Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9UH03 (SEPT3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Neuronal-specific septin-3
Gene names
Name:SEPT3
Synonyms:SEP3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length358 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

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 By similarity.

Subcellular location

Cytoplasm. Cytoplasmcytoskeleton By similarity. Cell junctionsynapse By similarity.

Tissue specificity

Brain-specific. Ref.1 Ref.8

Induction

Up-regulated during neuronal differentiation. Ref.1

Post-translational modification

Phosphorylated by PKG on serine residues. Phosphorylated by PKG on Ser-91 By similarity.

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 AAG00517.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAG00518.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAG00519.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAI11780.2 differs from that shown. Reason: Erroneous initiation.

The sequence CAD38797.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAG30458.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processCell cycle
Cell division
   Cellular componentCell junction
Cytoplasm
Cytoskeleton
Synapse
   Coding sequence diversityAlternative splicing
   LigandGTP-binding
Nucleotide-binding
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

cell division

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcell junction

Inferred from electronic annotation. Source: UniProtKB-KW

septin complex

Inferred from electronic annotation. Source: InterPro

synapse

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9UH03-1)

Also known as: A; SEP3A;

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: Q9UH03-2)

Also known as: B; SEP3B;

The sequence of this isoform differs from the canonical sequence as follows:
     338-358: GEGLLGTVLPPVPATPCPTAE → VSVDTEESHDSNP
Isoform 3 (identifier: Q9UH03-3)

Also known as: C; SEP3C;

The sequence of this isoform differs from the canonical sequence as follows:
     68-83: GQSGLGKSTLVNTLFK → AGSPLRSTSMSSTRSS
     84-358: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 358358Neuronal-specific septin-3
PRO_0000173517

Regions

Domain58 – 331274Septin-type G
Nucleotide binding68 – 758GTP
Nucleotide binding208 – 2169GTP

Sites

Binding site1021GTP
Binding site2651GTP; via amide nitrogen and carbonyl oxygen
Binding site2801GTP

Amino acid modifications

Modified residue911Phosphoserine By similarity

Natural variations

Alternative sequence68 – 8316GQSGL…NTLFK → AGSPLRSTSMSSTRSS in isoform 3.
VSP_025398
Alternative sequence84 – 358275Missing in isoform 3.
VSP_025399
Alternative sequence338 – 35821GEGLL…CPTAE → VSVDTEESHDSNP in isoform 2.
VSP_006049

Secondary structure

........................................ 358
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (A) (SEP3A) [UniParc].

Last modified May 15, 2007. Version 3.
Checksum: B49B0D1FBD9DE43B

FASTA35840,704
        10         20         30         40         50         60 
MSKGLPETRT DAAMSELVPE PRPKPAVPMK PMSINSNLLG YIGIDTIIEQ MRKKTMKTGF 

        70         80         90        100        110        120 
DFNIMVVGQS GLGKSTLVNT LFKSQVSRKA SSWNREEKIP KTVEIKAIGH VIEEGGVKMK 

       130        140        150        160        170        180 
LTVIDTPGFG DQINNENCWE PIEKYINEQY EKFLKEEVNI ARKKRIPDTR VHCCLYFISP 

       190        200        210        220        230        240 
TGHSLRPLDL EFMKHLSKVV NIIPVIAKAD TMTLEEKSEF KQRVRKELEV NGIEFYPQKE 

       250        260        270        280        290        300 
FDEDLEDKTE NDKIRQESMP FAVVGSDKEY QVNGKRVLGR KTPWGIIEVE NLNHCEFALL 

       310        320        330        340        350 
RDFVIRTHLQ DLKEVTHNIH YETYRAKRLN DNGGLPPGEG LLGTVLPPVP ATPCPTAE 

« Hide

Isoform 2 (B) (SEP3B) [UniParc].

Checksum: 71D66D57E04D6C93
Show »

FASTA35040,100
Isoform 3 (C) (SEP3C) [UniParc].

