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Q9UHD8 (SEPT9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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-9
Alternative name(s):
MLL septin-like fusion protein MSF-A
Short name=MLL septin-like fusion protein
Ovarian/Breast septin
Short name=Ov/Br septin
Septin D1
Gene names
Name:SEPT9
Synonyms:KIAA0991, MSF
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length586 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Filament-forming cytoskeletal GTPase By similarity. May play a role in cytokinesis Potential. May play a role in the internalization of 2 intracellular microbial pathogens, Listeria monocytogenes and Shigella flexneri.

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. Interacts with SEPT2, SEPT6, SEPT7, SEPT11 and SEPT14. Interacts with RTKN and ARHGEF18. In a mesenchymal cell line, Rho/RTKN signals cause disruption of wild-type septin filaments, but not of those containing isoform 2 variants HNA Trp-106 and Phe-111. In a mesenchymal cell line, isoform 2 variants HNA Trp-106 and Phe-111, but not wild type, form filaments with SEPT4. Ref.12 Ref.14 Ref.15 Ref.18 Ref.19 Ref.23

Subcellular location

Cytoplasmcytoskeleton. Note: In an epithelial cell line, concentrates at cell-cell contact areas. After TGF-beta1 treatment and induction of epithelial to mesenchymal transition, colocalizes partly with actin stress fibers. During bacterial infection, displays a collar shape structure next to actin at the pole of invading bacteria. Ref.18 Ref.19

Tissue specificity

Widely expressed. Isoforms are differentially expressed in testes, kidney, liver heart, spleen, brain, peripheral blood leukocytes, skeletal muscle and kidney. Specific isoforms appear to demonstrate tissue specificity. Isoform 5 is the most highly expressed in fetal tissue. Isoform 1 is detected in all tissues except the brain and thymus, while isoform 2, isoform 3, and isoform 4 are detected at low levels in approximately half of the fetal tissues. Ref.1 Ref.3 Ref.11 Ref.13

Involvement in disease

A chromosomal aberration involving SEPT9/MSF is found in therapy-related acute myeloid leukemia (t-AML). Translocation t(11;17)(q23;q25) with KMT2A/MLL1. Ref.1

Hereditary neuralgic amyotrophy (HNA) [MIM:162100]: Autosomal dominant form of recurrent focal neuropathy characterized clinically by acute, recurrent episodes of brachial plexus neuropathy with muscle weakness and atrophy preceded by severe pain in the affected arm. HNA is triggered by environmental factors such as infection or parturition.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.18 Ref.29 Ref.30 Ref.31

Sequence similarities

Belongs to the septin family.

Sequence caution

The sequence BAB14057.1 differs from that shown. Reason: Aberrant splicing.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

HIF1AQ166654EBI-851558,EBI-447269
SEPT14Q6ZU153EBI-851569,EBI-2009297

Alternative products

This entry describes 8 isoforms produced by alternative splicing. [Align] [Select]

Note: There are potentially 18 isoforms.
Isoform 1 (identifier: Q9UHD8-1)

Also known as: Epsilon; MSF-A;

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: Q9UHD8-2)

Also known as: Alpha;

The sequence of this isoform differs from the canonical sequence as follows:
     1-25: MKKSYSGGTRTSSGRLRRLGDSSGP → MERDRIS
Isoform 3 (identifier: Q9UHD8-3)

Also known as: Beta; MSF-B;

The sequence of this isoform differs from the canonical sequence as follows:
     1-164: Missing.
Isoform 4 (identifier: Q9UHD8-4)

Also known as: Delta;

The sequence of this isoform differs from the canonical sequence as follows:
     1-251: Missing.
Isoform 5 (identifier: Q9UHD8-5)

Also known as: Gamma;

The sequence of this isoform differs from the canonical sequence as follows:
     1-25: MKKSYSGGTRTSSGRLRRLGDSSGP → MSDPAVNAQLDGIISDFE
Isoform 7 (identifier: Q9UHD8-7)

