekin signaling in mammalian septin organization.";
Oncogene 24:7064-7072(2005).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85, 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).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30 AND THR-42, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1038/nbt1240; PubMed=16964243 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-278, AND MASS SPECTROMETRY.
DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan]
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.";
Cell 131:1190-1203(2007).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-85; SER-89 AND THR-142, 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-30, AND MASS SPECTROMETRY.
DOI=10.1021/pr0705441; PubMed=18220336 [NCBI, ExPASy, EBI, Israel, Japan]
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30 AND SER-80, AND MASS SPECTROMETRY.
DOI=10.1016/j.molcel.2008.07.007; PubMed=18691976 [NCBI, ExPASy, EBI, Israel, Japan]
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30; THR-38; THR-42 AND THR-49, 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).
[21]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
[22]
VARIANTS HNA TRP-106 AND PHE-111.
DOI=10.1038/ng1649; PubMed=16186812 [NCBI, ExPASy, EBI, Israel, Japan]
Kuhlenbaeumer G., Hannibal M.C., Nelis E., Schirmacher A., Verpoorten N., Meuleman J., Watts G.D.J., De Vriendt E., Young P., Stoegbauer F., Halfter H., Irobi J., Goossens D., Del-Favero J., Betz B.G., Hor H., Kurlemann G., Bird T.D., Airaksinen E., Mononen T., Serradell A.P., Prats J.M., Van Broeckhoven C., De Jonghe P., Timmerman V., Ringelstein E.B., Chance P.F.;
"Mutations in SEPT9 cause hereditary neuralgic amyotrophy.";
Nat. Genet. 37:1044-1046(2005).
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
AF123052; AAD39749.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ312319; CAC42221.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ312320; CAC42222.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ312321; CAC42223.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ312322; CAC42224.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF189712; AAF23373.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF189713; AAF23374.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF142408; AAG27919.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK022493; BAB14057.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT007215; AAP35879.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC021192; AAH21192.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC054004; AAH54004.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB023208; BAA76835.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL080131; CAB45728.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T12519; T12519.
RefSeq NP_001106963.1; -.
NP_001106965.1; -.
NP_001106966.1; -.
NP_001106968.1; -.
NP_006631.2; -.
UniGene Hs.440932
3D structure databases
ModBase Q9UHD8.
Protein-protein interaction databases
IntAct Q9UHD8; 5.
PTM databases
PhosphoSite Q9UHD8; -.
Organism-specific databases
GeneCards GC17P072790; -.
HGNC HGNC:7323; SEPT9.
GenAtlas SEPT9.
MIM 162100; phenotype. [NCBI / EBI]
604061; gene. [NCBI / EBI]
Orphanet 2901; Parsonage-Turner syndrome.
HUGE KIAA0991.
Gene expression databases
ArrayExpress Q9UHD8; -.
Bgee Q9UHD8; -.
CleanEx HS_SEPT9; -.
GermOnline ENSG00000184640; Homo sapiens.
Ontologies
GO
GO:0005874; Cellular component: microtubule (inferred from direct assay from UniProtKB).
GO:0048471; Cellular component: perinuclear region of cytoplasm (inferred from direct assay from UniProtKB).
GO:0005886; Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0001725; Cellular component: stress fiber (inferred from direct assay from UniProtKB).
GO:0005525; Molecular function: GTP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0003924; Molecular function: GTPase activity (traceable author statement from ProtInc).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0007049; Biological process: cell cycle (inferred from electronic annotation from UniProtKB-KW).
GO:0051301; Biological process: cell division (inferred from electronic annotation from UniProtKB-KW).
GO:0045786; Biological process: negative regulation of cell cycle (inferred from electronic annotation from UniProtKB-KW).
GO:0051291; Biological process: protein heterooligomerization (inferred from direct assay from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR000038; Cell_Div_GTP_bd.
Graphical view of domain structure.
PANTHER PTHR18884; Cell_Div_GTP_bd; 1.
Pfam PF00735; Septin; 1.
Pfam graphical view of domain structure.
ProDom PD002565; GTP_Cell_Div; 1.
[Domain structure / List of seq. sharing at least 1 domain]
Proteomic databases
PRIDE Q9UHD8; -.
Genome annotation databases
Ensembl ENSG00000184640; Homo sapiens. [Contig view]
GeneID 10801; -.
KEGG hsa:10801; -.
NMPDR fig|9606.3.peg.14468; -.
Phylogenomic databases
HOVERGEN Q9UHD8; -.
Other
NextBio 41021; -.
SOURCE SEPT9; Homo sapiens.
ProtoNet Q9UHD8.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; Anti-oncogene; Cell cycle; Cell division; Cell membrane; Chromosomal rearrangement; Disease mutation; GTP-binding; Membrane; Nucleotide-binding; Phosphoprotein; Polymorphism.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   586  586     Septin-9. PRO_0000173535
NP_BIND   305   312  8     GTP (By similarity). 
NP_BIND   447   453  7     GTP (By similarity). 
BINDING   501   501        GTP; via amide nitrogen and carbonyl oxygen (By similarity). 
MOD_RES   30    30        Phosphoserine. 
MOD_RES   38    38        Phosphothreonine. 
MOD_RES   42    42        Phosphothreonine. 
MOD_RES   49    49        Phosphothreonine. 
MOD_RES   80    80        Phosphoserine. 
MOD_RES   82    82        Phosphoserine. 
MOD_RES   85    85        Phosphoserine. 
MOD_RES   89    89        Phosphoserine. 
MOD_RES   142   142        Phosphothreonine. 
MOD_RES   278   278        Phosphotyrosine. 
VAR_SEQ   1   251        Missing (in isoform 4 and isoform 6). VSP_012335
VAR_SEQ   1   164        Missing (in isoform 3). VSP_012336
VAR_SEQ   1    25        MKKSYSGGTRTSSGRLRRLGDSSGP -> MERDRIS (in isoform 2). VSP_012337
VAR_SEQ   1    25        MKKSYSGGTRTSSGRLRRLGDSSGP -> MSDPAVNAQLDGIISDFE (in isoform 5). VSP_012338
VAR_SEQ   426   447        DIEFMKRLSKVVNIVPVIAKAD -> EQKVPLSQPSADCSARCGDRLE (in isoform 6). VSP_012339
VAR_SEQ   448   586        Missing (in isoform 6). VSP_012340
VARIANT   76    76  1     R -> C. VAR_020667 
VARIANT   106   106  1     R -> W (in HNA). VAR_033101 
VARIANT   111   111  1     S -> F (in HNA). VAR_033102 
VARIANT   145   145  1     P -> L (in dbSNP:rs34587622 [NCBI]). VAR_020668 
VARIANT   576   576  1     M -> V. VAR_020669 
CONFLICT   487   487        V -> E (in Ref. 5). 
Sequence information
Length: 586 AA [This is the length of the unprocessed precursor] Molecular weight: 65401 Da [This is the MW of the unprocessed precursor] CRC64: D4404578328CFCFE [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKKSYSGGTR TSSGRLRRLG DSSGPALKRS FEVEEVETPN STPPRRVQTP LLRATVASST 

