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Q80UG5 (SEPT9_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Septin-9
Alternative name(s):
SL3-3 integration site 1 protein
Gene names
Name:Sept9
Synonyms:Kiaa0991, Sint1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length583 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Filament-forming cytoskeletal GTPase By similarity. May play a role in cytokinesis Potential.

Subunit structure

Septins polymerize into heterooligomeric protein complexes that form filaments, and associate with cellular membranes, actin filaments, and microtubules. GTPase activity is required for filament formation. Interacts with SEPT2, SEPT6, SEPT7, SEPT11 and SEPT14. Interacts with RTKN and ARHGEF18 By similarity.

Subcellular location

Cytoplasmcytoskeleton. Note: In an epithelial cell line, concentrates at cell-cell contact areas. After TGF-beta1 treatment and induction of epithelial to mesenchymal transition, colocalizes with actin stress fibers. Ref.9

Tissue specificity

Expressed in all tissues examined except muscle. Isoforms are differentially expressed in testes, kidney, liver, heart, spleen and brain. Ref.1 Ref.2

Developmental stage

At 8 dpc mainly expressed in the lateral plate mesoderm and the somites. Beginning at 9 dpc the lateral plate expression is clearly focused in the developing fore- and hindlimb buds. In the cephalic region, expressed in the first and second branchial arch, in the nasal process and around the otic pit. At 9.5 dpc strongest expression is observed in the mesenchyme of the branchial arches, the limbs, and the developing dorsal root ganglia. Weak to intermediate expression is found in the neural epithelium. Expression is seen in the newly formed somites in the tail bud of older embryos. During formation of the digits, expression seems to outline the surviving tissue bordering it towards the apoptotic webbing. Expression is seen in the developing outer ear and in several areas known to be regulated by intensive epithelial mesenchymal interactions, like the viscera follicles and the developing mammary glands. Ref.2

Involvement in disease

Putative proto-oncogene involved in T-cell lymphomagenesis. May play a role in leukemogenesis.

Miscellaneous

Targeted by proviral insertion in T-cell lymphomas induced by the murine retrovirus SL3-3 MuLV.

Sequence similarities

Belongs to the septin family.

Sequence caution

The sequence BAC65697.2 differs from that shown. Reason: Erroneous initiation.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q80UG5-1)

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: Q80UG5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-249: Missing.
Isoform 3 (identifier: Q80UG5-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-25: MKKSYSGVTRTSSGRLRRLADPTGP → MSDPAVNAQLDGIISDFE

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 583583Septin-9
PRO_0000173536

Regions

Nucleotide binding303 – 3108GTP By similarity
Nucleotide binding443 – 4519GTP By similarity

Sites

Binding site3371GTP By similarity
Binding site3631GTP; via amide nitrogen By similarity
Binding site4991GTP; via amide nitrogen and carbonyl oxygen By similarity
Binding site5141GTP By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue301Phosphoserine Ref.10
Modified residue421Phosphothreonine By similarity
Modified residue621N6-acetyllysine Ref.11
Modified residue821Phosphoserine By similarity
Modified residue851Phosphoserine By similarity
Modified residue1431Phosphothreonine By similarity
Modified residue2761Phosphotyrosine By similarity
Modified residue3251Phosphoserine By similarity

Natural variations

Alternative sequence1 – 249249Missing in isoform 2.
VSP_012341
Alternative sequence1 – 2525MKKSY…DPTGP → MSDPAVNAQLDGIISDFE in isoform 3.
VSP_012342

Sequences

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

Last modified June 1, 2003. Version 1.
Checksum: 174D2F1E8EA382FC

FASTA58365,575
        10         20         30         40         50         60 
MKKSYSGVTR TSSGRLRRLA DPTGPALKRS FEVEEIEPPN STPPRRVQTP LLRATVASSS 

        70         80         90        100        110        120 
QKFQDLGVKN SEPAARLVDS LSQRSPKPSL RRVELAGAKA PEPMSRRTEI SIDISSKQVE 

       130        140        150        160        170        180 
STASAAGPSR FGLKRAEVLG HKTPEPVPRR TEITIVKPQE SVLRRVETPA SKIPEGSAVP 

       190        200        210        220        230        240 
ATDAAPKRVE IQVPKPAEAP NCPLPSQTLE NSEAPMSQLQ SRLEPRPSVA EVPYRNQEDS 

       250        260        270        280        290        300 
EVTPSCVGDM ADNPRDAMLK QAPASRNEKA PMEFGYVGID SILEQMRRKA MKQGFEFNIM 

       310        320        330        340        350        360 
VVGQSGLGKS TLINTLFKSK ISRKSVQPTS EERIPKTIEI KSITHDIEEK GVRMKLTVID 

       370        380        390        400        410        420 
TPGFGDHINN ENCWQPIMKF INDQYEKYLQ EEVNINRKKR IPDTRVHCCL YFIPATGHSL 

       430        440        450        460        470        480 
RPLDIEFMKR LSKVVNIVPV IAKADTLTLE ERVYFKQRIT ADLLSNGIDV YPQKEFDEDA 

       490        500        510        520        530        540 
EDRLVNEKFR EMIPFAVVGS DHEYQVNGKR ILGRKTKWGT IEVENTTHCE FAYLRDLLIR 

       550        560        570        580 
THMQNIKDIT SNIHFEAYRV KRLNEGNSAM ANGIEKEPEA QEM 

« Hide

Isoform 2 [UniParc].

Checksum: 42F7BED2F02F8846
Show »

FASTA33438,599
Isoform 3 [UniParc].

Checksum: 68E1AD335D980444
Show »

FASTA57664,775

References

« Hide 'large scale' references
[1]"Sint1, a common integration site in SL3-3-induced T-cell lymphomas, harbors a putative proto-oncogene with homology to the septin gene family."
Soerensen A.B., Lund A.H., Ethelberg S., Copeland N.G., Jenkins N.A., Pedersen F.S.
J. Virol. 74:2161-2168(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
[2]"Alternative splicing, expression, and gene structure of the septin-like putative proto-oncogene Sint1."
Soerensen A.B., Warming S., Fuechtbauer E.-M., Pedersen F.S.
Gene 285:79-89(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 2), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[3]"Prediction of the coding sequences of mouse homologues of KIAA gene: II. The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., Nakajima D., Nagase T., Ohara O., Koga H.
DNA Res. 10:35-48(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Embryonic tail.
[4]Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[5]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Strain: C57BL/6J.
Tissue: Head.
[6]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[7]"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).
Strain: 129.
Tissue: Mammary gland.
[8]Lubec G., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 548-559, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: OF1.
Tissue: Hippocampus.
[9]"SEPT9 sequence alternations causing hereditary neuralgic amyotrophy are associated with altered interactions with SEPT4/SEPT11 and resistance to Rho/Rhotekin-signaling."
Sudo K., Ito H., Iwamoto I., Morishita R., Asano T., Nagata K.
Hum. Mutat. 28:1005-1013(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[10]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[11]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-62, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ250723 mRNA. Translation: CAB59833.1.
AF450142, AF450141 Genomic DNA. Translation: AAL50685.1.
AK031757 mRNA. Translation: BAC27538.1.
AK122415 mRNA. Translation: BAC65697.2. Different initiation.
AK141312 mRNA. Translation: BAE24646.1.
AL603868, AL611935, AL645975 Genomic DNA. Translation: CAM13312.1.
AL645975, AL603868, AL611935 Genomic DNA. Translation: CAM15613.1.
AL611935, AL603868, AL645975 Genomic DNA. Translation: CAM19703.1.
BC046524 mRNA. Translation: AAH46524.1.
RefSeqNP_001106958.1. NM_001113486.1.
NP_001106959.1. NM_001113487.1.
NP_001106960.1. NM_001113488.1.
NP_059076.1. NM_017380.2.
XP_006533809.1. XM_006533746.1.
UniGeneMm.38450.
Mm.451420.

3D structure databases

ProteinModelPortalQ80UG5.
SMRQ80UG5. Positions 295-563.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid207494. 1 interaction.
IntActQ80UG5. 2 interactions.
MINTMINT-1866943.

PTM databases

PhosphoSiteQ80UG5.

Proteomic databases

PaxDbQ80UG5.
PRIDEQ80UG5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000019038; ENSMUSP00000019038; ENSMUSG00000059248. [Q80UG5-3]
ENSMUST00000093907; ENSMUSP00000091435; ENSMUSG00000059248. [Q80UG5-1]
ENSMUST00000100193; ENSMUSP00000097767; ENSMUSG00000059248. [Q80UG5-2]
ENSMUST00000106349; ENSMUSP00000101956; ENSMUSG00000059248. [Q80UG5-2]
GeneID53860.
KEGGmmu:53860.
UCSCuc007mnd.2. mouse. [Q80UG5-1]
uc007mne.2. mouse. [Q80UG5-3]

Organism-specific databases

CTD10801.
MGIMGI:1858222. Sept9.
RougeSearch...

Phylogenomic databases

eggNOGCOG5019.
GeneTreeENSGT00640000091410.
HOVERGENHBG098529.
InParanoidA2A6U4.
KOK16938.
OMAHRRMETP.
OrthoDBEOG7KWSJ5.
PhylomeDBQ80UG5.
TreeFamTF101078.

Gene expression databases

ArrayExpressQ80UG5.
BgeeQ80UG5.
CleanExMM_SEPT9.
GenevestigatorQ80UG5.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR000038. Cell_div_GTP-bd.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERPTHR18884. PTHR18884. 1 hit.
PfamPF00735. Septin. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
ProtoNetSearch...

Other

ChiTaRSSEPT9. mouse.
NextBio310701.
PROQ80UG5.
SOURCESearch...

Entry information

Entry nameSEPT9_MOUSE
AccessionPrimary (citable) accession number: Q80UG5
Secondary accession number(s): A2A6U2 expand/collapse secondary AC list , A2A6U4, A2A6U6, Q3URP2, Q80TM7, Q9QYX9
Entry history
Integrated into UniProtKB/Swiss-Prot: December 21, 2004
Last sequence update: June 1, 2003
Last modified: April 16, 2014
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot