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Q8IYM1

- SEP12_HUMAN

UniProt

Q8IYM1 - SEP12_HUMAN

Protein

Septin-12

Gene

SEPT12

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      Previous versions | rss
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    Functioni

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei89 – 891GTPBy similarity
    Binding sitei115 – 1151GTP; via amide nitrogenBy similarity
    Binding sitei251 – 2511GTP; via amide nitrogen and carbonyl oxygenBy similarity
    Binding sitei266 – 2661GTPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi56 – 638GTPBy similarity
    Nucleotide bindingi195 – 2039GTPBy similarity

    GO - Molecular functioni

    1. GDP binding Source: UniProtKB
    2. GTP binding Source: UniProtKB
    3. phosphatidylinositol binding Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. protein homodimerization activity Source: UniProtKB

    GO - Biological processi

    1. cell cycle Source: UniProtKB-KW
    2. cell division Source: UniProtKB-KW

    Keywords - Biological processi

    Cell cycle, Cell division

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Septin-12
    Gene namesi
    Name:SEPT12
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:26348. SEPT12.

    Subcellular locationi

    Cytoplasm. Cytoplasmcytoskeleton. Cytoplasmcytoskeletonspindle. Cell projectionciliumflagellum
    Note: At interphase, forms a filamentous structure in the cytoplasm. During anaphase, translocates to the central spindle region and to the midbody during cytokinesis. Found in the sperm annulus.

    GO - Cellular componenti

    1. cleavage furrow Source: UniProtKB
    2. microtubule cytoskeleton Source: HPA
    3. midbody Source: UniProtKB
    4. perinuclear region of cytoplasm Source: UniProtKB
    5. septin complex Source: UniProtKB
    6. sperm annulus Source: UniProtKB
    7. spindle Source: UniProtKB
    8. stress fiber Source: UniProtKB

    Keywords - Cellular componenti

    Cell projection, Cilium, Cytoplasm, Cytoskeleton, Flagellum

    Pathology & Biotechi

    Involvement in diseasei

    Spermatogenic failure 10 (SPGF10) [MIM:614822]: An infertility disorder caused by spermatogenesis defects. It results in decreased sperm motility, concentration, and multiple sperm structural defects. The most prominent feature is a defective sperm annulus, a ring structure that demarcates the midpiece and the principal piece of the sperm tail.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti89 – 891T → M in SPGF10; results in significantly reduced GTP hydrolysis. 1 Publication
    Corresponds to variant rs199696526 [ dbSNP | Ensembl ].
    VAR_068097
    Natural varianti197 – 1971D → N in SPGF10; results in significantly reduced GTP hydrolysis due to impaired GTP binding. 1 Publication
    VAR_068098

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi56 – 561G → N: Abolishes binding to GTP and to SEPT11, and also abolishes the ability of SEPT12 to form filamentous structures. 1 Publication

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi614822. phenotype.
    PharmGKBiPA162402916.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 358358Septin-12PRO_0000312860Add
    BLAST

    Proteomic databases

    PaxDbiQ8IYM1.
    PRIDEiQ8IYM1.

    PTM databases

    PhosphoSiteiQ8IYM1.

    Expressioni

    Tissue specificityi

    Widely expressed.1 Publication

    Gene expression databases

    ArrayExpressiQ8IYM1.
    BgeeiQ8IYM1.
    CleanExiHS_SEPT12.
    GenevestigatoriQ8IYM1.

    Organism-specific databases

    HPAiHPA041128.

    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 SEPT6 and SEPT11. Forms homodimers.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    SEPT6Q141413EBI-2585067,EBI-745901

    Protein-protein interaction databases

    BioGridi125863. 1 interaction.
    IntActiQ8IYM1. 1 interaction.
    STRINGi9606.ENSP00000268231.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8IYM1.
    SMRiQ8IYM1. Positions 48-315.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini46 – 317272Septin-type GAdd
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG5019.
    HOGENOMiHOG000233586.
    HOVERGENiHBG065093.
    InParanoidiQ8IYM1.
    KOiK16938.
    OMAiIRLNESH.
    PhylomeDBiQ8IYM1.
    TreeFamiTF101078.

