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Septin-12

 SEP12_HUMAN             Reviewed;         358 AA.
Q8IYM1; Q0P6B0; Q1PBH0; Q96LL0;
04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
02-JUN-2021, entry version 147.
RecName: Full=Septin-12;
Name=SEPTIN12 {ECO:0000312|HGNC:HGNC:26348}; Synonyms=SEPT12;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND ALTERNATIVE SPLICING (ISOFORM
1).
PubMed=17685441; DOI=10.1002/cm.20224;
Steels J.D., Estey M.P., Froese C.D., Reynaud D., Pace-Asciak C.,
Trimble W.S.;
"Sept12 is a component of the mammalian sperm tail annulus.";
Cell Motil. Cytoskeleton 64:794-807(2007).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH SEPTIN6 AND
SEPTIN11, AND SUBCELLULAR LOCATION.
TISSUE=Testis;
PubMed=18047794; DOI=10.5483/bmbrep.2007.40.6.973;
Ding X., Yu W., Liu M., Shen S., Chen F., Wan B., Yu L.;
"SEPT12 interacts with SEPT6 and this interaction alters the filament
structure of SEPT6 in Hela cells.";
J. Biochem. Mol. Biol. 40:973-978(2007).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Wang J.R., Xing X.W., Jiang X.Z., Tang Y.X., Yang J.F., Dai Y.B., Tan J.;
"Molecular cloning of septin 12 transcript variant 2 from human testis.";
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Testis;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
TISSUE SPECIFICITY.
PubMed=15915442; DOI=10.1002/path.1789;
Hall P.A., Jung K., Hillan K.J., Russell S.E.H.;
"Expression profiling the human septin gene family.";
J. Pathol. 206:269-278(2005).
[8]
TISSUE SPECIFICITY.
PubMed=17967425; DOI=10.1016/j.febslet.2007.10.032;
Cao L., Ding X., Yu W., Yang X., Shen S., Yu L.;
"Phylogenetic and evolutionary analysis of the septin protein family in
metazoan.";
FEBS Lett. 581:5526-5532(2007).
[9]
HOMODIMERIZATION, INTERACTION WITH SEPTIN11, GTP-BINDING, AND MUTAGENESIS
OF GLY-56.
PubMed=18443421;
Ding X., Yu W., Liu M., Shen S., Chen F., Cao L., Wan B., Yu L.;
"GTP binding is required for SEPT12 to form filaments and to interact with
SEPT11.";
Mol. Cells 25:385-389(2008).
[10]
SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
PubMed=20801438; DOI=10.1016/j.fertnstert.2010.07.1064;
Lin Y.H., Chou C.K., Hung Y.C., Yu I.S., Pan H.A., Lin S.W., Kuo P.L.;
"SEPT12 deficiency causes sperm nucleus damage and developmental arrest of
preimplantation embryos.";
Fertil. Steril. 95:363-365(2011).
[11]
SUBCELLULAR LOCATION, VARIANTS SPGF10 MET-89 AND ASN-197, AND
CHARACTERIZATION OF VARIANTS SPGF10 MET-89 AND ASN-197.
PubMed=22275165; DOI=10.1002/humu.22028;
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.;
"SEPT12 mutations cause male infertility with defective sperm annulus.";
Hum. Mutat. 33:710-719(2012).
[12]
FUNCTION, AND SUBUNIT.
PubMed=24213608; DOI=10.3390/ijms141122102;
Kuo P.L., Chiang H.S., Wang Y.Y., Kuo Y.C., Chen M.F., Yu I.S., Teng Y.N.,
Lin S.W., Lin Y.H.;
"SEPT12-microtubule complexes are required for sperm head and tail
formation.";
Int. J. Mol. Sci. 14:22102-22116(2013).
[13]
FUNCTION, SUBUNIT, AND CHARACTERIZATION OF VARIANTS SPGF10 MET-89 AND
ASN-197.
PubMed=25588830; DOI=10.1242/jcs.158998;
Kuo Y.C., Shen Y.R., Chen H.I., Lin Y.H., Wang Y.Y., Chen Y.R., Wang C.Y.,
Kuo P.L.;
"SEPT12 orchestrates the formation of mammalian sperm annulus by organizing
core octomeric complexes with other SEPT proteins.";
J. Cell Sci. 128:923-934(2015).
[14]
INTERACTION WITH SPAG4 AND LMNB1, SUBCELLULAR LOCATION, AND
CHARACTERIZATION OF VARIANTS SPGF10 MET-89 AND ASN-197.
PubMed=25775403; DOI=10.1371/journal.pone.0120722;
Yeh C.H., Kuo P.L., Wang Y.Y., Wu Y.Y., Chen M.F., Lin D.Y., Lai T.H.,
Chiang H.S., Lin Y.H.;
"SEPT12/SPAG4/LAMINB1 complexes are required for maintaining the integrity
of the nuclear envelope in postmeiotic male germ cells.";
PLoS ONE 10:E0120722-E0120722(2015).
-!- FUNCTION: Filament-forming cytoskeletal GTPase (By similarity).
