Q9UH03 (SEPT3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Neuronal-specific septin-3

Gene names

Name:	SEPT3
Synonyms:	SEP3

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	358 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Cytoplasm › cytoskeleton By similarity. Cell junction › synapse 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 septin family.
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 process	Cell cycle Cell division
Cellular component	Cell junction Cytoplasm Cytoskeleton Synapse
Coding sequence diversity	Alternative splicing
Ligand	GTP-binding Nucleotide-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cytokinesis Non-traceable author statement. Source: UniProtKB
Cellular_component	cell 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_function	GTP 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 358

358

Neuronal-specific septin-3

PRO_0000173517

Regions

Nucleotide binding

68 – 75

8

GTP

Nucleotide binding

208 – 216

9

GTP

Sites

Binding site

102

1

GTP

Binding site

265

1

GTP; via amide nitrogen and carbonyl oxygen

Binding site

280

1

GTP

Amino acid modifications

Modified residue

91

1

Phosphoserine By similarity

Natural variations

Alternative sequence

68 – 83

16

GQSGL…NTLFK → AGSPLRSTSMSSTRSS in isoform 3.

VSP_025398

Alternative sequence

84 – 358

275

Missing in isoform 3.

VSP_025399

Alternative sequence

338 – 358

21

GEGLL…CPTAE → VSVDTEESHDSNP in isoform 2.

VSP_006049

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

358

Helix Strand Turn

Details...

Beta strand

61 – 73

13

Helix

74 – 85

12

Beta strand

107 – 111

5

Beta strand

120 – 124

5

Helix

140 – 157

18

Beta strand

173 – 178

6

Beta strand

182 – 184

3

Helix

187 – 197

11

Beta strand

200 – 206

7

Helix

209 – 211

3

Helix

214 – 230

17

Helix

246 – 256

11

Beta strand

260 – 262

3

Beta strand

269 – 272

4

Beta strand

275 – 280

6

Beta strand

287 – 290

4

Turn

292 – 294

3

Helix

297 – 305

9

Turn

306 – 308

3

Helix

309 – 318

10

Helix

320 – 328

9

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (A) (SEP3A) [UniParc]. Last modified May 15, 2007. Version 3. Checksum: B49B0D1FBD9DE43B	FASTA	358	40,704
	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
	Isoform 2 (B) (SEP3B) [UniParc]. Checksum: 71D66D57E04D6C93	FASTA	350	40,100
	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 DNGGLPPVSV DTEESHDSNP
	Isoform 3 (C) (SEP3C) [UniParc]. Checksum: A1008153DB5F8F76	FASTA	83	9,061
	10 20 30 40 50 60 MSKGLPETRT DAAMSELVPE PRPKPAVPMK PMSINSNLLG YIGIDTIIEQ MRKKTMKTGF 70 80 DFNIMVVAGS PLRSTSMSST RSS

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.

IPI

IPI00022652.
IPI00384187.
IPI00745056.

PIR

JC7681.

RefSeq

NP_061979.3. NM_019106.5.
NP_663786.2. NM_145733.2.

UniGene

Hs.120483.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3SOP	X-ray	2.88	A/B	60-329	[»]

ProteinModelPortal

Q9UH03.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9UH03. 1 interaction.

MINT

MINT-1385903.

STRING

9606.ENSP00000379704.

PTM databases

PhosphoSite

Q9UH03.

Polymorphism databases

DMDM

147744590.

Proteomic databases

PaxDb

Q9UH03.

PRIDE

Q9UH03.

Protocols and materials databases

DNASU

55964.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000328414; ENSP00000332866; ENSG00000100167.
ENST00000396417; ENSP00000379695; ENSG00000100167.
ENST00000396425; ENSP00000379703; ENSG00000100167.
ENST00000396426; ENSP00000379704; ENSG00000100167.

GeneID

55964.

KEGG

hsa:55964.

UCSC

uc003bbr.4. human.
uc003bbs.4. human.

Organism-specific databases

CTD

55964.

GeneCards

GC22P042372.

HGNC

HGNC:10750. SEPT3.

HPA

CAB017633.
HPA003548.

MIM

608314. gene.

neXtProt

NX_Q9UH03.

PharmGKB

PA24355.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5019.

HOVERGEN

HBG065093.

InParanoid

Q9UH03.

OMA

SQYLRKE.

Gene expression databases

ArrayExpress

Q9UH03.

Bgee

Q9UH03.

CleanEx

HS_SEPT3.

Genevestigator

Q9UH03.

GermOnline

ENSG00000100167. Homo sapiens.

Family and domain databases

InterPro

IPR000038. Cell_div_GTP-bd.
IPR016491. Septin.
IPR008114. Septin3.
[Graphical view]

PANTHER

PTHR18884. PTHR18884. 1 hit.

Pfam

PF00735. Septin. 1 hit.
[Graphical view]

PIRSF

PIRSF006698. Septin. 1 hit.

PRINTS

PR01741. SEPTIN3.

ProtoNet

Search...

Other

ChiTaRS

SEPT3. human.

GenomeRNAi

55964.

NextBio

61373.

SOURCE

Search...

Entry information

Entry name

SEPT3_HUMAN

Accession

Primary (citable) accession number: Q9UH03
Secondary accession number(s): B1AHR0 , Q2NKJ7, Q59GF7, Q6IBZ6, Q8N3P3, Q9HD35

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2001
Last sequence update:	May 15, 2007
Last modified:	May 1, 2013
This is version 113 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.