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Q14141 (SEPT6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Septin-6
Gene names
Name:SEPT6
Synonyms:KIAA0128, SEP2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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. May play a role in HCV RNA replication. Ref.10 Ref.12

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 HCV NS5B and with HNRNPA1. Ref.9 Ref.10 Ref.11 Ref.12 Ref.15 Ref.18

Subcellular location

Cytoplasm. Cytoplasmcytoskeletonspindle. Chromosomecentromerekinetochore. Cleavage furrow. Midbody. 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. Ref.8

Tissue specificity

Widely expressed. Ref.6

Miscellaneous

Coordinated expression with SEPT2 and SEPT7.

Sequence similarities

Belongs to the septin family.

Binary interactions

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform II (identifier: Q14141-1)

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: Q14141-2)

Also known as: III;

The sequence of this isoform differs from the canonical sequence as follows:
     428-434: Missing.
Isoform IV (identifier: Q14141-3)

The sequence of this isoform differs from the canonical sequence as follows:
     263-267: VENEA → AAREV
     268-434: Missing.
Isoform V (identifier: Q14141-4)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 434433Septin-6
PRO_0000173525

Regions

Nucleotide binding49 – 568GTP
Nucleotide binding185 – 1939GTP
Coiled coil321 – 40989 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 Ref.4 Ref.14
Modified residue3671N6-acetyllysine Ref.16

Natural variations

Alternative sequence263 – 2675VENEA → AAREV in isoform IV.
VSP_006051
Alternative sequence268 – 434167Missing in isoform IV.
VSP_006052
Alternative sequence428 – 4347Missing in isoform I.
VSP_006053
Alternative sequence428 – 4347NPWLCTE → FF in isoform V.
VSP_006054

Experimental info

Sequence conflict4061L → P in AAH09291. Ref.3

Secondary structure

.................................. 434
Helix Strand Turn

Details...

Sequences

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

Last modified January 23, 2007. Version 4.
Checksum: E684AE6A93B32362

FASTA43449,717
        10         20         30         40         50         60 
MAATDIARQV GEGCRTVPLA GHVGFDSLPD QLVNKSVSQG FCFNILCVGE TGLGKSTLMD 

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

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

       190        200        210        220        230        240 
PIIAKADAIS KSELTKFKIK ITSELVSNGV QIYQFPTDDE SVAEINGTMN AHLPFAVIGS 

       250        260        270        280        290        300 
TEELKIGNKM MRARQYPWGT VQVENEAHCD FVKLREMLIR VNMEDLREQT HTRHYELYRR 

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

       370        380        390        400        410        420 
EKELHEKFDR LKKLHQDEKK KLEDKKKSLD DEVNAFKQRK TAAELLQSQG SQAGGSQTLK 

       430 
RDKEKKNNPW LCTE 

« Hide

Isoform I (III) [UniParc].

Checksum: 62EB88E308386ADE
Show »

FASTA42748,873
Isoform IV [UniParc].

Checksum: 7DD6D37AE3844845
Show »

FASTA26729,584
Isoform V [UniParc].

Checksum: 3D8EE2EB88E30838
Show »