Involved in spermatogenesis. Involved in the morphogenesis of sperm
heads and the elongation of sperm tails probably implicating the
association with alpha- and beta-tubulins (PubMed:24213608). Forms a
filamentous structure with SEPTIN7, SEPTIN6, SEPTIN2 and probably
SEPTIN4 at the sperm annulus which is required for the structural
integrity and motility of the sperm tail during postmeiotic
differentiation (PubMed:25588830). May play a role in cytokinesis
(Potential). {ECO:0000250, ECO:0000269|PubMed:24213608,
ECO:0000269|PubMed:25588830, ECO:0000305}.
-!- SUBUNIT: 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 SEPTIN6 and SEPTIN11. Self-
associates. Component of a septin core octomeric complex consisting of
SEPTIN12, SEPTIN7, SEPTIN6 and SEPTIN2 or SEPTIN4 in the order 12-7-6-
2-2-6-7-12 or 12-7-6-4-4-6-7-12 and located in the sperm annulus; the
octomer polymerizes into filaments via the SEPTIN12 N- and C-termini;
the SEPTIN12:SEPTIN7 association is mediated by the respective GTP-
binding domains (PubMed:25588830). Interacts with SPAG4 and LMNB1
(PubMed:25775403). Associates with alpha- and beta-tubulins
(PubMed:24213608). {ECO:0000250, ECO:0000269|PubMed:18047794,
ECO:0000269|PubMed:18443421, ECO:0000269|PubMed:24213608,
ECO:0000269|PubMed:25588830}.
-!- INTERACTION:
Q8IYM1; Q9UHP6: RSPH14; NbExp=3; IntAct=EBI-2585067, EBI-748350;
Q8IYM1; Q8WYJ6: SEPTIN1; NbExp=12; IntAct=EBI-2585067, EBI-693002;
Q8IYM1; Q8IYM1: SEPTIN12; NbExp=5; IntAct=EBI-2585067, EBI-2585067;
Q8IYM1; Q15019: SEPTIN2; NbExp=7; IntAct=EBI-2585067, EBI-741220;
Q8IYM1; O43236: SEPTIN4; NbExp=5; IntAct=EBI-2585067, EBI-1047513;
Q8IYM1; Q99719: SEPTIN5; NbExp=7; IntAct=EBI-2585067, EBI-373345;
Q8IYM1; Q14141: SEPTIN6; NbExp=14; IntAct=EBI-2585067, EBI-745901;
Q8IYM1; Q16181: SEPTIN7; NbExp=17; IntAct=EBI-2585067, EBI-2009373;
Q8IYM1; Q9NPE6: SPAG4; NbExp=6; IntAct=EBI-2585067, EBI-10819434;
-!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:18047794}. Cytoplasm, cytoskeleton, spindle
{ECO:0000269|PubMed:18047794}. Nucleus {ECO:0000269|PubMed:25775403}.
Cell projection, cilium, flagellum {ECO:0000269|PubMed:22275165}.
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. Colocalized
with SPAG4 at the nuclear periphery in round spermatids, at sperm neck
in elongated spermatids and at midpiece regions in ejaculated
spermatozoa. {ECO:0000269|PubMed:18047794, ECO:0000269|PubMed:20801438,
ECO:0000269|PubMed:22275165, ECO:0000269|PubMed:25775403}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8IYM1-1; Sequence=Displayed;
Name=2;
IsoId=Q8IYM1-2; Sequence=VSP_029918;
-!- TISSUE SPECIFICITY: Widely expressed. Expressed in lymph node.
{ECO:0000269|PubMed:15915442, ECO:0000269|PubMed:17967425}.
-!- DEVELOPMENTAL STAGE: At the first step of spermiogenesis concentrated
around the acrosome. Afterwards expressed between the edge of the
acrosome and the perinuclear mantle of the manchette. Next, encircles
the upper site of the acrosome and forms the rim of the sperm nucleus.
With the formation of mitochondria and mature spermatozoa, localized at
the neck and annulus regions. {ECO:0000269|PubMed:20801438}.
-!- DISEASE: 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. {ECO:0000269|PubMed:22275165, ECO:0000269|PubMed:25588830,
ECO:0000269|PubMed:25775403}. Note=The disease is caused by variants
affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
GTPase superfamily. Septin GTPase family. {ECO:0000255|PROSITE-
ProRule:PRU01056}.
-!- SEQUENCE CAUTION:
Sequence=AAH24017.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; DQ456996; ABE68946.1; -; mRNA.
EMBL; DQ517531; ABF61438.1; -; mRNA.
EMBL; EF620906; ABR10901.1; -; mRNA.
EMBL; AK058139; BAB71681.1; -; mRNA.
EMBL; CH471112; EAW85265.1; -; Genomic_DNA.
EMBL; BC024017; AAH24017.1; ALT_INIT; mRNA.
EMBL; BC035619; AAH35619.1; -; mRNA.
