Q14141 (SEPT6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Septin-6

Gene names

Name:	SEPT6
Synonyms:	KIAA0128, SEP2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	434 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.14 Ref.17
Subcellular location	Cytoplasm. Cytoplasm › cytoskeleton › spindle. Chromosome › centromere › kinetochore. 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.

Ontologies

Keywords
Biological process	Cell cycle Cell division Host-virus interaction
Cellular component	Centromere Chromosome Cytoplasm Cytoskeleton Kinetochore
Coding sequence diversity	Alternative splicing
Domain	Coiled coil
Ligand	GTP-binding Nucleotide-binding
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cytokinesis Traceable author statement Ref.1. Source: UniProtKB virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	axon terminus Inferred from electronic annotation. Source: Compara cleavage furrow Inferred from electronic annotation. Source: UniProtKB-SubCell condensed chromosome kinetochore Inferred from electronic annotation. Source: UniProtKB-SubCell cytoplasm Inferred from direct assay. Source: HPA midbody Inferred from electronic annotation. Source: UniProtKB-SubCell septin complex Inferred from electronic annotation. Source: InterPro spindle Inferred from electronic annotation. Source: UniProtKB-SubCell synaptic vesicle Inferred from electronic annotation. Source: Compara
Molecular_function	GTP binding Traceable author statement Ref.1. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SEPT12	Q8IYM1	3	EBI-745901,EBI-2585067
SEPT2	Q15019	4	EBI-745901,EBI-741220
SOCS7	O14512-1	2	EBI-745901,EBI-1539617

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.4

Chain

2 – 434

433

Septin-6

PRO_0000173525

Regions

Nucleotide binding

49 – 56

8

GTP

Nucleotide binding

185 – 193

9

GTP

Coiled coil

321 – 409

89

Potential

Sites

Binding site

104

1

GTP; via amide nitrogen By similarity

Binding site

239

1

GTP; via amide nitrogen and carbonyl oxygen By similarity

Binding site

254

1

GTP By similarity

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.4

Modified residue

367

1

N6-acetyllysine Ref.15

Modified residue

416

1

Phosphoserine By similarity

Natural variations

Alternative sequence

263 – 267

5

VENEA → AAREV in isoform IV.

VSP_006051

Alternative sequence

268 – 434

167

Missing in isoform IV.

VSP_006052

Alternative sequence

428 – 434

7

Missing in isoform I.

VSP_006053

Alternative sequence

428 – 434

7

NPWLCTE → FF in isoform V.

VSP_006054

Experimental info

Sequence conflict

406

1

L → P in AAH09291. Ref.3

Secondary structure

1

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434

Helix Strand Turn

Details...

Helix

30 – 35

6

Beta strand

42 – 48

7

Helix

56 – 63

8

Beta strand

80 – 89

10

Beta strand

94 – 103

10

Helix

111 – 114

4

Helix

116 – 132

17

Beta strand

150 – 155

6

Helix

164 – 172

9

Beta strand

177 – 184

8

Helix

186 – 188

3

Helix

191 – 205

15

Turn

229 – 231

3

Helix

272 – 280

9

Helix

285 – 293

9

Helix

296 – 303

8

Turn

304 – 306

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform II [UniParc]. Last modified January 23, 2007. Version 4. Checksum: E684AE6A93B32362	FASTA	434	49,717
	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
	Isoform I (III) [UniParc]. Checksum: 62EB88E308386ADE	FASTA	427	48,873
	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 RDKEKKN
	Isoform IV [UniParc]. Checksum: 7DD6D37AE3844845	FASTA	267	29,584
	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 TEELKIGNKM MRARQYPWGT VQAAREV
	Isoform V [UniParc]. Checksum: 3D8EE2EB88E30838	FASTA	429	49,167
	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 RDKEKKNFF

References

	« Hide 'large scale' referencesShow '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. , 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]	"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.
[15]	"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, MASS SPECTROMETRY.
[16]	"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].
[17]	"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.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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.

IPI

IPI00216139.
IPI00376992.
IPI00744597.
IPI00941331.

RefSeq

NP_055944.2. NM_015129.5.
NP_665798.1. NM_145799.3.
NP_665799.1. NM_145800.3.
NP_665801.1. NM_145802.3.

UniGene

Hs.496666.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2QAG	X-ray	4.00	B	1-427	[»]

ProteinModelPortal

Q14141.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q14141. 5 interactions.

STRING

9606.ENSP00000341524.

PTM databases

PhosphoSite

Q14141.

Polymorphism databases

DMDM

20178343.

2D gel databases

OGP

Q14141.

Proteomic databases

PaxDb

Q14141.

PeptideAtlas

Q14141.

PRIDE

Q14141.

Protocols and materials databases

DNASU

23157.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000343984; ENSP00000341524; ENSG00000125354.
ENST00000354228; ENSP00000346169; ENSG00000125354.
ENST00000360156; ENSP00000353278; ENSG00000125354.
ENST00000394610; ENSP00000378108; ENSG00000125354.
ENST00000460411; ENSP00000435818; ENSG00000125354.
ENST00000489216; ENSP00000418715; ENSG00000125354.

GeneID

23157.

KEGG

hsa:23157.

UCSC

uc004ers.3. human.

Organism-specific databases

CTD

23157.

GeneCards

GC0XM118750.

HGNC

HGNC:15848. SEPT6.

HPA

HPA005665.

MIM

300683. gene.

neXtProt

NX_Q14141.

PharmGKB

PA134941944.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5019.

HOVERGEN

HBG065093.

PhylomeDB

Q14141.

Gene expression databases

ArrayExpress

Q14141.

Bgee

Q14141.

CleanEx

HS_SEPT6.

Genevestigator

Q14141.

GermOnline

ENSG00000125354. Homo sapiens.

Family and domain databases

InterPro

IPR000038. Cell_div_GTP-bd.
IPR016491. Septin.
[Graphical view]

PANTHER

PTHR18884. PTHR18884. 1 hit.

Pfam

PF00735. Septin. 1 hit.
[Graphical view]

PIRSF

PIRSF006698. Septin. 1 hit.

ProtoNet

Search...

Other

ChiTaRS

SEPT6. human.

EvolutionaryTrace

Q14141.

GenomeRNAi

23157.

NextBio

44499.

SOURCE

Search...

Entry information

Entry name

SEPT6_HUMAN

Accession

Primary (citable) accession number: Q14141
Secondary accession number(s): Q5JTK0 , Q969W5, Q96A13, Q96GR1, Q96P86, Q96P87

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 119 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.