    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: Q8IYM1-1) [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

    MDPLRRSPSP CLSSQPSSPS TPPCEMLGPV GIEAVLDQLK IKAMKMGFEF    50
    NIMVVGQSGL GKSTMVNTLF KSKVWKSNPP GLGVPTPQTL QLHSLTHVIE 100
    EKGVKLKLTV TDTPGFGDQI NNDNCWDPIL GYINEQYEQY LQEEILITRQ 150
    RHIPDTRVHC CVYFVPPTGH CLRPLDIEFL QRLCRTVNVV PVIARADSLT 200
    MEEREAFRRR IQQNLRTHCI DVYPQMCFDE DINDKILNSK LRDRIPFAVV 250
    GADQEHLVNG RCVLGRKTKW GIIEVENMAH CEFPLLRDLL IRSHLQDLKD 300
    ITHNIHYENY RVIRLNESHL LPRGPGWVNL APASPGQLTT PRTFKVCRGA 350
    HDDSDDEF 358
    Length:358
    Mass (Da):40,748
    Last modified:March 1, 2003 - v1
    Checksum:i31968F366DEFB4FD
    GO
    Isoform 2 (identifier: Q8IYM1-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         125-170: Missing.

    Show »
    Length:312
    Mass (Da):35,191
    Checksum:iA9C83873ABB4CBE4
    GO

    Sequence cautioni

    The sequence AAH24017.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti22 – 221P → T in AAH24017. (PubMed:15489334)Curated
    Sequence conflicti258 – 2581V → M in BAB71681. (PubMed:14702039)Curated
    Sequence conflicti280 – 2801H → L in AAH24017. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti89 – 891T → M in SPGF10; results in significantly reduced GTP hydrolysis. 1 Publication
    Corresponds to variant rs199696526 [ dbSNP | Ensembl ].
    VAR_068097
    Natural varianti197 – 1971D → N in SPGF10; results in significantly reduced GTP hydrolysis due to impaired GTP binding. 1 Publication
    VAR_068098
    Natural varianti213 – 2131Q → R.
    Corresponds to variant rs6500633 [ dbSNP | Ensembl ].
    VAR_057176

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei125 – 17046Missing in isoform 2. 2 PublicationsVSP_029918Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ456996 mRNA. Translation: ABE68946.1.
    DQ517531 mRNA. Translation: ABF61438.1.
    EF620906 mRNA. Translation: ABR10901.1.
    AK058139 mRNA. Translation: BAB71681.1.
    CH471112 Genomic DNA. Translation: EAW85265.1.
    BC024017 mRNA. Translation: AAH24017.1. Different initiation.
    BC035619 mRNA. Translation: AAH35619.1.
    CCDSiCCDS10522.1. [Q8IYM1-1]
    CCDS53987.1. [Q8IYM1-2]
    RefSeqiNP_001147930.1. NM_001154458.2. [Q8IYM1-2]
    NP_653206.2. NM_144605.4. [Q8IYM1-1]
    XP_006720909.1. XM_006720846.1. [Q8IYM1-1]
    UniGeneiHs.126780.

    Genome annotation databases

    EnsembliENST00000268231; ENSP00000268231; ENSG00000140623. [Q8IYM1-1]
    ENST00000396693; ENSP00000379922; ENSG00000140623. [Q8IYM1-2]
    GeneIDi124404.
    KEGGihsa:124404.
    UCSCiuc002cxq.3. human. [Q8IYM1-1]
    uc002cxr.3. human. [Q8IYM1-2]

    Polymorphism databases

    DMDMi74750767.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ456996 mRNA. Translation: ABE68946.1 .
    DQ517531 mRNA. Translation: ABF61438.1 .
    EF620906 mRNA. Translation: ABR10901.1 .
    AK058139 mRNA. Translation: BAB71681.1 .
    CH471112 Genomic DNA. Translation: EAW85265.1 .
    BC024017 mRNA. Translation: AAH24017.1 . Different initiation.
    BC035619 mRNA. Translation: AAH35619.1 .
    CCDSi CCDS10522.1. [Q8IYM1-1 ]
    CCDS53987.1. [Q8IYM1-2 ]
    RefSeqi NP_001147930.1. NM_001154458.2. [Q8IYM1-2 ]
    NP_653206.2. NM_144605.4. [Q8IYM1-1 ]
    XP_006720909.1. XM_006720846.1. [Q8IYM1-1 ]
    UniGenei Hs.126780.

    3D structure databases

    ProteinModelPortali Q8IYM1.
    SMRi Q8IYM1. Positions 48-315.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 125863. 1 interaction.
    IntActi Q8IYM1. 1 interaction.
    STRINGi 9606.ENSP00000268231.

    PTM databases

    PhosphoSitei Q8IYM1.

    Polymorphism databases

    DMDMi 74750767.

    Proteomic databases

    PaxDbi Q8IYM1.
    PRIDEi Q8IYM1.

    Protocols and materials databases

    DNASUi 124404.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000268231 ; ENSP00000268231 ; ENSG00000140623 . [Q8IYM1-1 ]
    ENST00000396693 ; ENSP00000379922 ; ENSG00000140623 . [Q8IYM1-2 ]
    GeneIDi 124404.
    KEGGi hsa:124404.
    UCSCi uc002cxq.3. human. [Q8IYM1-1 ]
    uc002cxr.3. human. [Q8IYM1-2 ]

    Organism-specific databases

    CTDi 124404.
    GeneCardsi GC16M004829.
    HGNCi HGNC:26348. SEPT12.
    HPAi HPA041128.
    MIMi 611562. gene.
    614822. phenotype.
    neXtProti NX_Q8IYM1.
    PharmGKBi PA162402916.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5019.
    HOGENOMi HOG000233586.
    HOVERGENi HBG065093.
    InParanoidi Q8IYM1.
    KOi K16938.
    OMAi IRLNESH.
    PhylomeDBi Q8IYM1.
    TreeFami TF101078.

    Miscellaneous databases

    GenomeRNAii 124404.
    NextBioi 81269.
    PROi Q8IYM1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8IYM1.
    Bgeei Q8IYM1.
    CleanExi HS_SEPT12.
    Genevestigatori Q8IYM1.

    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

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING (ISOFORM 1).
    2. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH SEPT6 AND SEPT11, SUBCELLULAR LOCATION.
      Tissue: Testis.
    3. "Molecular cloning of septin 12 transcript variant 2 from human testis."
      Wang J.R., Xing X.W., Jiang X.Z., Tang Y.X., Yang J.F., Dai Y.B., Tan J.
      Submitted (MAY-2007) 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 1).
      Tissue: Testis.
    5. 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: Brain and Testis.
    7. "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.
    8. "GTP binding is required for SEPT12 to form filaments and to interact with SEPT11."
      Ding X., Yu W., Liu M., Shen S., Chen F., Cao L., Wan B., Yu L.
      Mol. Cells 25:385-389(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: HOMODIMERIZATION, INTERACTION WITH SEPT11, GTP-BINDING, MUTAGENESIS OF GLY-56.
    9. "SEPT12 mutations cause male infertility with defective sperm annulus."
      Kuo Y.C., Lin Y.H., Chen H.I., Wang Y.Y., Chiou Y.W., Lin H.H., Pan H.A., Wu C.M., Su S.M., Hsu C.C., Kuo P.L.
      Hum. Mutat. 33:710-719(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, VARIANTS SPGF10 MET-89 AND ASN-197, CHARACTERIZATION OF VARIANTS SPGF10 MET-89 AND ASN-197.

    Entry informationi

    Entry nameiSEP12_HUMAN
    AccessioniPrimary (citable) accession number: Q8IYM1
    Secondary accession number(s): Q0P6B0, Q1PBH0, Q96LL0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 4, 2007
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 98 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

    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