FASTA42949,167

References

« Hide 'large scale' references
[1]"SEPTIN6, a human homologue to mouse Septin6, is fused to MLL in infant acute myeloid leukemia with complex chromosomal abnormalities involving 11q23 and Xq24."
Ono R., Taki T., Taketani T., Kawaguchi H., Taniwaki M., Okamura T., Kawa K., Hanada R., Kobayashi M., Hayashi Y.
Cancer Res. 62:333-337(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS I; II; IV AND V).
[2]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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] (ISOFORMS II AND V).
Tissue: Muscle, Placenta and Testis.
[4]"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-8, ACETYLATION AT ALA-2.
Tissue: Platelet.
[5]"Prediction of the coding sequences of unidentified human genes. IV. The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of cDNA clones from human cell line KG-1."
Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.
DNA Res. 2:167-174(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-427 (ISOFORM I).
Tissue: Bone marrow.
[6]"Expression profiling the human septin gene family."
Hall P.A., Jung K., Hillan K.J., Russell S.E.H.
J. Pathol. 206:269-278(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[7]"Mammalian septins regulate microtubule stability through interaction with the microtubule-binding protein MAP4."
Kremer B.E., Haystead T., Macara I.G.
Mol. Biol. Cell 16:4648-4659(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: COORDINATED EXPRESSION WITH SEPT2 AND SEPT7.
[8]"A mitotic septin scaffold required for mammalian chromosome congression and segregation."
Spiliotis E.T., Kinoshita M., Nelson W.J.
Science 307:1781-1785(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[9]"Structural analysis of septin 2, 6, and 7 complexes."
Low C., Macara I.G.
J. Biol. Chem. 281:30697-30706(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SEPT2 AND SEPT7.
[10]"Septins regulate actin organization and cell-cycle arrest through nuclear accumulation of NCK mediated by SOCS7."
Kremer B.E., Adang L.A., Macara I.G.
Cell 130:837-850(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SOCS7.
[11]"SEPT12 interacts with SEPT6 and this interaction alters the filament structure of SEPT6 in Hela cells."
Ding X., Yu W., Liu M., Shen S., Chen F., Wan B., Yu L.
J. Biochem. Mol. Biol. 40:973-978(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SEPT12.
[12]"An RNA-binding protein, hnRNP A1, and a scaffold protein, septin 6, facilitate hepatitis C virus replication."
Kim C.S., Seol S.K., Song O.-K., Park J.H., Jang S.K.
J. Virol. 81:3852-3865(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HNRNPA1 AND HCV NS5B, FUNCTION.
[13]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[14]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Septins regulate bacterial entry into host cells."
Mostowy S., Nam Tham T., Danckaert A., Guadagnini S., Boisson-Dupuis S., Pizarro-Cerda J., Cossart P.
PLoS ONE 4:E4196-E4196(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SEPT9.
[16]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-367, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"Structural insight into filament formation by mammalian septins."
Sirajuddin M., Farkasovsky M., Hauer F., Kuehlmann D., Macara I.G., Weyand M., Stark H., Wittinghofer A.
Nature 449:311-315(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) OF 1-427 IN COMPLEX WITH GTP, ELECTRON MICROSCOPY OF SEPTIN COMPLEX, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF403058 mRNA. Translation: AAK98547.1.
AF403059 mRNA. Translation: AAK98548.1.
AF403060 mRNA. Translation: AAK98549.1.
AF403061 mRNA. Translation: AAK98550.1.
AF403062 mRNA. Translation: AAK98551.1.
AL355348, AC004913, AC005052 Genomic DNA. Translation: CAI41426.1.
BC009291 mRNA. Translation: AAH09291.1.
BC011922 mRNA. Translation: AAH11922.3.
BC036240 mRNA. Translation: AAH36240.1.
D50918 mRNA. Translation: BAA09477.1.
RefSeqNP_055944.2. NM_015129.5.
NP_665798.1. NM_145799.3.
NP_665799.1. NM_145800.3.
NP_665801.1. NM_145802.3.
UniGeneHs.496666.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2QAGX-ray4.00B1-427[»]
ProteinModelPortalQ14141.
SMRQ14141. Positions 39-304.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116770. 13 interactions.
DIPDIP-38218N.
IntActQ14141. 8 interactions.
MINTMINT-4532787.
STRING9606.ENSP00000341524.

PTM databases

PhosphoSiteQ14141.

Polymorphism databases

DMDM20178343.

2D gel databases

OGPQ14141.

Proteomic databases

PaxDbQ14141.
PeptideAtlasQ14141.
PRIDEQ14141.

Protocols and materials databases

DNASU23157.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000343984; ENSP00000341524; ENSG00000125354. [Q14141-1]
ENST00000354228; ENSP00000346169; ENSG00000125354. [Q14141-4]
ENST00000360156; ENSP00000353278; ENSG00000125354. [Q14141-2]
ENST00000394610; ENSP00000378108; ENSG00000125354. [Q14141-2]
ENST00000460411; ENSP00000435818; ENSG00000125354. [Q14141-3]
ENST00000489216; ENSP00000418715; ENSG00000125354. [Q14141-2]
GeneID23157.
KEGGhsa:23157.
UCSCuc004ers.3. human. [Q14141-1]

Organism-specific databases

CTD23157.
GeneCardsGC0XM118750.
HGNCHGNC:15848. SEPT6.
HPAHPA005665.
MIM300683. gene.
neXtProtNX_Q14141.
PharmGKBPA134941944.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5019.
HOVERGENHBG065093.
KOK16939.
OrthoDBEOG7J9VQK.
PhylomeDBQ14141.
TreeFamTF101080.

Gene expression databases

ArrayExpressQ14141.
BgeeQ14141.
CleanExHS_SEPT6.
GenevestigatorQ14141.

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.
ProtoNetSearch...

Other

ChiTaRSSEPT6. human.
EvolutionaryTraceQ14141.
GeneWikiSEPT6.
GenomeRNAi23157.
NextBio44499.
PROQ14141.
SOURCESearch...

Entry information

Entry nameSEPT6_HUMAN
AccessionPrimary (citable) accession number: Q14141
Secondary accession number(s): Q5JTK0 expand/collapse secondary AC list , Q969W5, Q96A13, Q96GR1, Q96P86, Q96P87
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 129 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM