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Protein

Septin-11

Gene

SEPT11

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.By similarityCurated2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei103GTP; via amide nitrogenBy similarity1
Binding sitei238GTP; via amide nitrogen and carbonyl oxygenBy similarity1
Binding sitei253GTPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi48 – 55GTPBy similarity8
Nucleotide bindingi184 – 192GTPBy similarity9

GO - Molecular functioni

GO - Biological processi

  • cell cycle Source: UniProtKB-KW
  • cell division Source: UniProtKB-KW
  • protein heterooligomerization Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Septin-11
Gene namesi
Name:SEPT11
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:25589. SEPT11.

Subcellular locationi

GO - Cellular componenti

  • axon Source: UniProtKB-SubCell
  • cell junction Source: UniProtKB-KW
  • cytoplasm Source: UniProtKB-KW
  • dendritic spine Source: UniProtKB-SubCell
  • extracellular exosome Source: UniProtKB
  • stress fiber Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell projection, Cytoplasm, Cytoskeleton, Synapse

Pathology & Biotechi

Involvement in diseasei

A chromosomal aberration involving SEPT11 may be a cause of chronic neutrophilic leukemia. Translocation t(4;11)(q21;q23) with KMT2A/MLL1.

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi48G → A: High reduction in GTPase activity. No effect on GTP-binding. Loss of filament formation. 1 Publication1

Organism-specific databases

DisGeNETi55752.
OpenTargetsiENSG00000138758.
PharmGKBiPA128394688.

Polymorphism and mutation databases

BioMutaiSEPT11.
DMDMi50401687.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001735422 – 429Septin-11Add BLAST428

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanine1 Publication1
Modified residuei9PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9NVA2.
MaxQBiQ9NVA2.
PaxDbiQ9NVA2.
PeptideAtlasiQ9NVA2.
PRIDEiQ9NVA2.

2D gel databases

OGPiQ9NVA2.
UCD-2DPAGEQ9NVA2.

PTM databases

iPTMnetiQ9NVA2.
PhosphoSitePlusiQ9NVA2.
SwissPalmiQ9NVA2.

Expressioni

Tissue specificityi

Widely expressed, except in leukocytes.2 Publications

Gene expression databases

BgeeiENSG00000138758.
CleanExiHS_SEPT11.
ExpressionAtlasiQ9NVA2. baseline and differential.
GenevisibleiQ9NVA2. HS.

Organism-specific databases

HPAiHPA003459.
HPA005665.

Interactioni

Subunit structurei

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.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SEPT1Q8WYJ64EBI-957999,EBI-693002
SEPT5Q997198EBI-957999,EBI-373345

Protein-protein interaction databases

BioGridi120870. 43 interactors.
DIPiDIP-36161N.
IntActiQ9NVA2. 3 interactors.
MINTiMINT-3074824.
STRINGi9606.ENSP00000264893.

Structurei

3D structure databases

ProteinModelPortaliQ9NVA2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini38 – 304Septin-type GAdd BLAST267

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili320 – 415Sequence analysisAdd BLAST96

Sequence similaritiesi

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG2655. Eukaryota.
COG5019. LUCA.
GeneTreeiENSGT00860000133721.
HOGENOMiHOG000233586.
HOVERGENiHBG065093.
InParanoidiQ9NVA2.
KOiK16939.
OMAiDHLKRTH.
OrthoDBiEOG091G0IKM.
PhylomeDBiQ9NVA2.
TreeFamiTF101080.

Family and domain databases

CDDicd01850. CDC_Septin. 1 hit.
Gene3Di3.40.50.300. 1 hit.
InterProiIPR030379. G_SEPTIN_dom.
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 (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9NVA2-1) [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
MAVAVGRPSN EELRNLSLSG HVGFDSLPDQ LVNKSTSQGF CFNILCVGET
60 70 80 90 100
GIGKSTLMDT LFNTKFESDP ATHNEPGVRL KARSYELQES NVRLKLTIVD
110 120 130 140 150
TVGFGDQINK DDSYKPIVEY IDAQFEAYLQ EELKIKRSLF NYHDTRIHAC
160 170 180 190 200
LYFIAPTGHS LKSLDLVTMK KLDSKVNIIP IIAKADTIAK NELHKFKSKI
210 220 230 240 250
MSELVSNGVQ IYQFPTDEET VAEINATMSV HLPFAVVGST EEVKIGNKMA
260 270 280 290 300
KARQYPWGVV QVENENHCDF VKLREMLIRV NMEDLREQTH TRHYELYRRC
310 320 330 340 350
KLEEMGFKDT DPDSKPFSLQ ETYEAKRNEF LGELQKKEEE MRQMFVMRVK
360 370 380 390 400
EKEAELKEAE KELHEKFDLL KRTHQEEKKK VEDKKKELEE EVNNFQKKKA
410 420
AAQLLQSQAQ QSGAQQTKKD KDKKNASFT
Length:429
Mass (Da):49,398
Last modified:January 23, 2007 - v3
Checksum:iD467F1F315FFD028
GO
Isoform 2 (identifier: Q9NVA2-2) [UniParc]FASTAAdd to basket

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

Note: No experimental confirmation available.
Show »
Length:439
Mass (Da):50,823
Checksum:iC8E82F016C56A392
GO

Sequence cautioni

The sequence BAB55250 differs from that shown. Reason: Erroneous initiation.Curated
The sequence CAB53741 differs from that shown. Contaminating sequence. Potential poly-A sequence.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti142Y → H in CAB53741 (PubMed:15489334).Curated1
Sequence conflicti298R → H in CAB53741 (PubMed:15489334).Curated1
Sequence conflicti321E → G in CAB53741 (PubMed:15489334).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0383201 – 9MAVAVGRPS → MEERKPAHVLRSFKYAAFM in isoform 2. 1 Publication9

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS34018.1. [Q9NVA2-1]
CCDS77931.1. [Q9NVA2-2]
RefSeqiNP_001293076.1. NM_001306147.1. [Q9NVA2-2]
NP_060713.1. NM_018243.3. [Q9NVA2-1]
XP_016863889.1. XM_017008400.1. [Q9NVA2-2]
UniGeneiHs.128199.

Genome annotation databases

EnsembliENST00000264893; ENSP00000264893; ENSG00000138758. [Q9NVA2-1]
ENST00000510515; ENSP00000422896; ENSG00000138758. [Q9NVA2-2]
GeneIDi55752.
KEGGihsa:55752.
UCSCiuc003hkj.4. human. [Q9NVA2-1]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS34018.1. [Q9NVA2-1]
CCDS77931.1. [Q9NVA2-2]
RefSeqiNP_001293076.1. NM_001306147.1. [Q9NVA2-2]
NP_060713.1. NM_018243.3. [Q9NVA2-1]
XP_016863889.1. XM_017008400.1. [Q9NVA2-2]
UniGeneiHs.128199.

3D structure databases

ProteinModelPortaliQ9NVA2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120870. 43 interactors.
DIPiDIP-36161N.
IntActiQ9NVA2. 3 interactors.
MINTiMINT-3074824.
STRINGi9606.ENSP00000264893.

PTM databases

iPTMnetiQ9NVA2.
PhosphoSitePlusiQ9NVA2.
SwissPalmiQ9NVA2.

Polymorphism and mutation databases

BioMutaiSEPT11.
DMDMi50401687.

2D gel databases

OGPiQ9NVA2.
UCD-2DPAGEQ9NVA2.

Proteomic databases

EPDiQ9NVA2.
MaxQBiQ9NVA2.
PaxDbiQ9NVA2.
PeptideAtlasiQ9NVA2.
PRIDEiQ9NVA2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000264893; ENSP00000264893; ENSG00000138758. [Q9NVA2-1]
ENST00000510515; ENSP00000422896; ENSG00000138758. [Q9NVA2-2]
GeneIDi55752.
KEGGihsa:55752.
UCSCiuc003hkj.4. human. [Q9NVA2-1]

Organism-specific databases

CTDi55752.
DisGeNETi55752.
GeneCardsiSEPT11.
HGNCiHGNC:25589. SEPT11.
HPAiHPA003459.
HPA005665.
MIMi612887. gene.
neXtProtiNX_Q9NVA2.
OpenTargetsiENSG00000138758.
PharmGKBiPA128394688.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2655. Eukaryota.
COG5019. LUCA.
GeneTreeiENSGT00860000133721.
HOGENOMiHOG000233586.
HOVERGENiHBG065093.
InParanoidiQ9NVA2.
KOiK16939.
OMAiDHLKRTH.
OrthoDBiEOG091G0IKM.
PhylomeDBiQ9NVA2.
TreeFamiTF101080.

Miscellaneous databases

ChiTaRSiSEPT11. human.
GeneWikiiSEPT11.
GenomeRNAii55752.
PROiQ9NVA2.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000138758.
CleanExiHS_SEPT11.
ExpressionAtlasiQ9NVA2. baseline and differential.
GenevisibleiQ9NVA2. HS.

Family and domain databases

CDDicd01850. CDC_Septin. 1 hit.
Gene3Di3.40.50.300. 1 hit.
InterProiIPR030379. G_SEPTIN_dom.
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]
ProtoNetiSearch...

Entry informationi

Entry nameiSEP11_HUMAN
AccessioniPrimary (citable) accession number: Q9NVA2
Secondary accession number(s): B7Z7Z6
, E9KL32, Q4W5G1, Q7L4N1, Q96SP1, Q9UFY9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 139 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.