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Q9NVA2 (SEP11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Septin-11
Gene names
Name:SEPT11
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length429 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. 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

Cytoplasmcytoskeleton. Cell junctionsynapse. Cell projectiondendritic spine. Cell projectionaxon 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 KMT2A/MLL1.

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 BAB55250.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAB53741.2 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SEPT5Q997196EBI-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 429428Septin-11
PRO_0000173542

Regions

Domain38 – 304267Septin-type G
Nucleotide binding48 – 558GTP By similarity
Nucleotide binding184 – 1929GTP By similarity
Coiled coil320 – 41596 Potential

Sites

Binding site1031GTP; via amide nitrogen By similarity
Binding site2381GTP; via amide nitrogen and carbonyl oxygen By similarity
Binding site2531GTP By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.7

Natural variations

Alternative sequence1 – 99MAVAVGRPS → MEERKPAHVLRSFKYAAFM in isoform 2.
VSP_038320

Experimental info

Mutagenesis481G → A: High reduction in GTPase activity. No effect on GTP-binding. Loss of filament formation. Ref.9
Sequence conflict1421Y → H in CAB53741. Ref.5
Sequence conflict2981R → H in CAB53741. Ref.5
Sequence conflict3211E → G in CAB53741. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: D467F1F315FFD028

FASTA42949,398
        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 

« Hide

Isoform 2 [UniParc].

Checksum: C8E82F016C56A392
Show »

FASTA43950,823

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY 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 KMT2A/MLL1.
[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.
CCDSCCDS34018.1. [Q9NVA2-1]
RefSeqNP_060713.1. NM_018243.2. [Q9NVA2-1]
XP_005263177.1. XM_005263120.1. [Q9NVA2-2]
UniGeneHs.128199.

3D structure databases

ProteinModelPortalQ9NVA2.
SMRQ9NVA2. Positions 18-306.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120870. 32 interactions.
IntActQ9NVA2. 2 interactions.
MINTMINT-3074824.
STRING9606.ENSP00000264893.

PTM databases

PhosphoSiteQ9NVA2.

Polymorphism databases

DMDM50401687.

2D gel databases

OGPQ9NVA2.
UCD-2DPAGEQ9NVA2.

Proteomic databases

MaxQBQ9NVA2.
PaxDbQ9NVA2.
PeptideAtlasQ9NVA2.
PRIDEQ9NVA2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000264893; ENSP00000264893; ENSG00000138758. [Q9NVA2-1]
ENST00000510515; ENSP00000422896; ENSG00000138758. [Q9NVA2-2]
ENST00000541121; ENSP00000443701; ENSG00000138758. [Q9NVA2-2]
GeneID55752.
KEGGhsa:55752.
UCSCuc003hkj.3. human. [Q9NVA2-1]
uc010ijh.1. human. [Q9NVA2-2]

Organism-specific databases

CTD55752.
GeneCardsGC04P077870.
HGNCHGNC:25589. SEPT11.
HPAHPA003459.
HPA005665.
MIM612887. gene.
neXtProtNX_Q9NVA2.
PharmGKBPA128394688.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5019.
HOGENOMHOG000233586.
HOVERGENHBG065093.
InParanoidQ9NVA2.
KOK16939.
OMAEVSNFQK.
OrthoDBEOG7J9VQK.
PhylomeDBQ9NVA2.
TreeFamTF101080.

Gene expression databases

ArrayExpressQ9NVA2.
BgeeQ9NVA2.
CleanExHS_SEPT11.
GenevestigatorQ9NVA2.

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

ChiTaRSSEPT11. human.
GeneWikiSEPT11.
GenomeRNAi55752.
NextBio60745.
PROQ9NVA2.
SOURCESearch...

Entry information

Entry nameSEP11_HUMAN
AccessionPrimary (citable) accession number: Q9NVA2
Secondary accession number(s): B7Z7Z6 expand/collapse secondary AC list , E9KL32, Q4W5G1, Q7L4N1, Q96SP1, Q9UFY9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 115 of the entry and version 3 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

MIM cross-references

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

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM