Q9NVA2 (SEP11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Septin-11

Gene names

Name:

SEPT11

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	429 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. May play a role in cytokinesis Potential. May play a role in the cytoarchitecture of neurons, including dendritic arborization and dendritic spines, and in GABAergic synaptic connectivity By similarity. During Listeria monocytogenes infection, not required for the bacterial entry process, but restricts its efficacy. Ref.9 Ref.15
Subunit structure	Septins polymerize into heterooligomeric protein complexes that form filaments, and can associate with cellular membranes, actin filaments and microtubules. GTPase activity is required for filament formation. Interacts with SEPT7, SEPT9 and SEPT12. Forms homooligomers. Ref.10 Ref.14 Ref.16
Subcellular location	Cytoplasm › cytoskeleton. Cell junction › synapse. Cell projection › dendritic spine. Cell projection › axon By similarity. Note: Partly colocalizes with stress fibers and microtubules. During bacterial infection, displays a collar shape structure next to actin at the pole of invading bacteria. Ref.9 Ref.13 Ref.16
Tissue specificity	Widely expressed, except in leukocytes. Ref.9 Ref.12
Involvement in disease	A chromosomal aberration involving SEPT11 may be a cause of chronic neutrophilic leukemia. Translocation t(4;11)(q21;q23) with MLL/HRX.
Sequence similarities	Belongs to the septin family.
Sequence caution	The sequence BAB55250.1 differs from that shown. Reason: Erroneous initiation. The sequence CAB53741.2 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

Ontologies

Keywords
Biological process	Cell cycle Cell division
Cellular component	Cell junction Cell projection Cytoplasm Cytoskeleton Synapse
Coding sequence diversity	Alternative splicing Chromosomal rearrangement
Domain	Coiled coil
Ligand	GTP-binding Nucleotide-binding
PTM	Acetylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from electronic annotation. Source: UniProtKB-KW protein heterooligomerization Inferred from direct assay Ref.10. Source: UniProtKB
Cellular_component	axon Inferred from electronic annotation. Source: UniProtKB-SubCell cell junction Inferred from electronic annotation. Source: UniProtKB-KW cytoplasm Inferred from direct assay. Source: HPA dendritic spine Inferred from electronic annotation. Source: UniProtKB-SubCell septin complex Inferred from electronic annotation. Source: InterPro stress fiber Inferred from direct assay Ref.10. Source: UniProtKB synapse Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SEPT5	Q99719	6	EBI-957999,EBI-373345

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9NVA2-1)

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: Q9NVA2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-9: MAVAVGRPS → MEERKPAHVLRSFKYAAFM

