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Q15019

- SEPT2_HUMAN

UniProt

Q15019 - SEPT2_HUMAN

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Protein
Septin-2
Gene
SEPT2, DIFF6, KIAA0158, NEDD5
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei78 – 781GTP By similarity
Binding sitei104 – 1041GTP; via amide nitrogen By similarity
Sitei156 – 1561Important for dimerization
Binding sitei241 – 2411GTP; via amide nitrogen and carbonyl oxygen
Binding sitei256 – 2561GTP

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi44 – 518GTP
Nucleotide bindingi183 – 1919GTP

GO - Molecular functioni

  1. GTP binding Source: UniProtKB-KW
  2. enzyme regulator activity Source: Ensembl
  3. protein binding Source: UniProtKB

GO - Biological processi

  1. cilium assembly Source: UniProtKB
  2. mitotic nuclear division Source: UniProtKB-KW
  3. neuron projection development Source: Ensembl
  4. regulation of L-glutamate transport Source: Ensembl
  5. regulation of protein localization Source: Ensembl
  6. smoothened signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Septin-2
Alternative name(s):
Neural precursor cell expressed developmentally down-regulated protein 5
Short name:
NEDD-5
Gene namesi
Name:SEPT2
Synonyms:DIFF6, KIAA0158, NEDD5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:7729. SEPT2.

Subcellular locationi

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.1 Publication

GO - Cellular componenti

  1. actin cytoskeleton Source: HPA
  2. cell surface Source: Ensembl
  3. ciliary membrane Source: UniProtKB
  4. cleavage furrow Source: UniProtKB-SubCell
  5. condensed chromosome kinetochore Source: UniProtKB-SubCell
  6. cytoplasm Source: UniProtKB
  7. exocyst Source: Ensembl
  8. extracellular vesicular exosome Source: UniProt
  9. midbody Source: UniProtKB-SubCell
  10. nucleolus Source: HPA
  11. nucleus Source: UniProtKB
  12. perinuclear region of cytoplasm Source: Ensembl
  13. septin complex Source: InterPro
  14. spindle Source: UniProtKB-SubCell
  15. synapse Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi156 – 1561F → D: Loss of dimerization. 1 Publication
Mutagenesisi218 – 2181S → A: Loss of phosphorylation. 1 Publication
Mutagenesisi260 – 2601W → A: Loss of dimerization. 1 Publication
Mutagenesisi270 – 2701H → D: Loss of dimerization. 1 Publication

Organism-specific databases

PharmGKBiPA31535.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 361361Septin-2
PRO_0000173515Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei17 – 171Phosphotyrosine By similarity
Modified residuei190 – 1901N6-acetyllysine1 Publication
Modified residuei218 – 2181Phosphoserine12 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ15019.
PaxDbiQ15019.
PRIDEiQ15019.

2D gel databases

OGPiQ15019.

PTM databases

PhosphoSiteiQ15019.

Expressioni

Tissue specificityi

Widely expressed. Up-regulated in liver cancer.2 Publications

Gene expression databases

ArrayExpressiQ15019.
BgeeiQ15019.
CleanExiHS_SEPT2.
GenevestigatoriQ15019.

Organism-specific databases

HPAiCAB017190.
HPA018481.

Interactioni

Subunit structurei

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 MAP4.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SEPT6Q141416EBI-741220,EBI-745901

Protein-protein interaction databases

BioGridi110812. 59 interactions.
DIPiDIP-38220N.
IntActiQ15019. 12 interactions.
MINTiMINT-1433588.
STRINGi9606.ENSP00000353157.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi23 – 3412
Beta strandi38 – 458
Helixi50 – 589
Beta strandi85 – 884
Beta strandi95 – 1028
Helixi118 – 13316
Beta strandi148 – 1536
Beta strandi155 – 1595
Helixi162 – 17110
Turni172 – 1743
Beta strandi177 – 1815
Helixi184 – 1863
Helixi189 – 20517
Helixi225 – 2328
Beta strandi236 – 2383
Beta strandi243 – 2453
Beta strandi254 – 2585
Beta strandi261 – 2644
Turni268 – 2703
Helixi273 – 28210
Helixi284 – 29310
Helixi295 – 30511

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QA5X-ray3.40A/B1-315[»]
2QAGX-ray4.00A1-361[»]
2QNRX-ray2.60A/B22-320[»]
ProteinModelPortaliQ15019.
SMRiQ15019. Positions 34-305.

Miscellaneous databases

EvolutionaryTraceiQ15019.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini34 – 306273Septin-type G
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni260 – 27011Important for dimerization
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG5019.
HOGENOMiHOG000233586.
HOVERGENiHBG065093.
KOiK16942.
OrthoDBiEOG79KPF0.
PhylomeDBiQ15019.
TreeFamiTF101079.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR000038. Cell_div_GTP-bd.
IPR027417. P-loop_NTPase.
IPR016491. Septin.
IPR008113. Septin2.
[Graphical view]
PANTHERiPTHR18884. PTHR18884. 1 hit.
PfamiPF00735. Septin. 1 hit.
[Graphical view]
PIRSFiPIRSF006698. Septin. 1 hit.
PRINTSiPR01740. SEPTIN2.
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS51719. G_SEPTIN. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q15019-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MSKQQPTQFI NPETPGYVGF ANLPNQVHRK SVKKGFEFTL MVVGESGLGK    50
STLINSLFLT DLYPERVIPG AAEKIERTVQ IEASTVEIEE RGVKLRLTVV 100
DTPGYGDAIN CRDCFKTIIS YIDEQFERYL HDESGLNRRH IIDNRVHCCF 150
YFISPFGHGL KPLDVAFMKA IHNKVNIVPV IAKADTLTLK ERERLKKRIL 200
DEIEEHNIKI YHLPDAESDE DEDFKEQTRL LKASIPFSVV GSNQLIEAKG 250
KKVRGRLYPW GVVEVENPEH NDFLKLRTML ITHMQDLQEV TQDLHYENFR 300
SERLKRGGRK VENEDMNKDQ ILLEKEAELR RMQEMIARMQ AQMQMQMQGG 350
DGDGGALGHH V 361
Length:361
Mass (Da):41,487
Last modified:November 1, 1997 - v1
Checksum:i12CCBBE30806F92F
GO
Isoform 2 (identifier: Q15019-2) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:396
Mass (Da):45,461
Checksum:i4BD59305219D99B5
GO
Isoform 3 (identifier: Q15019-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     72-72: A → AALNTRKTLLW

Note: No experimental confirmation available.

Show »
Length:371
Mass (Da):42,685
Checksum:i0ED0C05E2DA308B4
GO

Sequence cautioni

The sequence BAA09928.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
The sequence AAY14718.1 differs from that shown. Reason: Erroneous gene model prediction.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MPWISEGRATRPCLRVPSAR RGDEGLHQRDEASQKM in isoform 2.
VSP_038271
Alternative sequencei72 – 721A → AALNTRKTLLW in isoform 3.
VSP_055176

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti69 – 691P → S in AAH14455. 1 Publication
Sequence conflicti360 – 3612HV → TCKVMCTYKKSEKTLSWIKK KTFQMHDPAVCFQSLGGCHP HFNSTCA in BAA05893. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS2548.1. [Q15019-1]
RefSeqiNP_001008491.1. NM_001008491.2. [Q15019-1]
NP_001008492.1. NM_001008492.2. [Q15019-1]
NP_001269901.1. NM_001282972.1. [Q15019-2]
NP_001269902.1. NM_001282973.1.
NP_004395.1. NM_004404.4. [Q15019-1]
NP_006146.1. NM_006155.2. [Q15019-1]
XP_005247068.1. XM_005247011.1. [Q15019-1]
XP_005247069.1. XM_005247012.1. [Q15019-1]
XP_005247070.1. XM_005247013.1. [Q15019-1]
XP_006712611.1. XM_006712548.1. [Q15019-1]
XP_006712612.1. XM_006712549.1. [Q15019-1]
UniGeneiHs.721234.

