SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q14141

- SEPT6_HUMAN

UniProt

Q14141 - SEPT6_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Septin-6

Gene
SEPT6, KIAA0128, SEP2
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. Involved in cytokinesis. May play a role in HCV RNA replication.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei104 – 1041GTP; via amide nitrogen By similarity
Binding sitei239 – 2391GTP; via amide nitrogen and carbonyl oxygen By similarity
Binding sitei254 – 2541GTP By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi49 – 568GTP
Nucleotide bindingi185 – 1939GTP

GO - Molecular functioni

  1. GTP binding Source: UniProtKB
  2. protein binding Source: UniProtKB

GO - Biological processi

  1. cytokinesis Source: UniProtKB
  2. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Host-virus interaction

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Septin-6
Gene namesi
Name:SEPT6
Synonyms:KIAA0128, SEP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:15848. SEPT6.

Subcellular locationi

Cytoplasm. Cytoplasmcytoskeletonspindle. Chromosomecentromerekinetochore. Cleavage furrow. Midbody
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.1 Publication

GO - Cellular componenti

  1. axon terminus Source: Ensembl
  2. cleavage furrow Source: UniProtKB-SubCell
  3. condensed chromosome kinetochore Source: UniProtKB-SubCell
  4. midbody Source: UniProtKB-SubCell
  5. septin complex Source: InterPro
  6. spindle Source: UniProtKB-SubCell
  7. synaptic vesicle Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134941944.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 434433Septin-6PRO_0000173525Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei367 – 3671N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ14141.
PaxDbiQ14141.
PeptideAtlasiQ14141.
PRIDEiQ14141.

2D gel databases

OGPiQ14141.

PTM databases

PhosphoSiteiQ14141.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

ArrayExpressiQ14141.
BgeeiQ14141.
CleanExiHS_SEPT6.
GenevestigatoriQ14141.

Organism-specific databases

HPAiHPA005665.

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. Within the trimer, directly interacts with SEPT2 and SEPT7. Also interacts with SEPT9 and SEPT12. Interaction with SEPT12 alters filament structure. Interacts with SOCS7. Interacts with HCV NS5B and with HNRNPA1.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
P279584EBI-745901,EBI-6904388From a different organism.
HNRNPA1P096513EBI-745901,EBI-352662
SEPT12Q8IYM13EBI-745901,EBI-2585067
SEPT2Q150196EBI-745901,EBI-741220
SOCS7O14512-12EBI-745901,EBI-1539617

Protein-protein interaction databases

BioGridi116770. 13 interactions.
DIPiDIP-38218N.
IntActiQ14141. 10 interactions.
MINTiMINT-4532787.
STRINGi9606.ENSP00000341524.

Structurei

Secondary structure

1
434
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi30 – 356
Beta strandi42 – 487
Helixi56 – 638
Beta strandi80 – 8910
Beta strandi94 – 10310
Helixi111 – 1144
Helixi116 – 13217
Beta strandi150 – 1556
Helixi164 – 1729
Beta strandi177 – 1848
Helixi186 – 1883
Helixi191 – 20515
Turni229 – 2313
Helixi272 – 2809
Helixi285 – 2939
Helixi296 – 3038
Turni304 – 3063

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QAGX-ray4.00B1-427[»]
ProteinModelPortaliQ14141.
SMRiQ14141. Positions 41-307.

Miscellaneous databases

EvolutionaryTraceiQ14141.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini39 – 305267Septin-type GAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili321 – 40989 Reviewed predictionAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG5019.
HOVERGENiHBG065093.
KOiK16939.
OrthoDBiEOG7J9VQK.
PhylomeDBiQ14141.
TreeFamiTF101080.

Family and domain databases

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

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform II (identifier: Q14141-1) [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

MAATDIARQV GEGCRTVPLA GHVGFDSLPD QLVNKSVSQG FCFNILCVGE    50
TGLGKSTLMD TLFNTKFEGE PATHTQPGVQ LQSNTYDLQE SNVRLKLTIV 100
STVGFGDQIN KEDSYKPIVE FIDAQFEAYL QEELKIRRVL HTYHDSRIHV 150
CLYFIAPTGH SLKSLDLVTM KKLDSKVNII PIIAKADAIS KSELTKFKIK 200
ITSELVSNGV QIYQFPTDDE SVAEINGTMN AHLPFAVIGS TEELKIGNKM 250
MRARQYPWGT VQVENEAHCD FVKLREMLIR VNMEDLREQT HTRHYELYRR 300
CKLEEMGFKD TDPDSKPFSL QETYEAKRNE FLGELQKKEE EMRQMFVQRV 350
KEKEAELKEA EKELHEKFDR LKKLHQDEKK KLEDKKKSLD DEVNAFKQRK 400
TAAELLQSQG SQAGGSQTLK RDKEKKNNPW LCTE 434
Length:434
Mass (Da):49,717
Last modified:January 23, 2007 - v4
Checksum:iE684AE6A93B32362
GO
Isoform I (identifier: Q14141-2) [UniParc]FASTAAdd to Basket

Also known as: III

The sequence of this isoform differs from the canonical sequence as follows:
     428-434: Missing.