The sequence of this isoform differs from the canonical sequence as follows:
     7-25: Missing.
Note: No experimental confirmation available.
Isoform 8 (identifier: Q9UHD8-8)

The sequence of this isoform differs from the canonical sequence as follows:
     1-112: Missing.
     113-240: DISSKQVENA...VAEATPRSQE → MGSSFWEGLQ...CLATIGSDRQ
Note: No experimental confirmation available.
Isoform 9 (identifier: Q9UHD8-9)

The sequence of this isoform differs from the canonical sequence as follows:
     1-224: Missing.
     225-240: PKPQPPVAEATPRSQE → MAGAGCTGTWSWLWGT
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 586586Septin-9
PRO_0000173535

Regions

Nucleotide binding305 – 3128GTP By similarity
Nucleotide binding445 – 4539GTP By similarity

Sites

Binding site3391GTP By similarity
Binding site3651GTP; via amide nitrogen By similarity
Binding site5011GTP; via amide nitrogen and carbonyl oxygen By similarity
Binding site5161GTP By similarity

Amino acid modifications

Modified residue11N-acetylmethionine Ref.28
Modified residue301Phosphoserine Ref.17 Ref.20 Ref.21 Ref.24 Ref.25 Ref.27
Modified residue381Phosphothreonine Ref.21
Modified residue421Phosphothreonine Ref.17 Ref.21
Modified residue621N6-acetyllysine By similarity
Modified residue821Phosphoserine Ref.25
Modified residue851Phosphoserine Ref.16 Ref.25 Ref.27
Modified residue961Phosphoserine Ref.25
Modified residue1421Phosphothreonine Ref.25
Modified residue2781Phosphotyrosine Ref.24
Modified residue3271Phosphoserine Ref.27

Natural variations

Alternative sequence1 – 251251Missing in isoform 4.
VSP_012335
Alternative sequence1 – 224224Missing in isoform 9.
VSP_038315
Alternative sequence1 – 164164Missing in isoform 3.
VSP_012336
Alternative sequence1 – 112112Missing in isoform 8.
VSP_038316
Alternative sequence1 – 2525MKKSY…DSSGP → MERDRIS in isoform 2.
VSP_012337
Alternative sequence1 – 2525MKKSY…DSSGP → MSDPAVNAQLDGIISDFE in isoform 5.
VSP_012338
Alternative sequence7 – 2519Missing in isoform 7.
VSP_038317
Alternative sequence113 – 240128DISSK…PRSQE → MGSSFWEGLQVAVGLPQGCW PQGLDSGEPAEGGQLEAAPV CIVTRQSKETAGPTLGRGGW RQGSLRRGKGTSCRCRQLSP GHGPGRLTGCGECHRLPCRG LVSGFTGLRGQEEDDLAFCL ATIGSDRQ in isoform 8.
VSP_038318
Alternative sequence225 – 24016PKPQP…PRSQE → MAGAGCTGTWSWLWGT in isoform 9.
VSP_038319
Natural variant761R → C. Ref.2
VAR_020667
Natural variant1061R → W in HNA. Ref.18 Ref.29 Ref.30 Ref.31
VAR_033101
Natural variant1111S → F in HNA. Ref.18 Ref.29 Ref.31
VAR_033102
Natural variant1451P → L. Ref.2 Ref.5 Ref.31
Corresponds to variant rs34587622 [ dbSNP | Ensembl ].
VAR_020668
Natural variant5761M → V. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10
Corresponds to variant rs2627223 [ dbSNP | Ensembl ].
VAR_020669

Experimental info

Sequence conflict2511D → G in BAG64494. Ref.5
Sequence conflict4871V → E in BAB14057. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Epsilon) (MSF-A) [UniParc].

Last modified April 18, 2006. Version 2.
Checksum: D4404578328CFCFE

FASTA58665,401
        10         20         30         40         50         60 
MKKSYSGGTR TSSGRLRRLG DSSGPALKRS FEVEEVETPN STPPRRVQTP LLRATVASST 

        70         80         90        100        110        120 
QKFQDLGVKN SEPSARHVDS LSQRSPKASL RRVELSGPKA AEPVSRRTEL SIDISSKQVE 

       130        140        150        160        170        180 
NAGAIGPSRF GLKRAEVLGH KTPEPAPRRT EITIVKPQES AHRRMEPPAS KVPEVPTAPA 

       190        200        210        220        230        240 
TDAAPKRVEI QMPKPAEAPT APSPAQTLEN SEPAPVSQLQ SRLEPKPQPP VAEATPRSQE 

       250        260        270        280        290        300 
ATEAAPSCVG DMADTPRDAG LKQAPASRNE KAPVDFGYVG IDSILEQMRR KAMKQGFEFN 

       310        320        330        340        350        360 
IMVVGQSGLG KSTLINTLFK SKISRKSVQP TSEERIPKTI EIKSITHDIE EKGVRMKLTV 

       370        380        390        400        410        420 
IDTPGFGDHI NNENCWQPIM KFINDQYEKY LQEEVNINRK KRIPDTRVHC CLYFIPATGH 

       430        440        450        460        470        480 
SLRPLDIEFM KRLSKVVNIV PVIAKADTLT LEERVHFKQR ITADLLSNGI DVYPQKEFDE 

       490        500        510        520        530        540 
DSEDRLVNEK FREMIPFAVV GSDHEYQVNG KRILGRKTKW GTIEVENTTH CEFAYLRDLL 

       550        560        570        580 
IRTHMQNIKD ITSSIHFEAY RVKRLNEGSS AMANGMEEKE PEAPEM 

« Hide

Isoform 2 (Alpha) [UniParc].

Checksum: 47A03DD79B5D6147
Show »

FASTA56863,666
Isoform 3 (Beta) (MSF-B) [UniParc].

Checksum: F581FB2EA1A6E063
Show »

FASTA42247,501
Isoform 4 (Delta) [UniParc].

Checksum: 82375B44AEFFC64C
Show »

FASTA33538,518
Isoform 5 (Gamma) [UniParc].

Checksum: F176A071496AC44C
Show »

FASTA57964,682
Isoform 7 [UniParc].

Checksum: 73741167A05AA0E1
Show »

FASTA56763,502
Isoform 8 [UniParc].

Checksum: 5B5DCF81F2D1A597
Show »

FASTA47452,913
Isoform 9 [UniParc].

Checksum: 5530A4184F432A5C
Show »

