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) [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	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. In cilia, required for the integrity of the diffusion barrier at the base of the primary cilium that prevents diffusion of transmembrane proteins between the cilia and plasma membranes: probably acts by regulating the assembly of the tectonic-like complex (also named B9 complex) by localizing TMEM231 protein. May play a role in the internalization of 2 intracellular microbial pathogens, Listeria monocytogenes and Shigella flexneri. Ref.11 Ref.14 Ref.15 Ref.23
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.13 Ref.23 Ref.29 Ref.30
Subcellular location	Cytoplasm. Cytoplasm › cytoskeleton. Cytoplasm › cytoskeleton › spindle. Chromosome › centromere › kinetochore. Cleavage furrow. Midbody. Cytoplasm › cell cortex. Cell projection › cilium membrane By similarity. 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. Localizes at the base of the cilia near the morphological distinction between the cilia and plasma membranes. Ref.11
Tissue specificity	Widely expressed. Up-regulated in liver cancer. Ref.9 Ref.21
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	Cell membrane Cell projection Centromere Chromosome Cytoplasm Cytoskeleton Kinetochore Membrane
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 cilium assembly Inferred from sequence or structural similarity. Source: UniProtKB mitosis Inferred from electronic annotation. Source: UniProtKB-KW neuron projection development Inferred from electronic annotation. Source: Compara regulation of L-glutamate transport Inferred from electronic annotation. Source: Compara regulation of protein localization Inferred from electronic annotation. Source: Compara smoothened signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	actin cytoskeleton Inferred from direct assay. Source: HPA cell surface Inferred from electronic annotation. Source: Compara cilium membrane Inferred from sequence or structural similarity. Source: UniProtKB cleavage furrow Inferred from electronic annotation. Source: UniProtKB-SubCell condensed chromosome kinetochore Inferred from electronic annotation. Source: UniProtKB-SubCell cytoplasm Inferred from direct assay PubMed 10942595. Source: UniProtKB exocyst Inferred from electronic annotation. Source: Compara midbody Inferred from electronic annotation. Source: UniProtKB-SubCell nucleolus Inferred from direct assay. Source: HPA perinuclear region of cytoplasm Inferred from electronic annotation. Source: Compara septin complex Inferred from electronic annotation. Source: InterPro spindle Inferred from electronic annotation. Source: UniProtKB-SubCell synapse Inferred from electronic annotation. Source: Compara
Molecular_function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW enzyme regulator activity Inferred from electronic annotation. Source: Compara
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

190

1

N6-acetyllysine Ref.25

Modified residue

218

1

Phosphoserine Ref.8 Ref.12 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.24 Ref.26 Ref.28

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.29

Mutagenesis

218

1

S → A: Loss of phosphorylation. Ref.21

Mutagenesis

260

1

W → A: Loss of dimerization. Ref.29

Mutagenesis

270

1

H → D: Loss of dimerization. Ref.29

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

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

361

Helix Strand Turn

Details...

Helix

23 – 34

12

Beta strand

38 – 45

8

Helix

50 – 58

9

Beta strand

85 – 88

4

Beta strand

95 – 102

8

Helix

118 – 133

16

Beta strand

148 – 153

6

Beta strand

155 – 159

5

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

Beta strand

243 – 245

3

Beta strand

254 – 258

5

Beta strand

261 – 264

4

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MAP4, COORDINATED EXPRESSION WITH SEPT2 AND SEPT7.
[11]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[12]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"Structural analysis of septin 2, 6, and 7 complexes." Low C., Macara I.G. J. Biol. Chem. 281:30697-30706(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SEPT6 AND SEPT7.
[14]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION.
[15]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION, COLOCALIZATION WITH POLYGLUTAMYLATED TUBULIN.
[16]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, MASS SPECTROMETRY. Tissue: Platelet.
[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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, MASS SPECTROMETRY. Tissue: Liver.
[21]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-218, MUTAGENESIS OF SER-218, TISSUE SPECIFICITY.
[22]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, MASS SPECTROMETRY.
[23]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SEPT9, ROLE IN BACTERIAL INFECTION.
[24]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[25]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-190, MASS SPECTROMETRY.
[26]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[27]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[28]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, MASS SPECTROMETRY.
[29]	"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] [Europe PMC] [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.
[30]	"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.721234.

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.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q15019. 7 interactions.

MINT

MINT-1433588.

STRING

9606.ENSP00000353157.

PTM databases

PhosphoSite

Q15019.

Polymorphism databases

DMDM

2500769.

2D gel databases

OGP

Q15019.

Proteomic databases

PaxDb

Q15019.

PRIDE

Q15019.

Protocols and materials databases

DNASU

4735.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000360051; ENSP00000353157; ENSG00000168385.
ENST00000391971; ENSP00000375832; ENSG00000168385.
ENST00000391973; ENSP00000375834; ENSG00000168385.
ENST00000401990; ENSP00000385109; ENSG00000168385.
ENST00000402092; ENSP00000385172; ENSG00000168385.

GeneID

4735.

KEGG

hsa:4735.

UCSC

uc002wbc.3. human.
uc010zop.2. human.

Organism-specific databases

CTD

4735.

GeneCards

GC02P242254.

HGNC

HGNC:7729. SEPT2.

HPA

CAB017190.
HPA018481.

MIM

601506. gene.

neXtProt

NX_Q15019.

PharmGKB

PA31535.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5019.

HOGENOM

HOG000233586.

HOVERGEN

HBG065093.

OMA

QDCFSTI.

OrthoDB

EOG47SSF3.

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. PTHR18884. 1 hit.

Pfam

PF00735. Septin. 1 hit.
[Graphical view]

PIRSF

PIRSF006698. Septin. 1 hit.

PRINTS

PR01740. SEPTIN2.

ProtoNet

Search...

Other

ChiTaRS

SEPT2. human.

EvolutionaryTrace

Q15019.

GenomeRNAi

4735.

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:	May 1, 2013
This is version 143 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.