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Q99719

- SEPT5_HUMAN

UniProt

Q99719 - SEPT5_HUMAN

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Protein

Septin-5

Gene

SEPT5

Organism
Homo sapiens (Human)
Status
Reviewed - 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). May play a role in platelet secretion (By similarity).By similarityCurated

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei85 – 851GTPBy similarity
Binding sitei111 – 1111GTP; via amide nitrogenBy similarity
Binding sitei248 – 2481GTP; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei263 – 2631GTPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi51 – 588GTPBy similarity
Nucleotide bindingi190 – 1989GTPBy similarity

GO - Molecular functioni

  1. GTPase activity Source: ParkinsonsUK-UCL
  2. GTP binding Source: UniProtKB-KW
  3. structural molecule activity Source: ProtInc

GO - Biological processi

  1. cytokinesis Source: ProtInc
  2. GTP catabolic process Source: GOC
  3. regulation of exocytosis Source: UniProtKB
  4. regulation of synaptic vesicle exocytosis Source: ParkinsonsUK-UCL
  5. synaptic vesicle targeting Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Septin-5
Alternative name(s):
Cell division control-related protein 1
Short name:
CDCrel-1
Peanut-like protein 1
Gene namesi
Name:SEPT5
Synonyms:PNUTL1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:9164. SEPT5.

Subcellular locationi

Cytoplasm By similarity. Cytoplasmcytoskeleton By similarity
Note: In platelets, found in areas surrounding alpha-granules.

GO - Cellular componenti

  1. plasma membrane Source: UniProtKB
  2. septin complex Source: InterPro
  3. synaptic vesicle Source: UniProtKB
  4. terminal bouton Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33486.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 369369Septin-5PRO_0000173521Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei225 – 2251Phosphoserine2 Publications
Modified residuei327 – 3271Phosphoserine1 Publication
Modified residuei336 – 3361PhosphothreonineBy similarity

Post-translational modificationi

In platelets, phosphorylated in response to thrombin, phorbol-12-myristate-13-acetate and collagen.3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ99719.
PaxDbiQ99719.
PRIDEiQ99719.

2D gel databases

UCD-2DPAGEQ99719.

PTM databases

PhosphoSiteiQ99719.

Expressioni

Tissue specificityi

Expressed at high levels in the CNS, as well as in heart and platelets (at protein level).2 Publications

Gene expression databases

BgeeiQ99719.
CleanExiHS_SEPT5.
ExpressionAtlasiQ99719. baseline and differential.
GenevestigatoriQ99719.

Organism-specific databases

HPAiCAB016120.

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 SEPT2 and SEPT5. In platelets, associated with a complex containing STX4. Interacts with PARK2. This interaction leads to SEPT5 ubiquitination and degradation (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
SEPT11Q9NVA26EBI-373345,EBI-957999

Protein-protein interaction databases

BioGridi111414. 21 interactions.
IntActiQ99719. 8 interactions.
MINTiMINT-6943161.
STRINGi9606.ENSP00000391311.

Structurei

3D structure databases

ProteinModelPortaliQ99719.
SMRiQ99719. Positions 41-309.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini41 – 314274Septin-type GAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili338 – 36932Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG5019.
GeneTreeiENSGT00760000118899.
HOGENOMiHOG000233586.
HOVERGENiHBG065093.
InParanoidiQ99719.
KOiK04557.
OrthoDBiEOG79KPF0.
PhylomeDBiQ99719.
TreeFamiTF101079.

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 (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q99719-1) [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
MSTGLRYKSK LATPEDKQDI DKQYVGFATL PNQVHRKSVK KGFDFTLMVA
60 70 80 90 100
GESGLGKSTL VHSLFLTDLY KDRKLLSAEE RISQTVEILK HTVDIEEKGV
110 120 130 140 150
KLKLTIVDTP GFGDAVNNTE CWKPITDYVD QQFEQYFRDE SGLNRKNIQD
160 170 180 190 200
NRVHCCLYFI SPFGHGLRPV DVGFMKALHE KVNIVPLIAK ADCLVPSEIR
210 220 230 240 250
KLKERIREEI DKFGIHVYQF PECDSDEDED FKQQDRELKE SAPFAVIGSN
260 270 280 290 300
TVVEAKGQRV RGRLYPWGIV EVENQAHCDF VKLRNMLIRT HMHDLKDVTC
310 320 330 340 350
DVHYENYRAH CIQQMTSKLT QDSRMESPIP ILPLPTPDAE TEKLIRMKDE
360
ELRRMQEMLQ RMKQQMQDQ
Length:369
Mass (Da):42,777
Last modified:May 1, 1997 - v1
Checksum:i47054765DEA10D33
GO
Isoform 2 (identifier: Q99719-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-18: MSTGLRYKSKLATPEDKQ → MDSLAAPQDRLVEQLLSPRTQAQRRLK
     272-369: VENQAHCDFV...QRMKQQMQDQ → GALRLREAAQ...PAAAHPGRRD

Note: No experimental confirmation available.

Show »
Length:346
Mass (Da):39,332
Checksum:i380EACD6A7BFE814
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti224 – 2241D → N in CAA72332. (PubMed:9385360)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1818MSTGL…PEDKQ → MDSLAAPQDRLVEQLLSPRT QAQRRLK in isoform 2. 1 PublicationVSP_042689Add
BLAST
Alternative sequencei272 – 36998VENQA…QMQDQ → GALRLREAAQHAHPHAYARP QGRDVRRALRELPRALHPAD DQQTDPGQPHGEPHPDPAAA HPGRRD in isoform 2. 1 PublicationVSP_042690Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U74628 mRNA. Translation: AAB93438.1.
Y11593 mRNA. Translation: CAA72332.1.
AF006988 Genomic DNA. Translation: AAC39779.1.
CR456545 mRNA. Translation: CAG30431.1.
AK056273 mRNA. Translation: BAB71133.1.
AC000093 Genomic DNA. No translation available.
CH471176 Genomic DNA. Translation: EAX03032.1.
BC025261 mRNA. Translation: AAH25261.1.
CCDSiCCDS13764.1. [Q99719-1]
CCDS56224.1. [Q99719-2]
RefSeqiNP_001009939.1. NM_001009939.2. [Q99719-2]
NP_002679.2. NM_002688.5. [Q99719-1]
UniGeneiHs.728762.

Genome annotation databases

EnsembliENST00000438754; ENSP00000394541; ENSG00000184702. [Q99719-2]
ENST00000455784; ENSP00000391311; ENSG00000184702. [Q99719-1]
GeneIDi5413.
KEGGihsa:5413.
UCSCiuc002zpv.2. human. [Q99719-1]
uc002zpw.1. human. [Q99719-2]

Polymorphism databases

DMDMi6685760.

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
U74628 mRNA. Translation: AAB93438.1 .
Y11593 mRNA. Translation: CAA72332.1 .
AF006988 Genomic DNA. Translation: AAC39779.1 .
CR456545 mRNA. Translation: CAG30431.1 .
AK056273 mRNA. Translation: BAB71133.1 .
AC000093 Genomic DNA. No translation available.
CH471176 Genomic DNA. Translation: EAX03032.1 .
BC025261 mRNA. Translation: AAH25261.1 .
CCDSi CCDS13764.1. [Q99719-1 ]
CCDS56224.1. [Q99719-2 ]
RefSeqi NP_001009939.1. NM_001009939.2. [Q99719-2 ]
NP_002679.2. NM_002688.5. [Q99719-1 ]
UniGenei Hs.728762.

3D structure databases

ProteinModelPortali Q99719.
SMRi Q99719. Positions 41-309.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111414. 21 interactions.
IntActi Q99719. 8 interactions.
MINTi MINT-6943161.
STRINGi 9606.ENSP00000391311.

PTM databases

PhosphoSitei Q99719.