FASTA36241,187

References

« Hide 'large scale' references
[1]"MSF (MLL septin-like fusion), a fusion partner gene of MLL, in a therapy-related acute myeloid leukemia with a t(11;17)(q23;q25)."
Osaka M., Rowley J.D., Zeleznik-Le N.J.
Proc. Natl. Acad. Sci. U.S.A. 96:6428-6433(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT VAL-576, TISSUE SPECIFICITY, DISEASE, CHROMOSOMAL TRANSLOCATION.
[2]"Isolation and mapping of a human septin gene to a region on chromosome 17q, commonly deleted in sporadic epithelial ovarian tumors."
Russell S.E.H., McIlhatton M.A., Burrows J.F., Donaghy P.G., Chanduloy S., Petty E.M., Kalikin L.M., Church S.W., McIlroy S., Harkin D.P., Keilty G.W., Cranston A.N., Weissenbach J., Hickey I., Johnston P.G.
Cancer Res. 60:4729-4734(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4 AND 5), VARIANTS CYS-76; LEU-145 AND VAL-576.
[3]"Genomic and expression analyses of alternatively spliced transcripts of the MLL septin-like fusion gene (MSF) that map to a 17q25 region of loss in breast and ovarian tumors."
Kalikin L.M., Sims H.L., Petty E.M.
Genomics 63:165-172(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), VARIANT VAL-576, TISSUE SPECIFICITY, ALTERNATIVE SPLICING.
[4]"Novel human cell division control protein septin D1."
Zhang W., He L., Wan T., Yuan Z., Zhu X., Cao X.
Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT VAL-576.
[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. 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] (ISOFORMS 3; 4; 5; 7; 8 AND 9), VARIANTS LEU-145 AND VAL-576.
Tissue: Fetal brain, Mammary gland, Placenta, Teratocarcinoma, Thymus, Tongue and Trachea.
[6]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT VAL-576.
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT VAL-576.
[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] (ISOFORMS 2 AND 3), VARIANT VAL-576.
Tissue: Eye and Skin.
[9]"Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 6:63-70(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 26-586, VARIANT VAL-576.
Tissue: Brain.
[10]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 353-586, VARIANT VAL-576.
Tissue: Testis.
[11]"Genomic organization, complex splicing pattern and expression of a human septin gene on chromosome 17q25.3."
McIlhatton M.A., Burrows J.F., Donaghy P.G., Chanduloy S., Johnston P.G., Russell S.E.
Oncogene 20:5930-5939(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, ALTERNATIVE SPLICING.
[12]"Biochemical and cell biological analyses of a mammalian septin complex, Sept7/9b/11."
Nagata K., Asano T., Nozawa Y., Inagaki M.
J. Biol. Chem. 279:55895-55904(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SEPT7 AND SEPT11.
[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]"Cytoskeletal modification of Rho guanine nucleotide exchange factor activity: identification of a Rho guanine nucleotide exchange factor as a binding partner for Sept9b, a mammalian septin."
Nagata K., Inagaki M.
Oncogene 24:65-76(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ARHGEF18.
[15]"Possible role of Rho/Rhotekin signaling in mammalian septin organization."
Ito H., Iwamoto I., Morishita R., Nozawa Y., Narumiya S., Asano T., Nagata K.
Oncogene 24:7064-7072(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RTKN.
[16]"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-85, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30 AND THR-42, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"SEPT9 sequence alternations causing hereditary neuralgic amyotrophy are associated with altered interactions with SEPT4/SEPT11 and resistance to Rho/Rhotekin-signaling."
Sudo K., Ito H., Iwamoto I., Morishita R., Asano T., Nagata K.
Hum. Mutat. 28:1005-1013(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH SEPT4, VARIANTS HNA TRP-106 AND PHE-111.
[19]"Characterization of a SEPT9 interacting protein, SEPT14, a novel testis-specific septin."
Peterson E.A., Kalikin L.M., Steels J.D., Estey M.P., Trimble W.S., Petty E.M.
Mamm. Genome 18:796-807(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SEPT14, SUBCELLULAR LOCATION.
[20]"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-30, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[21]"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-30; THR-38 AND THR-42, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[22]"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].
[23]"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 SEPT2; SEPT6; SEPT7 AND SEPT11, ASSOCIATION WITH ACTIN FILAMENTS AND MICROTUBULES.
[24]"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-30 AND TYR-278, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[25]"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-30; SER-82; SER-85; SER-96 AND THR-142, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[26]"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].
[27]"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-30; SER-85 AND SER-327, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[28]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[29]"Mutations in SEPT9 cause hereditary neuralgic amyotrophy."
Kuhlenbaeumer G., Hannibal M.C., Nelis E., Schirmacher A., Verpoorten N., Meuleman J., Watts G.D.J., De Vriendt E., Young P., Stoegbauer F., Halfter H., Irobi J., Goossens D., Del-Favero J., Betz B.G., Hor H., Kurlemann G., Bird T.D. expand/collapse author list , Airaksinen E., Mononen T., Serradell A.P., Prats J.M., Van Broeckhoven C., De Jonghe P., Timmerman V., Ringelstein E.B., Chance P.F.
Nat. Genet. 37:1044-1046(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HNA TRP-106 AND PHE-111.
[30]"Dysmorphic syndrome of hereditary neuralgic amyotrophy associated with a SEPT9 gene mutation -- a family study."
Laccone F., Hannibal M.C., Neesen J., Grisold W., Chance P.F., Rehder H.
Clin. Genet. 74:279-283(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HNA TRP-106.
[31]"SEPT9 gene sequencing analysis reveals recurrent mutations in hereditary neuralgic amyotrophy."
Hannibal M.C., Ruzzo E.K., Miller L.R., Betz B., Buchan J.G., Knutzen D.M., Barnett K., Landsverk M.L., Brice A., LeGuern E., Bedford H.M., Worrall B.B., Lovitt S., Appel S.H., Andermann E., Bird T.D., Chance P.F.
Neurology 72:1755-1759(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HNA TRP-106 AND PHE-111, VARIANT LEU-145.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF123052 mRNA. Translation: AAD39749.1.
AJ312319 mRNA. Translation: CAC42221.1.
AJ312320 mRNA. Translation: CAC42222.1.
AJ312321 mRNA. Translation: CAC42223.1.
AJ312322 mRNA. Translation: CAC42224.1.
AF189712 mRNA. Translation: AAF23373.1.
AF189713 mRNA. Translation: AAF23374.1.
AF142408 mRNA. Translation: AAG27919.1.
AK022493 mRNA. Translation: BAB14057.1. Sequence problems.
AK290368 mRNA. Translation: BAF83057.1.
AK056495 mRNA. Translation: BAG51732.1.
AK300270 mRNA. Translation: BAG62031.1.
AK303449 mRNA. Translation: BAG64494.1.
AK304143 mRNA. Translation: BAG65036.1.
AK299828 mRNA. Translation: BAH13140.1.
AK316473 mRNA. Translation: BAH14844.1.
BT007215 mRNA. Translation: AAP35879.1.
CH471099 Genomic DNA. Translation: EAW89462.1.
CH471099 Genomic DNA. Translation: EAW89463.1.
CH471099 Genomic DNA. Translation: EAW89468.1.
BC021192 mRNA. Translation: AAH21192.1.
BC054004 mRNA. Translation: AAH54004.1.
AB023208 mRNA. Translation: BAA76835.2.
AL080131 mRNA. Translation: CAB45728.1.
PIRT12519.
RefSeqNP_001106963.1. NM_001113491.1.
NP_001106964.1. NM_001113492.1.
NP_001106965.1. NM_001113493.1.
NP_001106966.1. NM_001113494.1.
NP_001106967.1. NM_001113495.1.
NP_001106968.1. NM_001113496.1.
NP_006631.2. NM_006640.4.
XP_005257016.1. XM_005256959.1.
XP_005257017.1. XM_005256960.1.
XP_005257018.1. XM_005256961.1.
XP_005257019.1. XM_005256962.1.
UniGeneHs.440932.

3D structure databases

ProteinModelPortalQ9UHD8.
SMRQ9UHD8. Positions 297-565.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116015. 42 interactions.
IntActQ9UHD8. 8 interactions.
MINTMINT-5006676.

PTM databases

PhosphoSiteQ9UHD8.

Polymorphism databases

DMDM93141311.

Proteomic databases

PaxDbQ9UHD8.
PRIDEQ9UHD8.

Protocols and materials databases

DNASU10801.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000329047; ENSP00000329161; ENSG00000184640. [Q9UHD8-2]
ENST00000423034; ENSP00000405877; ENSG00000184640. [Q9UHD8-5]
ENST00000427177; ENSP00000391249; ENSG00000184640. [Q9UHD8-1]
ENST00000427180; ENSP00000415624; ENSG00000184640. [Q9UHD8-8]
ENST00000427674; ENSP00000403194; ENSG00000184640. [Q9UHD8-3]
ENST00000431235; ENSP00000406987; ENSG00000184640. [Q9UHD8-3]
ENST00000449803; ENSP00000400181; ENSG00000184640. [Q9UHD8-3]
ENST00000541152; ENSP00000438089; ENSG00000184640. [Q9UHD8-4]
ENST00000571241; ENSP00000460993; ENSG00000261843. [Q9UHD8-3]
ENST00000573468; ENSP00000458910; ENSG00000261843. [Q9UHD8-5]
ENST00000574362; ENSP00000459494; ENSG00000261843. [Q9UHD8-3]
ENST00000574853; ENSP00000461593; ENSG00000261843. [Q9UHD8-8]
ENST00000574891; ENSP00000461549; ENSG00000261843. [Q9UHD8-1]
ENST00000575088; ENSP00000458668; ENSG00000261843. [Q9UHD8-4]
ENST00000576289; ENSP00000460125; ENSG00000261843. [Q9UHD8-3]
ENST00000576977; ENSP00000460394; ENSG00000261843. [Q9UHD8-2]
ENST00000585924; ENSP00000467973; ENSG00000261843. [Q9UHD8-4]
ENST00000585930; ENSP00000468120; ENSG00000184640. [Q9UHD8-9]
ENST00000586105; ENSP00000465012; ENSG00000261843. [Q9UHD8-3]
ENST00000587968; ENSP00000465173; ENSG00000261843. [Q9UHD8-2]
ENST00000588583; ENSP00000467378; ENSG00000261843. [Q9UHD8-7]
ENST00000588690; ENSP00000468668; ENSG00000184640. [Q9UHD8-3]
ENST00000590294; ENSP00000465464; ENSG00000184640. [Q9UHD8-2]
ENST00000591088; ENSP00000466247; ENSG00000184640. [Q9UHD8-4]
ENST00000591198; ENSP00000468406; ENSG00000184640. [Q9UHD8-7]
ENST00000591262; ENSP00000467327; ENSG00000261843. [Q9UHD8-9]
ENST00000591339; ENSP00000467408; ENSG00000261843. [Q9UHD8-4]
ENST00000592951; ENSP00000466648; ENSG00000184640. [Q9UHD8-4]
GeneID10801.
KEGGhsa:10801.
UCSCuc002jts.4. human. [Q9UHD8-1]
uc002jtu.4. human. [Q9UHD8-2]
uc002jtv.3. human. [Q9UHD8-5]
uc010dhd.3. human. [Q9UHD8-8]
uc010wtk.2. human. [Q9UHD8-7]
uc010wtl.2. human. [Q9UHD8-9]

Organism-specific databases

CTD10801.
GeneCardsGC17P075277.
HGNCHGNC:7323. SEPT9.
HPAHPA042564.
HPA050627.
MIM162100. phenotype.
604061. gene.
neXtProtNX_Q9UHD8.
Orphanet2901. Neuralgic amyotrophy.
PharmGKBPA31132.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5019.
HOVERGENHBG098529.
InParanoidQ9UHD8.
KOK16938.
OMAEALSHEM.
PhylomeDBQ9UHD8.
TreeFamTF101078.

Gene expression databases

ArrayExpressQ9UHD8.
BgeeQ9UHD8.
CleanExHS_SEPT9.
GenevestigatorQ9UHD8.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR000038. Cell_div_GTP-bd.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERPTHR18884. PTHR18884. 1 hit.
PfamPF00735. Septin. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
ProtoNetSearch...

Other

ChiTaRSSEPT9. human.
GeneWikiSEPT9.
GenomeRNAi10801.
NextBio41021.
PROQ9UHD8.
SOURCESearch...

Entry information

Entry nameSEPT9_HUMAN
AccessionPrimary (citable) accession number: Q9UHD8
Secondary accession number(s): A8K2V3 expand/collapse secondary AC list , B3KPM0, B4DTL9, B4E0N2, B4E274, B7Z654, Q96QF3, Q96QF4, Q96QF5, Q9HA04, Q9UG40, Q9Y5W4
Entry history
Integrated into UniProtKB/Swiss-Prot: December 21, 2004
Last sequence update: April 18, 2006
Last modified: April 16, 2014
This is version 128 of the entry and version 2 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

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM