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Protein

Septin-1

Gene

SEPT1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Filament-forming cytoskeletal GTPase (By similarity). May play a role in cytokinesis (Potential).By similarityCurated

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei66 – 661GTPBy similarity
Binding sitei92 – 921GTP; via amide nitrogenBy similarity
Binding sitei229 – 2291GTP; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei245 – 2451GTPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi32 – 398GTPBy similarity
Nucleotide bindingi171 – 1799GTPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Septin-1
Alternative name(s):
LARP
Peanut-like protein 3
Serologically defined breast cancer antigen NY-BR-24
Gene namesi
Name:SEPT1
Synonyms:DIFF6, PNUTL3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Unplaced

Organism-specific databases

HGNCiHGNC:2879. SEPT1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi19 – 191S → A: No effect on phosphorylation. 1 Publication
Mutagenesisi206 – 2061S → A: No effect on phosphorylation. 1 Publication
Mutagenesisi248 – 2481S → A: Great reduction in phosphorylation. 1 Publication
Mutagenesisi307 – 3071S → A: Great reduction in phosphorylation. 1 Publication
Mutagenesisi312 – 3121S → A: No effect on phosphorylation. 1 Publication
Mutagenesisi315 – 3151S → A: Great reduction in phosphorylation. 1 Publication

Organism-specific databases

PharmGKBiPA24354.

Polymorphism and mutation databases

DMDMi20178107.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 367367Septin-1PRO_0000173513Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei206 – 2061Phosphoserine1 Publication
Modified residuei248 – 2481Phosphoserine; by AURKB2 Publications
Modified residuei307 – 3071Phosphoserine; by AURKB1 Publication
Modified residuei315 – 3151Phosphoserine; by AURKB2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8WYJ6.
PaxDbiQ8WYJ6.
PRIDEiQ8WYJ6.

PTM databases

PhosphoSiteiQ8WYJ6.

Expressioni

Tissue specificityi

Expressed at high levels in lymphoid and hematopoietic tissues.1 Publication

Gene expression databases

BgeeiQ8WYJ6.
CleanExiHS_SEPT1.
GenevestigatoriQ8WYJ6.

Organism-specific databases

HPAiHPA041566.

Interactioni

Subunit structurei

Septins polymerize into heterooligomeric protein complexes that form filaments, and can associate with cellular membranes, actin filaments and microtubules. GTPase activity is required for filament formation (By similarity). Interacts with AURKB.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
AMOTQ4VCS5-23EBI-693002,EBI-3891843
AURKBQ96GD46EBI-693002,EBI-624291
SEPT12Q8IYM13EBI-693002,EBI-2585067
SEPT5Q997195EBI-693002,EBI-373345
SEPT6Q141414EBI-693002,EBI-745901
TEX11Q8IYF33EBI-693002,EBI-742397

Protein-protein interaction databases

IntActiQ8WYJ6. 9 interactions.
MINTiMINT-1435466.
STRINGi9606.ENSP00000324511.

Structurei

3D structure databases

ProteinModelPortaliQ8WYJ6.
SMRiQ8WYJ6. Positions 22-295.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 296275Septin-type GAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG5019.
HOGENOMiHOG000233586.
HOVERGENiHBG065093.
InParanoidiQ8WYJ6.
KOiK13737.
PhylomeDBiQ8WYJ6.
TreeFamiTF101079.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR030379. G_SEPTIN_dom.
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 (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8WYJ6-1) [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

        10         20         30         40         50
MDKEYVGFAA LPNQLHRKSV KKGFDFTLMV AGESGLGKST LINSLFLTNL
60 70 80 90 100
YEDRQVPEAS ARLTQTLAIE RRGVEIEEGG VKVKLTLVDT PGFGDSVDCS
110 120 130 140 150
DCWLPVVKFI EEQFEQYLRD ESGLNRKNIQ DSRVHCCLYF ISPFGRGLRP
160 170 180 190 200
LDVAFLRAVH EKVNIIPVIG KADALMPQET QALKQKIRDQ LKEEEIHIYQ
210 220 230 240 250
FPECDSDEDE DFKRQDAEMK ESIPFAVVGS CEVVRDGGNR PVRGRRYSWG
260 270 280 290 300
TVEVENPHHC DFLNLRRMLV QTHLQDLKEV THDLLYEGYR ARCLQSLARP
310 320 330 340 350
GARDRASRSK LSRQSATEIP LPMLPLADTE KLIREKDEEL RRMQEMLEKM
360
QAQMQQSQAQ GEQSDAL
Length:367
Mass (Da):41,971
Last modified:April 16, 2002 - v2
Checksum:iE9C6BEF373CB0FC4
GO
Isoform 2 (identifier: Q8WYJ6-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     148-167: LRPLDVAFLRAVHEKVNIIP → SGGGILGAGAFREGWGVSAP
     168-367: Missing.

Note: No experimental confirmation available.

