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Q9R1T4

- SEPT6_MOUSE

UniProt

Q9R1T4 - SEPT6_MOUSE

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Protein

Septin-6

Gene

Sept6

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei104 – 1041GTP; via amide nitrogenBy similarity
Binding sitei239 – 2391GTP; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei254 – 2541GTPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi49 – 568GTPBy similarity
Nucleotide bindingi185 – 1939GTPBy similarity

GO - Molecular functioni

  1. GTP binding Source: UniProtKB-KW

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. cell division Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Septin-6
Gene namesi
Name:Sept6
Synonyms:Kiaa0128
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome X

Organism-specific databases

MGIiMGI:1888939. Sept6.

Subcellular locationi

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).By similarity

GO - Cellular componenti

  1. axon terminus Source: MGI
  2. kinetochore Source: UniProtKB-KW
  3. septin complex Source: InterPro
  4. synaptic vesicle Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 434433Septin-6PRO_0000173526Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei367 – 3671N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9R1T4.
PaxDbiQ9R1T4.
PRIDEiQ9R1T4.

PTM databases

PhosphoSiteiQ9R1T4.

Expressioni

Tissue specificityi

Associated with synaptic vesicles in various brain regions, including glomeruli of the olfactory bulb.1 Publication

Gene expression databases

BgeeiQ9R1T4.
CleanExiMM_SEPT6.
ExpressionAtlasiQ9R1T4. baseline and differential.
GenevestigatoriQ9R1T4.

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

BioGridi208037. 4 interactions.
IntActiQ9R1T4. 3 interactions.
MINTiMINT-4134187.

Structurei

3D structure databases

ProteinModelPortaliQ9R1T4.
SMRiQ9R1T4. Positions 41-307.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini39 – 305267Septin-type GAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili321 – 40787Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG5019.
GeneTreeiENSGT00760000118899.
HOVERGENiHBG065093.
InParanoidiQ9R1T4.
KOiK16939.
OMAiNHGFCFN.
OrthoDBiEOG7J9VQK.
PhylomeDBiQ9R1T4.
TreeFamiTF101080.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR000038. Cell_div_GTP-bd.
IPR027417. P-loop_NTPase.
IPR016491. Septin.
[Graphical view]
PANTHERiPTHR18884. PTHR18884. 1 hit.
PfamiPF00735. Septin. 1 hit.
[Graphical view]
PIRSFiPIRSF006698. Septin. 1 hit.
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS51719. G_SEPTIN. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Note: Additional isoforms seem to exist.

Isoform II (identifier: Q9R1T4-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MAAADIARQV GEDCRTVPLA GHVGFDSLPD QLVNKSVSQG FCFNILCVGE
60 70 80 90 100
TGLGKSTLMD TLFNTKFEGE PATHTQPGVQ LQSNTYDLQE SNVGLKLTIV
110 120 130 140 150
STVGFGDQIN KEDSYKPIVE FIDAQFEAYL QEELKIRRVL HSYHDSRIHV
160 170 180 190 200
CLYFIAPTGH SLKSLDLVTM KKLDSKVNII PVIAKSDAIS KSELAKFKIK
210 220 230 240 250
ITSELVSNGV QIYQFPTDDE SVSEINGTMN AHLPFAVVGS TEEVKIGNKM
260 270 280 290 300
MRARQYPWGT VQVENEAHCD FVKLREMLIR VNMEDLREQT HARHYELYRR
310 320 330 340 350
CKLEEMGFKD TDPDSKPFSL QETYEAKRNE FLGELQKKEE EMRQMFVQRV
360 370 380 390 400
KEKEAELKEA EKELHEKFDR LKKLHQEEKK KLEDKKKCLD EEMNAFKQRK
410 420 430
AAAELLQSQG SQAGGSQTLK RDKEKKNNPW LCIE
Length:434
Mass (Da):49,620
Last modified:January 23, 2007 - v4
Checksum:i33DCD4F44607168A
GO
Isoform I (identifier: Q9R1T4-2) [UniParc]FASTAAdd to Basket

Also known as: III

The sequence of this isoform differs from the canonical sequence as follows:
     428-434: Missing.

