Reviewed, UniProtKB/Swiss-Prot Q15019 (SEPT2_HUMAN)

Names and origin

Protein names

Recommended name:
    Septin-2
Alternative name(s):
    Neural precursor cell expressed developmentally down-regulated protein 5
      Short name=NEDD-5

Gene names

Name:	SEPT2
Synonyms:	DIFF6, KIAA0158, NEDD5

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	361 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Required for normal progress through mitosis. Involved in cytokinesis. Ref.8
Subunit structure	Monomer, and homodimer. Nucleotide binding promotes dimerization. Heterohexamer composed of two heterotrimers containing one copy each of SEPT2, SEPT6 and SEPT7. The asymmetrical heterotrimers associate head-to-head to form a hexameric unit that assembles into filaments. Ref.22 Ref.23
Subcellular location	Cytoplasm. Spindle. Note: Accumulates near the contractile ring from anaphase through telophase, and finally condenses into the midbody. In interphase and postmitotic cells, localised to fibrous or granular structures, depending on the growth state of the cell By similarity.
Sequence similarities	Belongs to the septin family.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Cellular component	Cytoplasm
Ligand	GTP-binding Nucleotide-binding
PTM	Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	cell division Inferred from electronic annotation. Source: UniProtKB-KW mitosis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleus Inferred from direct assay. Source: UniProtKB septin complex Inferred from electronic annotation. Source: InterPro spindle Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SEPT11	Q9NVA2	1	EBI-741220,EBI-957999
SEPT6	Q14141	1	EBI-741220,EBI-745901
SEPT8	Q92599	1	EBI-741220,EBI-958021

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 361	361	Septin-2		PRO_0000173515
Regions
	Nucleotide binding	44 – 51	8	GTP
	Nucleotide binding	185 – 191	7	GTP
	Region	260 – 270	11	Important for dimerization
Sites
	Binding site	241	1	GTP; via amide nitrogen and carbonyl oxygen
	Binding site	258	1	GTP
	Site	156	1	Important for dimerization
Amino acid modifications
	Modified residue	17	1	Phosphotyrosine Ref.7
	Modified residue	211	1	Phosphotyrosine Ref.12
	Modified residue	218	1	Phosphoserine Ref.6 Ref.9 Ref.10 Ref.11 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20
	Modified residue	228	1	Phosphothreonine By similarity
Experimental info
	Mutagenesis	156	1	F → D: Loss of dimerization. Ref.22
	Mutagenesis	260	1	W → A: Loss of dimerization. Ref.22
	Mutagenesis	270	1	H → D: Loss of dimerization. Ref.22
	Sequence conflict	69	1	P → S in AAH14455. Ref.4
	Sequence conflict	72	1	A → AALNTRKTLLW in AAH33559. Ref.4
	Sequence conflict	360 – 361	2	HV → TCKVMCTYKKSEKTLSWIKK KTFQMHDPAVCFQSLGGCHP HFNSTCA in BAA05893. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q15019-1 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: 12CCBBE30806F92F	FASTA	361	41,487
	10 20 30 40 50 60 MSKQQPTQFI NPETPGYVGF ANLPNQVHRK SVKKGFEFTL MVVGESGLGK STLINSLFLT 70 80 90 100 110 120 DLYPERVIPG AAEKIERTVQ IEASTVEIEE RGVKLRLTVV DTPGYGDAIN CRDCFKTIIS 130 140 150 160 170 180 YIDEQFERYL HDESGLNRRH IIDNRVHCCF YFISPFGHGL KPLDVAFMKA IHNKVNIVPV 190 200 210 220 230 240 IAKADTLTLK ERERLKKRIL DEIEEHNIKI YHLPDAESDE DEDFKEQTRL LKASIPFSVV 250 260 270 280 290 300 GSNQLIEAKG KKVRGRLYPW GVVEVENPEH NDFLKLRTML ITHMQDLQEV TQDLHYENFR 310 320 330 340 350 360 SERLKRGGRK VENEDMNKDQ ILLEKEAELR RMQEMIARMQ AQMQMQMQGG DGDGGALGHH V

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Prediction of the coding sequences of unidentified human genes. IV. The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of cDNA clones from human cell line KG-1." Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N. DNA Res. 2:167-174(1995) [PubMed: 8590280] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Bone marrow.
[2]	"Isolation and mapping of a human gene (DIFF6) homologous to yeast CDC3, CDC10, CDC11, and CDC12, and mouse Diff6." Mori T., Miura K., Fujiwara T., Shin S., Inazawa J., Nakamura Y. Cytogenet. Cell Genet. 73:224-227(1996) [PubMed: 8697812] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[3]	"Human homolog of mouse Nedd5 mRNA." Hu G. Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Muscle and Testis.
[5]	Lubec G., Afjehi-Sadat L. Submitted (MAR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 51-66, MASS SPECTROMETRY. Tissue: Brain and Cajal-Retzius cell.
[6]	"Septin 2 phosphorylation: theoretical and mass spectrometric evidence for the existence of a single phosphorylation site in vivo." She Y.M., Huang Y.W., Zhang L., Trimble W.S. Rapid Commun. Mass Spectrom. 18:1123-1130(2004) [PubMed: 15150837] [Abstract] Cited for: PHOSPHORYLATION AT SER-218.
[7]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-17, MASS SPECTROMETRY.
[8]	"A mitotic septin scaffold required for mammalian chromosome congression and segregation." Spiliotis E.T., Kinoshita M., Nelson W.J. Science 307:1781-1785(2005) [PubMed: 15774761] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[9]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, MASS SPECTROMETRY. Tissue: Epithelium.
[10]	"Phosphoproteomic analysis of the human pituitary." Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F. Pituitary 9:109-120(2006) [PubMed: 16807684] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, MASS SPECTROMETRY. Tissue: Pituitary.
[11]	"Phosphoproteome analysis of the human mitotic spindle." Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R. Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, MASS SPECTROMETRY. Tissue: Epithelium.
[12]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-211, MASS SPECTROMETRY.
[13]	"Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line." Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S. Electrophoresis 28:2027-2034(2007) [PubMed: 17487921] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, MASS SPECTROMETRY.
[14]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, MASS SPECTROMETRY. Tissue: Epithelium.
[15]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, MASS SPECTROMETRY.
[16]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, MASS SPECTROMETRY. Tissue: Platelet.
[17]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, MASS SPECTROMETRY.
[18]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, MASS SPECTROMETRY.
[19]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, MASS SPECTROMETRY.
[20]	"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography." Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J. Proteomics 8:1346-1361(2008) [PubMed: 18318008] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, MASS SPECTROMETRY. Tissue: Liver.
[21]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[22]	"Structural insight into filament formation by mammalian septins." Sirajuddin M., Farkasovsky M., Hauer F., Kuehlmann D., Macara I.G., Weyand M., Stark H., Wittinghofer A. Nature 449:311-315(2007) [PubMed: 17637674] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 1-315 IN COMPLEXES WITH GTP, ELECTRON MICROSCOPY, MUTAGENESIS OF PHE-156; TRP-260 AND HIS-270, SUBUNIT.
[23]	"Human septin 2 in complex with GDP." Structural genomics consortium (SGC) Submitted (AUG-2007) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 21-320 IN COMPLEX WITH GDP, SUBUNIT.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBLGenBankDDBJ

D63878 mRNA. Translation: BAA09928.2. Different initiation.
D28540 mRNA. Translation: BAA05893.1.
AF038404 mRNA. Translation: AAB92377.1.
BC014455 mRNA. Translation: AAH14455.1.
BC033559 mRNA. Translation: AAH33559.1.

IPI

IPI00014177.

RefSeq

NP_001008491.1.
NP_001008492.1.
NP_004395.1.
NP_006146.1.

UniGene

Hs.335057
Hs.712657

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2QA5	X-ray	3.40	A/B	1-315	[»]
2QAG	X-ray	4.00	A	1-361	[»]
2QNR	X-ray	2.60	A/B	22-320	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q15019. 13 interactions.

PTM databases

PhosphoSite

Q15019.

2-D gel databases

OGP

Q15019.

Proteomic databases

PRIDE

Q15019.

Genome annotation databases

Ensembl

ENSG00000168385. Homo sapiens. [Contig view]

GeneID

4735.

KEGG

hsa:4735.

Organism-specific databases

GeneCards

GC02P241975.

H-InvDB

HIX0002981.

HGNC

HGNC:7729. SEPT2.

HPA

CAB017190.
HPA018481.

MIM

601506. gene.

HUGE

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GenAtlas

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Phylogenomic databases

HOGENOM

Q15019.

HOVERGEN

Q15019.

Gene expression databases

ArrayExpress

Q15019.

Bgee

Q15019.

CleanEx

HS_SEPT2.

GermOnline

ENSG00000168385. Homo sapiens.

Family and domain databases

InterPro

IPR000038. Cell_Div_GTP_bd.
IPR016491. Septin.
IPR008113. Septin2.
[Graphical view]

PANTHER

PTHR18884. Cell_Div_GTP_bd. 1 hit.

Pfam

PF00735. Septin. 1 hit.
[Graphical view]

PIRSF

PIRSF006698. Septin. 1 hit.

PRINTS

PR01740. SEPTIN2.

ProDom

PD002565. GTP_Cell_Div. 1 hit.
[Graphical view] [Entries sharing at least one domain]

ProtoNet

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Other Resources

NextBio

18256.

SOURCE

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Entry information

Entry name

SEPT2_HUMAN

Accession

Primary (citable) accession number: Q15019
Secondary accession number(s): Q14132, Q8IUK9, Q96CB0

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	June 16, 2009
This is version 101 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)