Show »
Length:167
Mass (Da):18,354
Checksum:i2C7A515F1236AAC4
GO

Sequence cautioni

The sequence AAK61491.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti60 – 601S → G in AAL40393 (Ref. 1) Curated
Sequence conflicti148 – 1503LRP → SR in AAL40393 (Ref. 1) Curated
Sequence conflicti240 – 2412RP → GL in AAL40393 (Ref. 1) Curated
Sequence conflicti324 – 3241L → P in AAL40393 (Ref. 1) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti80 – 801G → V.
Corresponds to variant rs34518080 [ dbSNP | Ensembl ].
VAR_051934

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei148 – 16720LRPLD…VNIIP → SGGGILGAGAFREGWGVSAP in isoform 2. 1 PublicationVSP_038269Add
BLAST
Alternative sequencei168 – 367200Missing in isoform 2. 1 PublicationVSP_038270Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF085235 mRNA. Translation: AAL40393.1.
AY034176 mRNA. Translation: AAK61491.1. Different initiation.
AK301045 mRNA. Translation: BAG62658.1.
BC012161 mRNA. Translation: AAH12161.1.
AL833004 mRNA. Translation: CAH56484.1.
AF308288 Genomic DNA. Translation: AAG48256.1.
RefSeqiNP_443070.5. NM_052838.4.
UniGeneiHs.632176.

Genome annotation databases

EnsembliENST00000571393; ENSP00000460441; ENSG00000180096.
GeneIDi1731.
KEGGihsa:1731.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF085235 mRNA. Translation: AAL40393.1.
AY034176 mRNA. Translation: AAK61491.1. Different initiation.
AK301045 mRNA. Translation: BAG62658.1.
BC012161 mRNA. Translation: AAH12161.1.
AL833004 mRNA. Translation: CAH56484.1.
AF308288 Genomic DNA. Translation: AAG48256.1.
RefSeqiNP_443070.5. NM_052838.4.
UniGeneiHs.632176.

3D structure databases

ProteinModelPortaliQ8WYJ6.
SMRiQ8WYJ6. Positions 22-295.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8WYJ6. 9 interactions.
MINTiMINT-1435466.
STRINGi9606.ENSP00000324511.

PTM databases

PhosphoSiteiQ8WYJ6.

Polymorphism and mutation databases

DMDMi20178107.

Proteomic databases

MaxQBiQ8WYJ6.
PaxDbiQ8WYJ6.
PRIDEiQ8WYJ6.

Protocols and materials databases

DNASUi1731.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000571393; ENSP00000460441; ENSG00000180096.
GeneIDi1731.
KEGGihsa:1731.

Organism-specific databases

CTDi1731.
GeneCardsiGC16M030389.
HGNCiHGNC:2879. SEPT1.
HPAiHPA041566.
MIMi612897. gene.
neXtProtiNX_Q8WYJ6.
PharmGKBiPA24354.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5019.
HOGENOMiHOG000233586.
HOVERGENiHBG065093.
InParanoidiQ8WYJ6.
KOiK13737.
PhylomeDBiQ8WYJ6.
TreeFamiTF101079.

Miscellaneous databases

ChiTaRSiSEPT1. human.
GeneWikiiSEPT1.
GenomeRNAii1731.
NextBioi7009.
PROiQ8WYJ6.
SOURCEiSearch...

Gene expression databases

BgeeiQ8WYJ6.
CleanExiHS_SEPT1.
GenevestigatoriQ8WYJ6.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR030379. G_SEPTIN_dom.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of a novel human gene, HSLARP."
    Tu Q., Yu L., Bi A., Zhang H., Zhao Y., Zhao S.
    Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Molecular cloning and characterization of human septins which are expressed in liver."
    Peng J., Yu L.
    Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "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: Spleen.
  4. "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: B-cell.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 79-367.
    Tissue: Stomach.
  6. "Humoral immunity to human breast cancer: antigen definition and quantitative analysis of mRNA expression."
    Scanlan M.J., Gout I., Gordon C.M., Williamson B., Stockert E., Gure A.O., Jaeger D., Chen Y.-T., Mackay A., O'Hare M.J., Old L.J.
    Cancer Immun. 1:4-4(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 93-367.
    Tissue: Mammary gland.
  7. "Septin1, a new interaction partner for human serine/threonine kinase aurora-B."
    Qi M., Yu W., Liu S., Jia H., Tang L., Shen M., Yan X., Saiyin H., Lang Q., Wan B., Zhao S., Yu L.
    Biochem. Biophys. Res. Commun. 336:994-1000(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH AURKB, PHOSPHORYLATION AT SER-248; SER-307 AND SER-315, MUTAGENESIS OF SER-19; SER-206; SER-248; SER-307; SER-312 AND SER-315.
  8. "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.
  9. "From midbody protein-protein interaction network construction to novel regulators in cytokinesis."
    Chen T.C., Lee S.A., Hong T.M., Shih J.Y., Lai J.M., Chiou H.Y., Yang S.C., Chan C.H., Kao C.Y., Yang P.C., Huang C.Y.
    J. Proteome Res. 8:4943-4953(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  10. "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-248 AND SER-315, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiSEPT1_HUMAN
AccessioniPrimary (citable) accession number: Q8WYJ6
Secondary accession number(s): B4DVE6
, Q658T1, Q8NEZ1, Q96EL4, Q9H285
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2002
Last sequence update: April 16, 2002
Last modified: May 27, 2015
This is version 125 of the entry and version 2 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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.