        70         80         90        100        110        120 
QKFQDLGVKN SEPSARHVDS LSQRSPKASL RRVELSGPKA AEPVSRRTEL SIDISSKQVE 

       130        140        150        160        170        180 
NAGAIGPSRF GLKRAEVLGH KTPEPAPRRT EITIVKPQES AHRRMEPPAS KVPEVPTAPA 

       190        200        210        220        230        240 
TDAAPKRVEI QMPKPAEAPT APSPAQTLEN SEPAPVSQLQ SRLEPKPQPP VAEATPRSQE 

       250        260        270        280        290        300 
ATEAAPSCVG DMADTPRDAG LKQAPASRNE KAPVDFGYVG IDSILEQMRR KAMKQGFEFN 

       310        320        330        340        350        360 
IMVVGQSGLG KSTLINTLFK SKISRKSVQP TSEERIPKTI EIKSITHDIE EKGVRMKLTV 

       370        380        390        400        410        420 
IDTPGFGDHI NNENCWQPIM KFINDQYEKY LQEEVNINRK KRIPDTRVHC CLYFIPATGH 

       430        440        450        460        470        480 
SLRPLDIEFM KRLSKVVNIV PVIAKADTLT LEERVHFKQR ITADLLSNGI DVYPQKEFDE 

       490        500        510        520        530        540 
DSEDRLVNEK FREMIPFAVV GSDHEYQVNG KRILGRKTKW GTIEVENTTH CEFAYLRDLL 

       550        560        570        580 
IRTHMQNIKD ITSSIHFEAY RVKRLNEGSS AMANGMEEKE PEAPEM 

Q9UHD8 in FASTA format

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