Show »
Length:427
Mass (Da):48,764
Checksum:i6A6315BB1E6B24C4
GO
Isoform V (identifier: Q9R1T4-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:429
Mass (Da):49,058
Checksum:i59BB0A6315BB1E6B
GO

Sequence cautioni

The sequence BAD32172.1 differs from that shown. Reason: Erroneous initiation.
The sequence CAM19782.1 differs from that shown. Reason: Erroneous gene model prediction.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti10 – 101V → L in BAB28516. (PubMed:16141072)Curated
Sequence conflicti10 – 101Missing in BAC33342. (PubMed:16141072)Curated
Sequence conflicti62 – 621L → P in BAC40335. (PubMed:16141072)Curated
Sequence conflicti141 – 1411H → Y in BAA82838. 1 PublicationCurated
Sequence conflicti170 – 1701M → I in BAE36069. (PubMed:16141072)Curated
Sequence conflicti238 – 2392VG → C in BAB28516. (PubMed:16141072)Curated
Sequence conflicti350 – 3501V → A in BAC40335. (PubMed:16141072)Curated
Sequence conflicti403 – 4031A → R in BAA82838. 1 PublicationCurated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei428 – 4347Missing in isoform I. 1 PublicationVSP_006055
Alternative sequencei428 – 4347NPWLCIE → FF in isoform V. 2 PublicationsVSP_006056

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS30066.1. [Q9R1T4-3]
CCDS53051.1. [Q9R1T4-1]
CCDS57749.1. [Q9R1T4-2]
RefSeqiNP_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]
UniGeneiMm.260036.
Mm.470184.

Genome annotation databases

EnsembliENSMUST00000053456; ENSMUSP00000054034; ENSMUSG00000050379. [Q9R1T4-2]
ENSMUST00000060474; ENSMUSP00000062014; ENSMUSG00000050379. [Q9R1T4-3]
ENSMUST00000115239; ENSMUSP00000110894; ENSMUSG00000050379. [Q9R1T4-1]
GeneIDi56526.
KEGGimmu:56526.
UCSCiuc009sxx.2. mouse. [Q9R1T4-3]
uc009sxz.2. mouse. [Q9R1T4-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSi CCDS30066.1. [Q9R1T4-3 ]
CCDS53051.1. [Q9R1T4-1 ]
CCDS57749.1. [Q9R1T4-2 ]
RefSeqi NP_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 ]
UniGenei Mm.260036.
Mm.470184.

3D structure databases

ProteinModelPortali Q9R1T4.
SMRi Q9R1T4. Positions 41-307.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 208037. 4 interactions.
IntActi Q9R1T4. 3 interactions.
MINTi MINT-4134187.

PTM databases

PhosphoSitei Q9R1T4.

Proteomic databases

MaxQBi Q9R1T4.
PaxDbi Q9R1T4.
PRIDEi Q9R1T4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000053456 ; ENSMUSP00000054034 ; ENSMUSG00000050379 . [Q9R1T4-2 ]
ENSMUST00000060474 ; ENSMUSP00000062014 ; ENSMUSG00000050379 . [Q9R1T4-3 ]
ENSMUST00000115239 ; ENSMUSP00000110894 ; ENSMUSG00000050379 . [Q9R1T4-1 ]
GeneIDi 56526.
KEGGi mmu:56526.
UCSCi uc009sxx.2. mouse. [Q9R1T4-3 ]
uc009sxz.2. mouse. [Q9R1T4-1 ]

Organism-specific databases

CTDi 23157.
MGIi MGI:1888939. Sept6.
Rougei Search...

Phylogenomic databases

eggNOGi COG5019.
GeneTreei ENSGT00760000118899.
HOVERGENi HBG065093.
InParanoidi Q9R1T4.
KOi K16939.
OMAi NHGFCFN.
OrthoDBi EOG7J9VQK.
PhylomeDBi Q9R1T4.
TreeFami TF101080.

Miscellaneous databases

ChiTaRSi SEPT6. mouse.
NextBioi 312866.
PROi Q9R1T4.
SOURCEi Search...

Gene expression databases

Bgeei Q9R1T4.
CleanExi MM_SEPT6.
ExpressionAtlasi Q9R1T4. baseline and differential.
Genevestigatori Q9R1T4.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
InterProi IPR000038. Cell_div_GTP-bd.
IPR027417. P-loop_NTPase.
IPR016491. Septin.
[Graphical view ]
PANTHERi PTHR18884. PTHR18884. 1 hit.
Pfami PF00735. Septin. 1 hit.
[Graphical view ]
PIRSFi PIRSF006698. Septin. 1 hit.
SUPFAMi SSF52540. SSF52540. 1 hit.
PROSITEi PS51719. G_SEPTIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiSEPT6_MOUSE
AccessioniPrimary (citable) accession number: Q9R1T4
Secondary accession number(s): A2A3V9
, A2A3W0, Q3TRH9, Q3TUA2, Q542H3, Q6A0C4, Q8C2L2, Q8C848, Q91XH2, Q9CZ94
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 129 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Coordinated expression with SEPT2 and SEPT7.By similarity

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3