Show »
Length:427
Mass (Da):48,873
Checksum:i62EB88E308386ADE
GO
Isoform IV (identifier: Q14141-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     263-267: VENEA → AAREV
     268-434: Missing.

Show »
Length:267
Mass (Da):29,584
Checksum:i7DD6D37AE3844845
GO
Isoform V (identifier: Q14141-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     428-434: NPWLCTE → FF

Show »
Length:429
Mass (Da):49,167
Checksum:i3D8EE2EB88E30838
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei263 – 2675VENEA → AAREV in isoform IV. VSP_006051
Alternative sequencei268 – 434167Missing in isoform IV. VSP_006052Add
BLAST
Alternative sequencei428 – 4347Missing in isoform I. VSP_006053
Alternative sequencei428 – 4347NPWLCTE → FF in isoform V. VSP_006054

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti406 – 4061L → P in AAH09291. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF403058 mRNA. Translation: AAK98547.1.
AF403059 mRNA. Translation: AAK98548.1.
AF403060 mRNA. Translation: AAK98549.1.
AF403061 mRNA. Translation: AAK98550.1.
AF403062 mRNA. Translation: AAK98551.1.
AL355348, AC004913, AC005052 Genomic DNA. Translation: CAI41426.1.
BC009291 mRNA. Translation: AAH09291.1.
BC011922 mRNA. Translation: AAH11922.3.
BC036240 mRNA. Translation: AAH36240.1.
D50918 mRNA. Translation: BAA09477.1.
CCDSiCCDS14583.1. [Q14141-4]
CCDS14584.1. [Q14141-1]
CCDS14585.1. [Q14141-2]
RefSeqiNP_055944.2. NM_015129.5. [Q14141-1]
NP_665798.1. NM_145799.3. [Q14141-2]
NP_665799.1. NM_145800.3. [Q14141-2]
NP_665801.1. NM_145802.3. [Q14141-4]
XP_006724812.1. XM_006724749.1. [Q14141-2]
XP_006724813.1. XM_006724750.1. [Q14141-2]
UniGeneiHs.496666.

Genome annotation databases

EnsembliENST00000343984; ENSP00000341524; ENSG00000125354. [Q14141-1]
ENST00000354228; ENSP00000346169; ENSG00000125354. [Q14141-4]
ENST00000360156; ENSP00000353278; ENSG00000125354. [Q14141-2]
ENST00000394610; ENSP00000378108; ENSG00000125354. [Q14141-2]
ENST00000460411; ENSP00000435818; ENSG00000125354. [Q14141-3]
ENST00000489216; ENSP00000418715; ENSG00000125354. [Q14141-2]
GeneIDi23157.
KEGGihsa:23157.
UCSCiuc004ers.3. human. [Q14141-1]

Polymorphism databases

DMDMi20178343.

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
AF403058 mRNA. Translation: AAK98547.1 .
AF403059 mRNA. Translation: AAK98548.1 .
AF403060 mRNA. Translation: AAK98549.1 .
AF403061 mRNA. Translation: AAK98550.1 .
AF403062 mRNA. Translation: AAK98551.1 .
AL355348 , AC004913 , AC005052 Genomic DNA. Translation: CAI41426.1 .
BC009291 mRNA. Translation: AAH09291.1 .
BC011922 mRNA. Translation: AAH11922.3 .
BC036240 mRNA. Translation: AAH36240.1 .
D50918 mRNA. Translation: BAA09477.1 .
CCDSi CCDS14583.1. [Q14141-4 ]
CCDS14584.1. [Q14141-1 ]
CCDS14585.1. [Q14141-2 ]
RefSeqi NP_055944.2. NM_015129.5. [Q14141-1 ]
NP_665798.1. NM_145799.3. [Q14141-2 ]
NP_665799.1. NM_145800.3. [Q14141-2 ]
NP_665801.1. NM_145802.3. [Q14141-4 ]
XP_006724812.1. XM_006724749.1. [Q14141-2 ]
XP_006724813.1. XM_006724750.1. [Q14141-2 ]
UniGenei Hs.496666.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2QAG X-ray 4.00 B 1-427 [» ]
ProteinModelPortali Q14141.
SMRi Q14141. Positions 41-307.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116770. 13 interactions.
DIPi DIP-38218N.
IntActi Q14141. 10 interactions.
MINTi MINT-4532787.
STRINGi 9606.ENSP00000341524.

PTM databases

PhosphoSitei Q14141.

Polymorphism databases

DMDMi 20178343.

2D gel databases

OGPi Q14141.

Proteomic databases

MaxQBi Q14141.
PaxDbi Q14141.
PeptideAtlasi Q14141.
PRIDEi Q14141.

Protocols and materials databases

DNASUi 23157.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000343984 ; ENSP00000341524 ; ENSG00000125354 . [Q14141-1 ]
ENST00000354228 ; ENSP00000346169 ; ENSG00000125354 . [Q14141-4 ]
ENST00000360156 ; ENSP00000353278 ; ENSG00000125354 . [Q14141-2 ]
ENST00000394610 ; ENSP00000378108 ; ENSG00000125354 . [Q14141-2 ]
ENST00000460411 ; ENSP00000435818 ; ENSG00000125354 . [Q14141-3 ]
ENST00000489216 ; ENSP00000418715 ; ENSG00000125354 . [Q14141-2 ]
GeneIDi 23157.
KEGGi hsa:23157.
UCSCi uc004ers.3. human. [Q14141-1 ]

Organism-specific databases

CTDi 23157.
GeneCardsi GC0XM118750.
HGNCi HGNC:15848. SEPT6.
HPAi HPA005665.
MIMi 300683. gene.
neXtProti NX_Q14141.
PharmGKBi PA134941944.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5019.
HOVERGENi HBG065093.
KOi K16939.
OrthoDBi EOG7J9VQK.
PhylomeDBi Q14141.
TreeFami TF101080.

Miscellaneous databases

ChiTaRSi SEPT6. human.
EvolutionaryTracei Q14141.
GeneWikii SEPT6.
GenomeRNAii 23157.
NextBioi 44499.
PROi Q14141.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q14141.
Bgeei Q14141.
CleanExi HS_SEPT6.
Genevestigatori Q14141.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "SEPTIN6, a human homologue to mouse Septin6, is fused to MLL in infant acute myeloid leukemia with complex chromosomal abnormalities involving 11q23 and Xq24."
    Ono R., Taki T., Taketani T., Kawaguchi H., Taniwaki M., Okamura T., Kawa K., Hanada R., Kobayashi M., Hayashi Y.
    Cancer Res. 62:333-337(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS I; II; IV AND V).
  2. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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] (ISOFORMS II AND V).
    Tissue: Muscle, Placenta and Testis.
  4. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-8, ACETYLATION AT ALA-2.
    Tissue: Platelet.
  5. "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] OF 4-427 (ISOFORM I).
    Tissue: Bone marrow.
  6. "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.
  7. "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: COORDINATED EXPRESSION WITH SEPT2 AND SEPT7.
  8. "A mitotic septin scaffold required for mammalian chromosome congression and segregation."
    Spiliotis E.T., Kinoshita M., Nelson W.J.
    Science 307:1781-1785(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  9. "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 SEPT2 AND SEPT7.
  10. "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, INTERACTION WITH SOCS7.
  11. "SEPT12 interacts with SEPT6 and this interaction alters the filament structure of SEPT6 in Hela cells."
    Ding X., Yu W., Liu M., Shen S., Chen F., Wan B., Yu L.
    J. Biochem. Mol. Biol. 40:973-978(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SEPT12.
  12. "An RNA-binding protein, hnRNP A1, and a scaffold protein, septin 6, facilitate hepatitis C virus replication."
    Kim C.S., Seol S.K., Song O.-K., Park J.H., Jang S.K.
    J. Virol. 81:3852-3865(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HNRNPA1 AND HCV NS5B, FUNCTION.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  14. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: INTERACTION WITH SEPT9.
  16. "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-367, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. Cited for: X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) OF 1-427 IN COMPLEX WITH GTP, ELECTRON MICROSCOPY OF SEPTIN COMPLEX, SUBUNIT.

Entry informationi

Entry nameiSEPT6_HUMAN
AccessioniPrimary (citable) accession number: Q14141
Secondary accession number(s): Q5JTK0
, Q969W5, Q96A13, Q96GR1, Q96P86, Q96P87
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 133 of the entry and version 4 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 SEPT2 and SEPT7.

Keywords - Technical termi

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

Documents

  1. Human chromosome X
    Human chromosome X: 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

Similar proteinsi