Polymorphism databases

DMDMi 6685760.

2D gel databases

UCD-2DPAGE Q99719.

Proteomic databases

MaxQBi Q99719.
PaxDbi Q99719.
PRIDEi Q99719.

Protocols and materials databases

DNASUi 5413.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000438754 ; ENSP00000394541 ; ENSG00000184702 . [Q99719-2 ]
ENST00000455784 ; ENSP00000391311 ; ENSG00000184702 . [Q99719-1 ]
GeneIDi 5413.
KEGGi hsa:5413.
UCSCi uc002zpv.2. human. [Q99719-1 ]
uc002zpw.1. human. [Q99719-2 ]

Organism-specific databases

CTDi 5413.
GeneCardsi GC22P019701.
H-InvDB HIX0016241.
HGNCi HGNC:9164. SEPT5.
HPAi CAB016120.
MIMi 602724. gene.
neXtProti NX_Q99719.
PharmGKBi PA33486.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5019.
GeneTreei ENSGT00760000118899.
HOGENOMi HOG000233586.
HOVERGENi HBG065093.
InParanoidi Q99719.
KOi K04557.
OrthoDBi EOG79KPF0.
PhylomeDBi Q99719.
TreeFami TF101079.

Miscellaneous databases

ChiTaRSi SEPT5. human.
GeneWikii SEPT5.
GenomeRNAii 5413.
NextBioi 20957.
PROi Q99719.
SOURCEi Search...

Gene expression databases

Bgeei Q99719.
CleanExi HS_SEPT5.
ExpressionAtlasi Q99719. baseline and differential.
Genevestigatori Q99719.

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. "Alternative expression of platelet glycoprotein Ib(beta) mRNA from an adjacent 5' gene with an imperfect polyadenylation signal sequence."
    Zieger B., Hashimoto Y., Ware J.
    J. Clin. Invest. 99:520-525(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Brain.
  2. "A human gene similar to Drosophila melanogaster peanut maps to the DiGeorge syndrome region of 22q11."
    McKie J., Sutherland H., Harvey E., Kim U.J., Scambler P.J.
    Hum. Genet. 101:6-12(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Heart.
  3. "Structure and expression of the human septin gene HCDCREL-1."
    Yagi M., Zieger B., Roth G.J., Ware J.
    Gene 212:229-236(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Brain.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  5. "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).
  6. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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: Lung.
  9. Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 23-36; 42-71; 82-90; 182-190; 297-308 AND 325-343, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
  10. "Human septin-septin interaction: CDCrel-1 partners with KIAA0202."
    Blaeser S., Jersch K., Hainmann I., Wunderle D., Zgaga-Griesz A., Busse A., Zieger B.
    FEBS Lett. 519:169-172(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SEPT8, TISSUE SPECIFICITY.
  11. Cited for: IDENTIFICATION IN A COMPLEX WITH STX4, PHOSPHORYLATION.
  12. "Dopamine-dependent neurodegeneration in rats induced by viral vector-mediated overexpression of the parkin target protein, CDCrel-1."
    Dong Z., Ferger B., Paterna J.-C., Vogel D., Furler S., Osinde M., Feldon J., Bueeler H.
    Proc. Natl. Acad. Sci. U.S.A. 100:12438-12443(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: POSSIBLE INVOLVEMENT IN PARK2.
  13. "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.
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  15. "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-225 AND SER-327, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSEPT5_HUMAN
AccessioniPrimary (citable) accession number: Q99719
Secondary accession number(s): O15251, Q96MY5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1997
Last modified: October 29, 2014
This is version 133 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

In a heterologous system, SEPT5 overexpression has been shown to exert dopamine-dependent neurotoxicity. As wild-type PARK2, but not familial-linked PARK2 mutants, ubiquitinates mouse SEPT5 and promotes its degradation, it has been sugested that a deficiency in SEPT5 degradation may contribute to the development of early onset Parkinson disease 2 (PARK2).

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3