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.7
	Chain	2 – 429	428	Septin-11		PRO_0000173542
Regions
	Nucleotide binding	48 – 55	8	GTP By similarity
	Nucleotide binding	184 – 192	9	GTP By similarity
	Coiled coil	320 – 415	96	Potential
Sites
	Binding site	103	1	GTP; via amide nitrogen By similarity
	Binding site	238	1	GTP; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	253	1	GTP By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.7
Natural variations
	Alternative sequence	1 – 9	9	MAVAVGRPS → MEERKPAHVLRSFKYAAFM in isoform 2.		VSP_038320
Experimental info
	Mutagenesis	48	1	G → A: High reduction in GTPase activity. No effect on GTP-binding. Loss of filament formation. Ref.9
	Sequence conflict	142	1	Y → H in CAB53741. Ref.5
	Sequence conflict	298	1	R → H in CAB53741. Ref.5
	Sequence conflict	321	1	E → G in CAB53741. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: D467F1F315FFD028	FASTA	429	49,398
	10 20 30 40 50 60 MAVAVGRPSN EELRNLSLSG HVGFDSLPDQ LVNKSTSQGF CFNILCVGET GIGKSTLMDT 70 80 90 100 110 120 LFNTKFESDP ATHNEPGVRL KARSYELQES NVRLKLTIVD TVGFGDQINK DDSYKPIVEY 130 140 150 160 170 180 IDAQFEAYLQ EELKIKRSLF NYHDTRIHAC LYFIAPTGHS LKSLDLVTMK KLDSKVNIIP 190 200 210 220 230 240 IIAKADTIAK NELHKFKSKI MSELVSNGVQ IYQFPTDEET VAEINATMSV HLPFAVVGST 250 260 270 280 290 300 EEVKIGNKMA KARQYPWGVV QVENENHCDF VKLREMLIRV NMEDLREQTH TRHYELYRRC 310 320 330 340 350 360 KLEEMGFKDT DPDSKPFSLQ ETYEAKRNEF LGELQKKEEE MRQMFVMRVK EKEAELKEAE 370 380 390 400 410 420 KELHEKFDLL KRTHQEEKKK VEDKKKELEE EVNNFQKKKA AAQLLQSQAQ QSGAQQTKKD KDKKNASFT
	Isoform 2 [UniParc]. Checksum: C8E82F016C56A392	FASTA	439	50,823
	10 20 30 40 50 60 MEERKPAHVL RSFKYAAFMN EELRNLSLSG HVGFDSLPDQ LVNKSTSQGF CFNILCVGET 70 80 90 100 110 120 GIGKSTLMDT LFNTKFESDP ATHNEPGVRL KARSYELQES NVRLKLTIVD TVGFGDQINK 130 140 150 160 170 180 DDSYKPIVEY IDAQFEAYLQ EELKIKRSLF NYHDTRIHAC LYFIAPTGHS LKSLDLVTMK 190 200 210 220 230 240 KLDSKVNIIP IIAKADTIAK NELHKFKSKI MSELVSNGVQ IYQFPTDEET VAEINATMSV 250 260 270 280 290 300 HLPFAVVGST EEVKIGNKMA KARQYPWGVV QVENENHCDF VKLREMLIRV NMEDLREQTH 310 320 330 340 350 360 TRHYELYRRC KLEEMGFKDT DPDSKPFSLQ ETYEAKRNEF LGELQKKEEE MRQMFVMRVK 370 380 390 400 410 420 EKEAELKEAE KELHEKFDLL KRTHQEEKKK VEDKKKELEE EVNNFQKKKA AAQLLQSQAQ 430 QSGAQQTKKD KDKKNASFT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Systematic mapping and functional analysis of a family of human epididymal secretory sperm-located proteins." Li J., Liu F., Wang H., Liu X., Liu J., Li N., Wan F., Wang W., Zhang C., Jin S., Liu J., Zhu P., Liu Y. Mol. Cell. Proteomics 9:2517-2528(2010) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Epididymis.
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Teratocarcinoma and Testis.
[3]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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). Tissue: Colon and Skin.
[6]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-337. Tissue: Fetal kidney.
[7]	"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 2-14 (ISOFORM 1), ACETYLATION AT ALA-2. Tissue: Platelet.
[8]	Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 15-34; 55-79; 84-93; 96-110; 176-184; 309-336; 387-397 AND 400-418, MASS SPECTROMETRY. Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[9]	"Biochemical and cell biological characterization of a mammalian septin, Sept11." Hanai N., Nagata K., Kawajiri A., Shiromizu T., Saitoh N., Hasegawa Y., Murakami S., Inagaki M. FEBS Lett. 568:83-88(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF GLY-48, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[10]	"Biochemical and cell biological analyses of a mammalian septin complex, Sept7/9b/11." Nagata K., Asano T., Nozawa Y., Inagaki M. J. Biol. Chem. 279:55895-55904(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SEPT7 AND SEPT9.
[11]	"FLJ10849, a septin family gene, fuses MLL in a novel leukemia cell line CNLBC1 derived from chronic neutrophilic leukemia in transformation with t(4;11)(q21;q23)." Kojima K., Sakai I., Hasegawa A., Niiya H., Azuma T., Matsuo Y., Fujii N., Tanimoto M., Fujita S. Leukemia 18:998-1005(2004) [PubMed] [Europe PMC] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH MLL/HRX.
[12]	"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.
[13]	"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.
[14]	"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.
[15]	"Septin 11 restricts InlB-mediated invasion by Listeria." Mostowy S., Danckaert A., Tham T.N., Machu C., Guadagnini S., Pizarro-Cerda J., Cossart P. J. Biol. Chem. 284:11613-11621(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ROLE IN BACTERIAL INFECTION.
[16]	"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, SUBCELLULAR LOCATION.
[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].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	GU727629 mRNA. Translation: ADU87631.1. AK001711 mRNA. Translation: BAA91853.1. AK027633 mRNA. Translation: BAB55250.1. Different initiation. AK302700 mRNA. Translation: BAH13782.1. AC104687 Genomic DNA. Translation: AAY40922.1. AC111196 Genomic DNA. No translation available. CH471057 Genomic DNA. Translation: EAX05805.1. BC008083 mRNA. Translation: AAH08083.3. BC063615 mRNA. Translation: AAH63615.1. AL110300 mRNA. Translation: CAB53741.2. Sequence problems.
IPI	IPI00019376. IPI00952909.
RefSeq	NP_060713.1. NM_018243.2.
UniGene	Hs.128199.
3D structure databases
ProteinModelPortal	Q9NVA2.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9NVA2. 2 interactions.
STRING	9606.ENSP00000264893.
PTM databases
PhosphoSite	Q9NVA2.
Polymorphism databases
DMDM	50401687.
2D gel databases
OGP	Q9NVA2.
UCD-2DPAGE	Q9NVA2.
Proteomic databases
PaxDb	Q9NVA2.
PeptideAtlas	Q9NVA2.
PRIDE	Q9NVA2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000264893; ENSP00000264893; ENSG00000138758. ENST00000510515; ENSP00000422896; ENSG00000138758. ENST00000541121; ENSP00000443701; ENSG00000138758.
GeneID	55752.
KEGG	hsa:55752.
UCSC	uc003hkj.3. human. uc010ijh.1. human.
Organism-specific databases
CTD	55752.
GeneCards	GC04P077870.
HGNC	HGNC:25589. SEPT11.
HPA	HPA003459. HPA005665.
MIM	612887. gene.
neXtProt	NX_Q9NVA2.
PharmGKB	PA128394688.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5019.
HOGENOM	HOG000233586.
HOVERGEN	HBG065093.
InParanoid	Q9NVA2.
OMA	AFMNEEL.
OrthoDB	EOG4320Z8.
Gene expression databases
ArrayExpress	Q9NVA2.
Bgee	Q9NVA2.
CleanEx	HS_SEPT11.
Genevestigator	Q9NVA2.
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	SEPT11. human.
GenomeRNAi	55752.
NextBio	60745.
SOURCE	Search...

Entry information

Entry name

SEP11_HUMAN

Accession

Primary (citable) accession number: Q9NVA2
Secondary accession number(s): B7Z7Z6 , E9KL32, Q4W5G1, Q7L4N1, Q96SP1, Q9UFY9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 103 of the entry and version 3 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.