Q15019 (SEPT2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Filament-forming cytoskeletal GTPase. Required for normal organization of the actin cytoskeleton. Plays a role in the biogenesis of polarized columnar-shaped epithelium by maintaining polyglutamylated microtubules, thus facilitating efficient vesicle transport, and by impeding MAP4 binding to tubulin. Required for the progression through mitosis. Forms a scaffold at the midplane of the mitotic splindle required to maintain CENPE localization at kinetochores and consequently chromosome congression. During anaphase, may be required for chromosome segregation and spindle elongation. Plays a role in ciliogenesis and collective cell movements. May play a role in the internalization of 2 intracellular microbial pathogens, Listeria monocytogenes and Shigella flexneri. Ref.12 Ref.17 Ref.22 Ref.32
Subunit structure	Septins polymerize into heterooligomeric protein complexes that form filaments, and associate with cellular membranes, actin filaments and microtubules. GTPase activity is required for filament formation. Filaments are assembled from asymmetrical heterotrimers, composed of SEPT2, SEPT6 and SEPT7 that associate head-to-head to form a hexameric unit. Interaction between SEPT2 and SEPT7 seems indirect. Interacts with SEPT5 By similarity. Interaction with SEPT4 not detected By similarity. Interacts with SEPT9. Interacts with MAP4. Ref.10 Ref.14 Ref.32 Ref.36 Ref.37
Subcellular location	Cytoplasm. Cytoplasm › cytoskeleton. Cytoplasm › cytoskeleton › spindle. Chromosome › centromere › kinetochore. Cleavage furrow. Midbody. Cytoplasm › cell cortex. Note: In metaphase cells, localized within the microtubule spindle. At the metaphase plate, in close apposition to the kinetochores of the congressed chromosomes. In cells undergoing cytokinesis, localized to the midbody, the ingressing cleavage furrow, and the central spindle. During bacterial infection, displays a collar shape structure next to actin at the pole of invading bacteria. In epithelial cells, colocalizes with polyglutamylated tubulin around the trans-Golgi network, as well as juxatnuclear and proximal Golgi apparatus. Ref.12
Tissue specificity	Widely expressed. Up-regulated in liver cancer. Ref.9 Ref.30
Miscellaneous	Coordinated expression with SEPT6 and SEPT7.
Sequence similarities	Belongs to the septin family.
Sequence caution	The sequence AAY14718.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence BAA09928.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Cellular component	Centromere Chromosome Cytoplasm Cytoskeleton Kinetochore
Coding sequence diversity	Alternative splicing
Ligand	GTP-binding Nucleotide-binding
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	cell division Inferred from electronic annotation. Source: UniProtKB-KW mitosis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	actin cytoskeleton Inferred from direct assay. Source: HPA cleavage furrow Inferred from electronic annotation. Source: UniProtKB-SubCell condensed chromosome kinetochore Inferred from electronic annotation. Source: UniProtKB-SubCell midbody Inferred from electronic annotation. Source: UniProtKB-SubCell nucleolus Inferred from direct assay. Source: HPA 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
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SEPT6	Q14141	4	EBI-741220,EBI-745901

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q15019-1)

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: Q15019-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MPWISEGRATRPCLRVPSARRGDEGLHQRDEASQKM

Note: No experimental confirmation available.

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

183 – 191

9

GTP

Region

260 – 270

11

Important for dimerization

Sites

Binding site

78

1

GTP By similarity

Binding site

104

1

GTP; via amide nitrogen By similarity

Binding site

241

1

GTP; via amide nitrogen and carbonyl oxygen

Binding site

256

1

GTP

Site

156

1

Important for dimerization

Amino acid modifications

Modified residue

17

1

Phosphotyrosine Ref.11

Modified residue

190

1

N6-acetyllysine Ref.34

Modified residue

211

1

Phosphotyrosine Ref.18

Modified residue

218

1

Phosphoserine Ref.8 Ref.13 Ref.15 Ref.16 Ref.19 Ref.20 Ref.21 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.33

Modified residue

228

1

Phosphothreonine By similarity

Natural variations

Alternative sequence

1

1

M → MPWISEGRATRPCLRVPSAR RGDEGLHQRDEASQKM in isoform 2.

VSP_038271

Experimental info

Mutagenesis

156

1

F → D: Loss of dimerization. Ref.36

Mutagenesis

218

1

S → A: Loss of phosphorylation. Ref.30

Mutagenesis

260

1

W → A: Loss of dimerization. Ref.36

Mutagenesis

270

1

H → D: Loss of dimerization. Ref.36

Sequence conflict

69

1

P → S in AAH14455. Ref.6

Sequence conflict

72

1

A → AALNTRKTLLW in AAH33559. Ref.6

Sequence conflict

360 – 361

2

HV → TCKVMCTYKKSEKTLSWIKK KTFQMHDPAVCFQSLGGCHP HFNSTCA in BAA05893. Ref.2

Secondary structure

1

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361

Helix Strand Turn

Details...

Beta strand

38 – 43

6

Helix

51 – 58

8

Beta strand

85 – 88

4

Beta strand

95 – 99

5

Helix

118 – 133

16

Beta strand

148 – 153

6

Helix

162 – 171

10

Turn

172 – 174

3

Beta strand

177 – 181

5

Helix

184 – 186

3

Helix

189 – 205

17

Helix

225 – 232

8

Beta strand

236 – 238

3

Turn

268 – 270

3

Helix

273 – 282

10

Helix

284 – 293

10

Helix

295 – 305

11

Sequences

	Sequence		Length	Mass (Da)
	Isoform 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
	Isoform 2 [UniParc]. Checksum: 4BD59305219D99B5	FASTA	396	45,461
	10 20 30 40 50 60 MPWISEGRAT RPCLRVPSAR RGDEGLHQRD EASQKMSKQQ PTQFINPETP GYVGFANLPN 70 80 90 100 110 120 QVHRKSVKKG FEFTLMVVGE SGLGKSTLIN SLFLTDLYPE RVIPGAAEKI ERTVQIEAST 130 140 150 160 170 180 VEIEERGVKL RLTVVDTPGY GDAINCRDCF KTIISYIDEQ FERYLHDESG LNRRHIIDNR 190 200 210 220 230 240 VHCCFYFISP FGHGLKPLDV AFMKAIHNKV NIVPVIAKAD TLTLKERERL KKRILDEIEE 250 260 270 280 290 300 HNIKIYHLPD AESDEDEDFK EQTRLLKASI PFSVVGSNQL IEAKGKKVRG RLYPWGVVEV 310 320 330 340 350 360 ENPEHNDFLK LRTMLITHMQ DLQEVTQDLH YENFRSERLK RGGRKVENED MNKDQILLEK 370 380 390 EAELRRMQEM IARMQAQMQM QMQGGDGDGG ALGHHV

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] (ISOFORM 1). 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] (ISOFORM 1). 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] (ISOFORM 1).
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Amygdala.
[5]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed: 15815621] [Abstract] 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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Muscle and Testis.
[7]	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.
[8]	"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.
[9]	"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: 15915442] [Abstract] Cited for: TISSUE SPECIFICITY.
[10]	"Mammalian septins regulate microtubule stability through interaction with the microtubule-binding protein MAP4." Kremer B.E., Haystead T., Macara I.G. Mol. Biol. Cell 16:4648-4659(2005) [PubMed: 16093351] [Abstract] Cited for: INTERACTION WITH MAP4, COORDINATED EXPRESSION WITH SEPT2 AND SEPT7.
[11]	"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.
[12]	"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.
[13]	"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: Cervix carcinoma.
[14]	"Structural analysis of septin 2, 6, and 7 complexes." Low C., Macara I.G. J. Biol. Chem. 281:30697-30706(2006) [PubMed: 16914550] [Abstract] Cited for: INTERACTION WITH SEPT6 AND SEPT7.
[15]	"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.
[16]	"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: Cervix adenocarcinoma.
[17]	"Septins regulate actin organization and cell-cycle arrest through nuclear accumulation of NCK mediated by SOCS7." Kremer B.E., Adang L.A., Macara I.G. Cell 130:837-850(2007) [PubMed: 17803907] [Abstract] Cited for: FUNCTION.
[18]	"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. Tissue: Lung carcinoma.
[19]	"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. Tissue: Prostate cancer.
[20]	"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: Cervix carcinoma.
[21]	"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. Tissue: Embryonic kidney.
[22]	"Epithelial polarity requires septin coupling of vesicle transport to polyglutamylated microtubules." Spiliotis E.T., Hunt S.J., Hu Q., Kinoshita M., Nelson W.J. J. Cell Biol. 180:295-303(2008) [PubMed: 18209106] [Abstract] Cited for: FUNCTION, COLOCALIZATION WITH POLYGLUTAMYLATED TUBULIN.
[23]	"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.
[24]	"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. Tissue: Cervix carcinoma.
[25]	"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment." Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J. J. Proteome Res. 7:5167-5176(2008) [PubMed: 19367720] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, MASS SPECTROMETRY. Tissue: T-cell.
[26]	"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. Tissue: Cervix carcinoma.
[27]	"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. Tissue: Cervix carcinoma.
[28]	"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.
[29]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[30]	"The phosphorylation of SEPT2 on Ser218 by casein kinase 2 is important to hepatoma carcinoma cell proliferation." Yu W., Ding X., Chen F., Liu M., Shen S., Gu X., Yu L. Mol. Cell. Biochem. 325:61-67(2009) [PubMed: 19165576] [Abstract] Cited for: PHOSPHORYLATION AT SER-218, MUTAGENESIS OF SER-218, TISSUE SPECIFICITY.
[31]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, MASS SPECTROMETRY.
[32]	"Septins regulate bacterial entry into host cells." Mostowy S., Nam Tham T., Danckaert A., Guadagnini S., Boisson-Dupuis S., Pizarro-Cerda J., Cossart P. PLoS ONE 4:E4196-E4196(2009) [PubMed: 19145258] [Abstract] Cited for: INTERACTION WITH SEPT9, ROLE IN BACTERIAL INFECTION.
[33]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[34]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-190, MASS SPECTROMETRY.
[35]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[36]	"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.
[37]	"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

EMBL
GenBank
DDBJ

D63878 mRNA. Translation: BAA09928.2. Different initiation.
D28540 mRNA. Translation: BAA05893.1.
AF038404 mRNA. Translation: AAB92377.1.
AK294563 mRNA. Translation: BAG57759.1.
AC005104 Genomic DNA. No translation available.
AC104841 Genomic DNA. Translation: AAY14718.1. Sequence problems.
BC014455 mRNA. Translation: AAH14455.1.
BC033559 mRNA. Translation: AAH33559.1.

IPI

IPI00014177.
IPI00871851.

RefSeq

NP_001008491.1. NM_001008491.1.
NP_001008492.1. NM_001008492.1.
NP_004395.1. NM_004404.3.
NP_006146.1. NM_006155.1.

UniGene

Hs.335057.
Hs.728805.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q15019.

SMR

Q15019. Positions 34-305.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q15019. 5 interactions.

MINT

MINT-1433588.

STRING

Q15019.

PTM databases

PhosphoSite

Q15019.

Polymorphism databases

DMDM

2500769.

2D gel databases

OGP

Q15019.

Proteomic databases

PRIDE

Q15019.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000360051; ENSP00000353157; ENSG00000168385.
ENST00000391971; ENSP00000375832; ENSG00000168385.
ENST00000391972; ENSP00000375833; ENSG00000168385.
ENST00000391973; ENSP00000375834; ENSG00000168385.
ENST00000401990; ENSP00000385109; ENSG00000168385.
ENST00000402092; ENSP00000385172; ENSG00000168385.
ENST00000402251; ENSP00000385387; ENSG00000168385.

GeneID

4735.

KEGG

hsa:4735.

UCSC

uc002wbc.1. human.

Organism-specific databases

CTD

4735.

GeneCards

GC02P242254.

H-InvDB

HIX0002981.

HGNC

HGNC:7729. SEPT2.

HPA

CAB017190.
HPA018481.

MIM

601506. gene.

neXtProt

NX_Q15019.

PharmGKB

PA31535.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG07957.

GeneTree

ENSGT00590000082878.

HOVERGEN

HBG065093.

OMA

MQLQMQG.

OrthoDB

EOG47SSF3.

PhylomeDB

Q15019.

Gene expression databases

ArrayExpress

Q15019.

Bgee

Q15019.

CleanEx

HS_SEPT2.

Genevestigator

Q15019.

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.

ProtoNet

Search...

Other

NextBio

18256.

SOURCE

Search...

Entry information

Entry name

SEPT2_HUMAN

Accession

Primary (citable) accession number: Q15019
Secondary accession number(s): B4DGE8 , Q14132, Q53QU3, Q8IUK9, Q96CB0

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	January 25, 2012
This is version 129 of the entry and version 1 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.