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Protein

Septin-14

Gene

SEPT14

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Filament-forming cytoskeletal GTPase (By similarity). May play a role in cytokinesis (Potential).By similarityCurated

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei114GTP; via amide nitrogenBy similarity1
Binding sitei249GTP; via amide nitrogen and carbonyl oxygenBy similarity1
Binding sitei264GTPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi59 – 66GTPBy similarity8
Nucleotide bindingi195 – 203GTPBy similarity9

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Septin-14
Gene namesi
Name:SEPT14
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:33280. SEPT14.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Organism-specific databases

DisGeNETi346288.
MalaCardsiSEPT14.
OpenTargetsiENSG00000154997.
Orphaneti251579. Giant cell glioblastoma.
251576. Gliosarcoma.
PharmGKBiPA162402917.

Polymorphism and mutation databases

BioMutaiSEPT14.
DMDMi152112291.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002944251 – 432Septin-14Add BLAST432

Proteomic databases

MaxQBiQ6ZU15.
PaxDbiQ6ZU15.
PeptideAtlasiQ6ZU15.
PRIDEiQ6ZU15.

PTM databases

iPTMnetiQ6ZU15.
PhosphoSitePlusiQ6ZU15.

Expressioni

Tissue specificityi

Testis-specific.1 Publication

Gene expression databases

BgeeiENSG00000154997.
CleanExiHS_SEPT14.

Organism-specific databases

HPAiHPA058456.

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 (By similarity). Interacts with SEPT9.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
SEPT9Q9UHD8-13EBI-2009297,EBI-851558
SEPT9Q9UHD8-33EBI-2009297,EBI-851569

Protein-protein interaction databases

BioGridi131376. 5 interactors.
IntActiQ6ZU15. 8 interactors.
STRINGi9606.ENSP00000373627.

Structurei

3D structure databases

ProteinModelPortaliQ6ZU15.
SMRiQ6ZU15.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini49 – 315Septin-type GAdd BLAST267

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili332 – 412Sequence analysisAdd BLAST81

Sequence similaritiesi

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG2655. Eukaryota.
COG5019. LUCA.
GeneTreeiENSGT00860000133721.
HOGENOMiHOG000233586.
HOVERGENiHBG065093.
InParanoidiQ6ZU15.
KOiK16941.
OMAiNIRCLTT.
OrthoDBiEOG091G0IKM.
PhylomeDBiQ6ZU15.
TreeFamiTF101080.

Family and domain databases

CDDicd01850. CDC_Septin. 1 hit.
Gene3Di3.40.50.300. 2 hits.
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]

Sequencei

Sequence statusi: Complete.

Q6ZU15-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAERTMAMPT QIPADGDTQK ENNIRCLTTI GHFGFECLPN QLVSRSIRQG
60 70 80 90 100
FTFNILCVGE TGIGKSTLID TLFNTNLKDN KSSHFYSNVG LQIQTYELQE
110 120 130 140 150
SNVQLKLTVV ETVGYGDQID KEASYQPIVD YIDAQFEAYL QEELKIKRSL
160 170 180 190 200
FEYHDSRVHV CLYFISPTGH SLKSLDLLTM KNLDSKVNII PLIAKADTIS
210 220 230 240 250
KNDLQTFKNK IMSELISNGI QIYQLPTDEE TAAQANSSVS GLLPFAVVGS
260 270 280 290 300
TDEVKVGKRM VRGRHYPWGV LQVENENHCD FVKLRDMLLC TNMENLKEKT
310 320 330 340 350
HTQHYECYRY QKLQKMGFTD VGPNNQPVSF QEIFEAKRQE FYDQCQREEE
360 370 380 390 400
ELKQRFMQRV KEKEATFKEA EKELQDKFEH LKMIQQEEIR KLEEEKKQLE
410 420 430
GEIIDFYKMK AASEALQTQL STDTKKDKHR KK
Length:432
Mass (Da):50,025
Last modified:July 10, 2007 - v2
Checksum:iAFFF9A953F1FC637
GO

Sequence cautioni

The sequence BAC86412 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK126048 mRNA. Translation: BAC86412.1. Different initiation.
AK301928 mRNA. Translation: BAG63348.1.
AC092647 Genomic DNA. No translation available.
CCDSiCCDS5519.2.
RefSeqiNP_997249.2. NM_207366.2.
XP_011513675.1. XM_011515373.2.
UniGeneiHs.453629.

Genome annotation databases

EnsembliENST00000388975; ENSP00000373627; ENSG00000154997.
GeneIDi346288.
KEGGihsa:346288.
UCSCiuc003tqz.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK126048 mRNA. Translation: BAC86412.1. Different initiation.
AK301928 mRNA. Translation: BAG63348.1.
AC092647 Genomic DNA. No translation available.
CCDSiCCDS5519.2.
RefSeqiNP_997249.2. NM_207366.2.
XP_011513675.1. XM_011515373.2.
UniGeneiHs.453629.

3D structure databases

ProteinModelPortaliQ6ZU15.
SMRiQ6ZU15.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi131376. 5 interactors.
IntActiQ6ZU15. 8 interactors.
STRINGi9606.ENSP00000373627.

PTM databases

iPTMnetiQ6ZU15.
PhosphoSitePlusiQ6ZU15.

Polymorphism and mutation databases

BioMutaiSEPT14.
DMDMi152112291.

Proteomic databases

MaxQBiQ6ZU15.
PaxDbiQ6ZU15.
PeptideAtlasiQ6ZU15.
PRIDEiQ6ZU15.

Protocols and materials databases

DNASUi346288.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000388975; ENSP00000373627; ENSG00000154997.
GeneIDi346288.
KEGGihsa:346288.
UCSCiuc003tqz.2. human.

Organism-specific databases

CTDi346288.
DisGeNETi346288.
GeneCardsiSEPT14.
H-InvDBHIX0025388.
HGNCiHGNC:33280. SEPT14.
HPAiHPA058456.
MalaCardsiSEPT14.
MIMi612140. gene.
neXtProtiNX_Q6ZU15.
OpenTargetsiENSG00000154997.
Orphaneti251579. Giant cell glioblastoma.
251576. Gliosarcoma.
PharmGKBiPA162402917.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2655. Eukaryota.
COG5019. LUCA.
GeneTreeiENSGT00860000133721.
HOGENOMiHOG000233586.
HOVERGENiHBG065093.
InParanoidiQ6ZU15.
KOiK16941.
OMAiNIRCLTT.
OrthoDBiEOG091G0IKM.
PhylomeDBiQ6ZU15.
TreeFamiTF101080.

Miscellaneous databases

GenomeRNAii346288.
PROiQ6ZU15.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000154997.
CleanExiHS_SEPT14.

Family and domain databases

CDDicd01850. CDC_Septin. 1 hit.
Gene3Di3.40.50.300. 2 hits.
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 nameiSEP14_HUMAN
AccessioniPrimary (citable) accession number: Q6ZU15
Secondary accession number(s): A6NCC2, B4DXD6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: July 10, 2007
Last modified: November 30, 2016
This is version 102 of the entry and version 2 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, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: 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.