Checksum: A1008153DB5F8F76
Show »

FASTA839,061

References

« Hide 'large scale' references
[1]"Human septin 3 on chromosome 22q13.2 is upregulated by neuronal differentiation."
Methner A., Leypoldt F., Joost P., Lewerenz J.
Biochem. Biophys. Res. Commun. 283:48-56(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), INDUCTION, TISSUE SPECIFICITY.
[2]"A genome annotation-driven approach to cloning the human ORFeome."
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.
Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[3]"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] (ISOFORM 2).
Tissue: Amygdala.
[4]"The DNA sequence of human chromosome 22."
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. expand/collapse author list , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.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].
[6]"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).
[7]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 133-358 (ISOFORM 2).
Tissue: Brain.
[8]"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.
[9]"The structure and properties of septin 3: a possible missing link in septin filament formation."
Macedo J.N., Valadares N.F., Marques I.A., Ferreira F.M., Damalio J.C., Pereira H.M., Garratt R.C., Araujo A.P.
Biochem. J. 450:95-105(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.88 ANGSTROMS) OF 60-329, GTP-BINDING SITES.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF285107 mRNA. Translation: AAG00517.1. Different initiation.
AF285108 mRNA. Translation: AAG00518.1. Different initiation.
AF285109 mRNA. Translation: AAG00519.1. Different initiation.
CR456572 mRNA. Translation: CAG30458.1. Different initiation.
AL833942 mRNA. Translation: CAD38797.1. Different initiation.
Z99716 Genomic DNA. Translation: CAI41693.1.
Z99716 Genomic DNA. Translation: CAQ07552.1.
CH471095 Genomic DNA. Translation: EAW60480.1.
BC111779 mRNA. Translation: AAI11780.2. Different initiation.
AB209152 mRNA. Translation: BAD92389.1.
CCDSCCDS14026.2. [Q9UH03-1]
CCDS14027.2. [Q9UH03-2]
PIRJC7681.
RefSeqNP_061979.3. NM_019106.5. [Q9UH03-2]
NP_663786.2. NM_145733.2. [Q9UH03-1]
UniGeneHs.120483.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3SOPX-ray2.88A/B60-329[»]
ProteinModelPortalQ9UH03.
SMRQ9UH03. Positions 60-329.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121011. 3 interactions.
IntActQ9UH03. 2 interactions.
MINTMINT-1385903.
STRING9606.ENSP00000379704.

PTM databases

PhosphoSiteQ9UH03.

Polymorphism databases

DMDM147744590.

Proteomic databases

MaxQBQ9UH03.
PaxDbQ9UH03.
PRIDEQ9UH03.

Protocols and materials databases

DNASU55964.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000328414; ENSP00000332866; ENSG00000100167. [Q9UH03-3]
ENST00000396417; ENSP00000379695; ENSG00000100167. [Q9UH03-3]
ENST00000396425; ENSP00000379703; ENSG00000100167. [Q9UH03-2]
ENST00000396426; ENSP00000379704; ENSG00000100167. [Q9UH03-1]
GeneID55964.
KEGGhsa:55964.
UCSCuc003bbr.4. human. [Q9UH03-1]
uc003bbs.4. human. [Q9UH03-2]

Organism-specific databases

CTD55964.
GeneCardsGC22P042372.
HGNCHGNC:10750. SEPT3.
HPACAB017633.
HPA003548.
MIM608314. gene.
neXtProtNX_Q9UH03.
PharmGKBPA24355.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5019.
HOVERGENHBG065093.
InParanoidQ9UH03.
KOK16938.
OMARKELTAM.
PhylomeDBQ9UH03.
TreeFamTF101078.

Gene expression databases

ArrayExpressQ9UH03.
BgeeQ9UH03.
CleanExHS_SEPT3.
GenevestigatorQ9UH03.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR000038. Cell_div_GTP-bd.
IPR027417. P-loop_NTPase.
IPR016491. Septin.
IPR008114. Septin3.
[Graphical view]
PANTHERPTHR18884. PTHR18884. 1 hit.
PfamPF00735. Septin. 1 hit.
[Graphical view]
PIRSFPIRSF006698. Septin. 1 hit.
PRINTSPR01741. SEPTIN3.
SUPFAMSSF52540. SSF52540. 1 hit.
PROSITEPS51719. G_SEPTIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSEPT3. human.
GeneWikiSEPT3.
GenomeRNAi55964.
NextBio61373.
PROQ9UH03.
SOURCESearch...

Entry information

Entry nameSEPT3_HUMAN
AccessionPrimary (citable) accession number: Q9UH03
Secondary accession number(s): B1AHR0 expand/collapse secondary AC list , Q2NKJ7, Q59GF7, Q6IBZ6, Q8N3P3, Q9HD35
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: May 15, 2007
Last modified: July 9, 2014
This is version 124 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM