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Q9R1T4 (SEPT6_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 127. 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-6
Gene names
Name:Sept6
Synonyms:Kiaa0128
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length434 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Filament-forming cytoskeletal GTPase. Required for normal organization of the actin cytoskeleton. Involved in cytokinesis.

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. Filaments are assembled from asymmetrical heterotrimers, composed of SEPT2, SEPT6 and SEPT7 that associate head-to-head to form a hexameric unit. Within the trimer, directly interacts with SEPT2 and SEPT7. Also interacts with SEPT9 and SEPT12. Interaction with SEPT12 alters filament structure. Interacts with SOCS7. Interacts with HNRNPA1 By similarity.

Subcellular location

Cytoplasm. Cytoplasmcytoskeletonspindle. Chromosomecentromerekinetochore By similarity. Cleavage furrow By similarity. Midbody By similarity. Note: In metaphase cells, localized within the microtubule spindle. At the metaphase plate, in close apposition to the kinetochores of the congressed chromosomes. In cells undergoing cytokinesis, localized to the midbody, the ingressing cleavage furrow, and the central spindle By similarity.

Tissue specificity

Associated with synaptic vesicles in various brain regions, including glomeruli of the olfactory bulb. Ref.7

Miscellaneous

Coordinated expression with SEPT2 and SEPT7 By similarity.

Sequence similarities

Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. Septin GTPase family.

Contains 1 septin-type G (guanine nucleotide-binding) domain.

Sequence caution

The sequence BAD32172.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAM19782.1 differs from that shown. Reason: Erroneous gene model prediction.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform II (identifier: Q9R1T4-1)

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 I (identifier: Q9R1T4-2)

Also known as: III;

The sequence of this isoform differs from the canonical sequence as follows:
     428-434: Missing.
Isoform V (identifier: Q9R1T4-3)

The sequence of this isoform differs from the canonical sequence as follows:
     428-434: NPWLCIE → FF

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 434433Septin-6
PRO_0000173526

Regions

Domain39 – 305267Septin-type G
Nucleotide binding49 – 568GTP By similarity
Nucleotide binding185 – 1939GTP By similarity
Coiled coil321 – 40787 Potential

Sites

Binding site1041GTP; via amide nitrogen By similarity
Binding site2391GTP; via amide nitrogen and carbonyl oxygen By similarity
Binding site2541GTP By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue3671N6-acetyllysine By similarity

Natural variations

Alternative sequence428 – 4347Missing in isoform I.
VSP_006055
Alternative sequence428 – 4347NPWLCIE → FF in isoform V.
VSP_006056

Experimental info

Sequence conflict101V → L in BAB28516. Ref.2
Sequence conflict101Missing in BAC33342. Ref.2
Sequence conflict621L → P in BAC40335. Ref.2
Sequence conflict1411H → Y in BAA82838. Ref.1
Sequence conflict1701M → I in BAE36069. Ref.2
Sequence conflict238 – 2392VG → C in BAB28516. Ref.2
Sequence conflict3501V → A in BAC40335. Ref.2
Sequence conflict4031A → R in BAA82838. Ref.1

Sequences

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

Last modified January 23, 2007. Version 4.
Checksum: 33DCD4F44607168A

FASTA43449,620
        10         20         30         40         50         60 
MAAADIARQV GEDCRTVPLA GHVGFDSLPD QLVNKSVSQG FCFNILCVGE TGLGKSTLMD 

        70         80         90        100        110        120 
TLFNTKFEGE PATHTQPGVQ LQSNTYDLQE SNVGLKLTIV STVGFGDQIN KEDSYKPIVE 

       130        140        150        160        170        180 
FIDAQFEAYL QEELKIRRVL HSYHDSRIHV CLYFIAPTGH SLKSLDLVTM KKLDSKVNII 

       190        200        210        220        230        240 
PVIAKSDAIS KSELAKFKIK ITSELVSNGV QIYQFPTDDE SVSEINGTMN AHLPFAVVGS 

       250        260        270        280        290        300 
TEEVKIGNKM MRARQYPWGT VQVENEAHCD FVKLREMLIR VNMEDLREQT HARHYELYRR 

       310        320        330        340        350        360 
CKLEEMGFKD TDPDSKPFSL QETYEAKRNE FLGELQKKEE EMRQMFVQRV KEKEAELKEA 

       370        380        390        400        410        420 
EKELHEKFDR LKKLHQEEKK KLEDKKKCLD EEMNAFKQRK AAAELLQSQG SQAGGSQTLK 

       430 
RDKEKKNNPW LCIE 

« Hide

Isoform I (III) [UniParc].

Checksum: 6A6315BB1E6B24C4
Show »

FASTA42748,764
Isoform V [UniParc].

Checksum: 59BB0A6315BB1E6B
Show »

FASTA42949,058

References

« Hide 'large scale' references
[1]"Identification of mouse Septin6 gene and its product."
Kinoshita M.
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM V).
Strain: NIH Swiss.
Tissue: Heart.
[2]"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 II AND V).
Strain: C57BL/6J and NOD.
Tissue: Embryo, Head and Thymus.
[3]"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.
[4]"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 I).
Tissue: Salivary gland.
[5]"Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 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., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
DNA Res. 11:205-218(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-427.
Tissue: Fetal brain.
[6]Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 16-111; 164-171; 177-185; 255-273; 281-287; 294-299; 310-337; 388-397 AND 400-420, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6 and OF1.
Tissue: Brain and Hippocampus.
[7]"Differential localization of septins in the mouse brain."
Kinoshita A., Noda M., Kinoshita M.
J. Comp. Neurol. 428:223-239(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB023622 mRNA. Translation: BAA82838.1.
AK012858 mRNA. Translation: BAB28516.1.
AK048455 mRNA. Translation: BAC33342.1.
AK088406 mRNA. Translation: BAC40335.1.
AK088614 mRNA. Translation: BAC40453.1.
AK160884 mRNA. Translation: BAE36069.1.
AK162755 mRNA. Translation: BAE37050.1.
AL450399 Genomic DNA. Translation: CAM19780.1.
AL450399 Genomic DNA. Translation: CAM19781.1.
AL450399 Genomic DNA. Translation: CAM19782.1. Sequence problems.
BC010489 mRNA. Translation: AAH10489.1.
AK172894 mRNA. Translation: BAD32172.1. Different initiation.
CCDSCCDS30066.1. [Q9R1T4-3]
CCDS53051.1. [Q9R1T4-1]
CCDS57749.1. [Q9R1T4-2]
RefSeqNP_001170794.1. NM_001177323.2.
NP_001170795.1. NM_001177324.1. [Q9R1T4-1]
NP_001240635.1. NM_001253706.1. [Q9R1T4-2]
NP_064326.2. NM_019942.5. [Q9R1T4-3]
XP_006541452.1. XM_006541389.1. [Q9R1T4-2]
XP_006541453.1. XM_006541390.1. [Q9R1T4-2]
UniGeneMm.260036.
Mm.470184.

3D structure databases

ProteinModelPortalQ9R1T4.
SMRQ9R1T4. Positions 41-307.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid208037. 4 interactions.
IntActQ9R1T4. 3 interactions.
MINTMINT-4134187.

PTM databases

PhosphoSiteQ9R1T4.

Proteomic databases

MaxQBQ9R1T4.
PaxDbQ9R1T4.
PRIDEQ9R1T4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000053456; ENSMUSP00000054034; ENSMUSG00000050379. [Q9R1T4-2]
ENSMUST00000060474; ENSMUSP00000062014; ENSMUSG00000050379. [Q9R1T4-3]
ENSMUST00000115239; ENSMUSP00000110894; ENSMUSG00000050379. [Q9R1T4-1]
GeneID56526.
KEGGmmu:56526.
UCSCuc009sxx.2. mouse. [Q9R1T4-3]
uc009sxz.2. mouse. [Q9R1T4-1]

Organism-specific databases

CTD23157.
MGIMGI:1888939. Sept6.
RougeSearch...

Phylogenomic databases

eggNOGCOG5019.
GeneTreeENSGT00640000091237.
HOVERGENHBG065093.
InParanoidQ9R1T4.
KOK16939.
OMANHGFCFN.
OrthoDBEOG7J9VQK.
PhylomeDBQ9R1T4.
TreeFamTF101080.

Gene expression databases

ArrayExpressQ9R1T4.
BgeeQ9R1T4.
CleanExMM_SEPT6.
GenevestigatorQ9R1T4.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR000038. Cell_div_GTP-bd.
IPR027417. P-loop_NTPase.
IPR016491. Septin.
[Graphical view]
PANTHERPTHR18884. PTHR18884. 1 hit.
PfamPF00735. Septin. 1 hit.
[Graphical view]
PIRSFPIRSF006698. Septin. 1 hit.
SUPFAMSSF52540. SSF52540. 1 hit.
PROSITEPS51719. G_SEPTIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSEPT6. mouse.
NextBio312866.
PROQ9R1T4.
SOURCESearch...

Entry information

Entry nameSEPT6_MOUSE
AccessionPrimary (citable) accession number: Q9R1T4
Secondary accession number(s): A2A3V9 expand/collapse secondary AC list , A2A3W0, Q3TRH9, Q3TUA2, Q542H3, Q6A0C4, Q8C2L2, Q8C848, Q91XH2, Q9CZ94
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 127 of the entry and version 4 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