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Q15019 (SEPT2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 153. 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·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length361 AA.
Sequence statusComplete.
Protein existenceEvidence 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.24

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.24 Ref.30 Ref.31

Subcellular location

Cytoplasm. Cytoplasmcytoskeleton. Cytoplasmcytoskeletonspindle. Chromosomecentromerekinetochore. Cleavage furrow. Midbody. Cytoplasmcell cortex. Cell projectioncilium 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.22

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 processCell cycle
Cell division
Mitosis
   Cellular componentCell membrane
Cell projection
Centromere
Chromosome
Cytoplasm
Cytoskeleton
Kinetochore
Membrane
   Coding sequence diversityAlternative splicing
   LigandGTP-binding
Nucleotide-binding
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcilium 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: Ensembl

regulation of L-glutamate transport

Inferred from electronic annotation. Source: Ensembl

regulation of protein localization

Inferred from electronic annotation. Source: Ensembl

smoothened signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentactin cytoskeleton

Inferred from direct assay. Source: HPA

cell surface

Inferred from electronic annotation. Source: Ensembl

ciliary 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: Ensembl

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

midbody

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleolus

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay PubMed 10942595. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

septin complex

Inferred from electronic annotation. Source: InterPro

spindle

Inferred from electronic annotation. Source: UniProtKB-SubCell

synapse

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

enzyme regulator activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SEPT6Q141414EBI-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 361361Septin-2
PRO_0000173515

Regions

Nucleotide binding44 – 518GTP
Nucleotide binding183 – 1919GTP
Region260 – 27011Important for dimerization

Sites

Binding site781GTP By similarity
Binding site1041GTP; via amide nitrogen By similarity
Binding site2411GTP; via amide nitrogen and carbonyl oxygen
Binding site2561GTP
Site1561Important for dimerization

Amino acid modifications

Modified residue171Phosphotyrosine By similarity
Modified residue1901N6-acetyllysine Ref.26
Modified residue2181Phosphoserine Ref.8 Ref.12 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.22 Ref.23 Ref.25 Ref.27 Ref.29

Natural variations

Alternative sequence11M → MPWISEGRATRPCLRVPSAR RGDEGLHQRDEASQKM in isoform 2.
VSP_038271

Experimental info

Mutagenesis1561F → D: Loss of dimerization. Ref.30
Mutagenesis2181S → A: Loss of phosphorylation. Ref.22
Mutagenesis2601W → A: Loss of dimerization. Ref.30
Mutagenesis2701H → D: Loss of dimerization. Ref.30
Sequence conflict691P → S in AAH14455. Ref.6
Sequence conflict721A → AALNTRKTLLW in AAH33559. Ref.6
Sequence conflict360 – 3612HV → TCKVMCTYKKSEKTLSWIKK KTFQMHDPAVCFQSLGGCHP HFNSTCA in BAA05893. Ref.2

Secondary structure

............................................ 361
Helix Strand Turn

Details...

Sequences

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

Last modified November 1, 1997. Version 1.
Checksum: 12CCBBE30806F92F

FASTA36141,487
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 4BD59305219D99B5
Show »

FASTA39645,461

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[21]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"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.
[23]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]"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.
[25]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[26]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[28]"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].
[29]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[30]"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.
[31]"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.

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.
RefSeqNP_001008491.1. NM_001008491.2.
NP_001008492.1. NM_001008492.2.
NP_001269901.1. NM_001282972.1.
NP_001269902.1. NM_001282973.1.
NP_004395.1. NM_004404.4.
NP_006146.1. NM_006155.2.
XP_005247068.1. XM_005247011.1.
XP_005247069.1. XM_005247012.1.
XP_005247070.1. XM_005247013.1.
UniGeneHs.721234.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2QA5X-ray3.40A/B1-315[»]
2QAGX-ray4.00A1-361[»]
2QNRX-ray2.60A/B22-320[»]
ProteinModelPortalQ15019.
SMRQ15019. Positions 34-305.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110812. 58 interactions.
DIPDIP-38220N.
IntActQ15019. 12 interactions.
MINTMINT-1433588.
STRING9606.ENSP00000353157.

PTM databases

PhosphoSiteQ15019.

Polymorphism databases

DMDM2500769.

2D gel databases

OGPQ15019.

Proteomic databases

PaxDbQ15019.
PRIDEQ15019.

Protocols and materials databases

DNASU4735.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000360051; ENSP00000353157; ENSG00000168385. [Q15019-1]
ENST00000391971; ENSP00000375832; ENSG00000168385. [Q15019-1]
ENST00000391973; ENSP00000375834; ENSG00000168385. [Q15019-1]
ENST00000401990; ENSP00000385109; ENSG00000168385.
ENST00000402092; ENSP00000385172; ENSG00000168385. [Q15019-1]
GeneID4735.
KEGGhsa:4735.
UCSCuc002wbc.3. human. [Q15019-1]
uc010zop.2. human. [Q15019-2]

Organism-specific databases

CTD4735.
GeneCardsGC02P242254.
HGNCHGNC:7729. SEPT2.
HPACAB017190.
HPA018481.
MIM601506. gene.
neXtProtNX_Q15019.
PharmGKBPA31535.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5019.
HOGENOMHOG000233586.
HOVERGENHBG065093.
KOK16942.
OrthoDBEOG79KPF0.
PhylomeDBQ15019.
TreeFamTF101079.

Gene expression databases

ArrayExpressQ15019.
BgeeQ15019.
CleanExHS_SEPT2.
GenevestigatorQ15019.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR000038. Cell_div_GTP-bd.
IPR027417. P-loop_NTPase.
IPR016491. Septin.
IPR008113. Septin2.
[Graphical view]
PANTHERPTHR18884. PTHR18884. 1 hit.
PfamPF00735. Septin. 1 hit.
[Graphical view]
PIRSFPIRSF006698. Septin. 1 hit.
PRINTSPR01740. SEPTIN2.
SUPFAMSSF52540. SSF52540. 1 hit.
ProtoNetSearch...

Other

ChiTaRSSEPT2. human.
EvolutionaryTraceQ15019.
GeneWikiSEPT2.
GenomeRNAi4735.
NextBio18256.
PROQ15019.
SOURCESearch...

Entry information

Entry nameSEPT2_HUMAN
AccessionPrimary (citable) accession number: Q15019
Secondary accession number(s): B4DGE8 expand/collapse secondary AC list , Q14132, Q53QU3, Q8IUK9, Q96CB0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: April 16, 2014
This is version 153 of the entry and version 1 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 2

Human chromosome 2: entries, gene names and cross-references to MIM