Genome annotation databases

EnsembliENST00000360051; ENSP00000353157; ENSG00000168385. [Q15019-1]
ENST00000391971; ENSP00000375832; ENSG00000168385. [Q15019-1]
ENST00000391973; ENSP00000375834; ENSG00000168385. [Q15019-1]
ENST00000401990; ENSP00000385109; ENSG00000168385.
ENST00000402092; ENSP00000385172; ENSG00000168385. [Q15019-1]
GeneIDi4735.
KEGGihsa:4735.
UCSCiuc002wbc.3. human. [Q15019-1]
uc010zop.2. human. [Q15019-2]

Polymorphism databases

DMDMi2500769.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS2548.1. [Q15019-1 ]
RefSeqi NP_001008491.1. NM_001008491.2. [Q15019-1 ]
NP_001008492.1. NM_001008492.2. [Q15019-1 ]
NP_001269901.1. NM_001282972.1. [Q15019-2 ]
NP_001269902.1. NM_001282973.1.
NP_004395.1. NM_004404.4. [Q15019-1 ]
NP_006146.1. NM_006155.2. [Q15019-1 ]
XP_005247068.1. XM_005247011.1. [Q15019-1 ]
XP_005247069.1. XM_005247012.1. [Q15019-1 ]
XP_005247070.1. XM_005247013.1. [Q15019-1 ]
XP_006712611.1. XM_006712548.1. [Q15019-1 ]
XP_006712612.1. XM_006712549.1. [Q15019-1 ]
UniGenei Hs.721234.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali Q15019.
SMRi Q15019. Positions 34-305.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110812. 59 interactions.
DIPi DIP-38220N.
IntActi Q15019. 12 interactions.
MINTi MINT-1433588.
STRINGi 9606.ENSP00000353157.

PTM databases

PhosphoSitei Q15019.

Polymorphism databases

DMDMi 2500769.

2D gel databases

OGPi Q15019.

Proteomic databases

MaxQBi Q15019.
PaxDbi Q15019.
PRIDEi Q15019.

Protocols and materials databases

DNASUi 4735.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000360051 ; ENSP00000353157 ; ENSG00000168385 . [Q15019-1 ]
ENST00000391971 ; ENSP00000375832 ; ENSG00000168385 . [Q15019-1 ]
ENST00000391973 ; ENSP00000375834 ; ENSG00000168385 . [Q15019-1 ]
ENST00000401990 ; ENSP00000385109 ; ENSG00000168385 .
ENST00000402092 ; ENSP00000385172 ; ENSG00000168385 . [Q15019-1 ]
GeneIDi 4735.
KEGGi hsa:4735.
UCSCi uc002wbc.3. human. [Q15019-1 ]
uc010zop.2. human. [Q15019-2 ]

Organism-specific databases

CTDi 4735.
GeneCardsi GC02P242254.
HGNCi HGNC:7729. SEPT2.
HPAi CAB017190.
HPA018481.
MIMi 601506. gene.
neXtProti NX_Q15019.
PharmGKBi PA31535.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5019.
HOGENOMi HOG000233586.
HOVERGENi HBG065093.
KOi K16942.
OrthoDBi EOG79KPF0.
PhylomeDBi Q15019.
TreeFami TF101079.

Miscellaneous databases

ChiTaRSi SEPT2. human.
EvolutionaryTracei Q15019.
GeneWikii SEPT2.
GenomeRNAii 4735.
NextBioi 18256.
PROi Q15019.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q15019.
Bgeei Q15019.
CleanExi HS_SEPT2.
Genevestigatori Q15019.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
InterProi IPR000038. Cell_div_GTP-bd.
IPR027417. P-loop_NTPase.
IPR016491. Septin.
IPR008113. Septin2.
[Graphical view ]
PANTHERi PTHR18884. PTHR18884. 1 hit.
Pfami PF00735. Septin. 1 hit.
[Graphical view ]
PIRSFi PIRSF006698. Septin. 1 hit.
PRINTSi PR01740. SEPTIN2.
SUPFAMi SSF52540. SSF52540. 1 hit.
PROSITEi PS51719. G_SEPTIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] (ISOFORMS 1 AND 3).
    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, 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. 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. 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. 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. 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. 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.

Entry informationi

Entry nameiSEPT2_HUMAN
AccessioniPrimary (citable) accession number: Q15019
Secondary accession number(s): B4DGE8
, Q14132, Q53QU3, Q8IUK9, Q96CB0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: September 3, 2014
This is version 157 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Miscellaneous

Coordinated expression with SEPT6 and SEPT7.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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