CCDS; CCDS10522.1; -. [Q8IYM1-1]
CCDS; CCDS53987.1; -. [Q8IYM1-2]
RefSeq; NP_001147930.1; NM_001154458.2. [Q8IYM1-2]
RefSeq; NP_653206.2; NM_144605.4. [Q8IYM1-1]
RefSeq; XP_006720909.1; XM_006720846.2. [Q8IYM1-1]
PDB; 6MQ9; X-ray; 1.86 A; A/B/C/D=46-320.
PDB; 6MQB; X-ray; 2.12 A; A=46-320.
PDB; 6MQK; X-ray; 2.19 A; A/B/C/D=46-320.
PDB; 6MQL; X-ray; 2.17 A; A=46-320.
PDBsum; 6MQ9; -.
PDBsum; 6MQB; -.
PDBsum; 6MQK; -.
PDBsum; 6MQL; -.
SMR; Q8IYM1; -.
BioGRID; 125863; 17.
IntAct; Q8IYM1; 20.
STRING; 9606.ENSP00000268231; -.
iPTMnet; Q8IYM1; -.
PhosphoSitePlus; Q8IYM1; -.
BioMuta; SEPT12; -.
DMDM; 74750767; -.
MassIVE; Q8IYM1; -.
PaxDb; Q8IYM1; -.
PeptideAtlas; Q8IYM1; -.
PRIDE; Q8IYM1; -.
ProteomicsDB; 71202; -. [Q8IYM1-1]
ProteomicsDB; 71203; -. [Q8IYM1-2]
Antibodypedia; 24423; 145 antibodies.
DNASU; 124404; -.
Ensembl; ENST00000268231; ENSP00000268231; ENSG00000140623. [Q8IYM1-1]
Ensembl; ENST00000396693; ENSP00000379922; ENSG00000140623. [Q8IYM1-2]
GeneID; 124404; -.
KEGG; hsa:124404; -.
UCSC; uc002cxq.4; human. [Q8IYM1-1]
CTD; 124404; -.
DisGeNET; 124404; -.
GeneCards; SEPTIN12; -.
HGNC; HGNC:26348; SEPTIN12.
HPA; ENSG00000140623; Tissue enriched (testis).
MalaCards; SEPTIN12; -.
MIM; 611562; gene.
MIM; 614822; phenotype.
neXtProt; NX_Q8IYM1; -.
OpenTargets; ENSG00000140623; -.
Orphanet; 276234; Non-syndromic male infertility due to sperm motility disorder.
PharmGKB; PA162402916; -.
VEuPathDB; HostDB:ENSG00000140623.13; -.
eggNOG; KOG1547; Eukaryota.
GeneTree; ENSGT00940000158310; -.
HOGENOM; CLU_017718_7_1_1; -.
InParanoid; Q8IYM1; -.
OMA; CFDEDVN; -.
OrthoDB; 845354at2759; -.
PhylomeDB; Q8IYM1; -.
TreeFam; TF101078; -.
PathwayCommons; Q8IYM1; -.
SIGNOR; Q8IYM1; -.
BioGRID-ORCS; 124404; 4 hits in 954 CRISPR screens.
GenomeRNAi; 124404; -.
Pharos; Q8IYM1; Tbio.
PRO; PR:Q8IYM1; -.
Proteomes; UP000005640; Chromosome 16.
RNAct; Q8IYM1; protein.
Bgee; ENSG00000140623; Expressed in testis and 93 other tissues.
ExpressionAtlas; Q8IYM1; baseline and differential.
Genevisible; Q8IYM1; HS.
GO; GO:0032153; C:cell division site; IBA:GO_Central.
GO; GO:0032154; C:cleavage furrow; ISS:UniProtKB.
GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
GO; GO:0030496; C:midbody; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0031105; C:septin complex; IDA:UniProtKB.
GO; GO:0005940; C:septin ring; IBA:GO_Central.
GO; GO:0097227; C:sperm annulus; IDA:UniProtKB.
GO; GO:0005819; C:spindle; IDA:UniProtKB.
GO; GO:0001725; C:stress fiber; ISS:UniProtKB.
GO; GO:0019003; F:GDP binding; ISS:UniProtKB.
GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
GO; GO:0035091; F:phosphatidylinositol binding; ISS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0034613; P:cellular protein localization; IBA:GO_Central.
GO; GO:0061640; P:cytoskeleton-dependent cytokinesis; IBA:GO_Central.
GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
CDD; cd01850; CDC_Septin; 1.
InterPro; IPR030379; G_SEPTIN_dom.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR016491; Septin.
Pfam; PF00735; Septin; 1.
PIRSF; PIRSF006698; Septin; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS51719; G_SEPTIN; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell cycle; Cell division;
Cell projection; Cilium; Cytoplasm; Cytoskeleton; Differentiation;
Disease variant; Flagellum; GTP-binding; Nucleotide-binding; Nucleus;
Reference proteome; Spermatogenesis.
CHAIN 1..358
/note="Septin-12"
/id="PRO_0000312860"
DOMAIN 46..317
/note="Septin-type G"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
NP_BIND 56..63
/note="GTP"
/evidence="ECO:0000250"
NP_BIND 195..203
/note="GTP"
/evidence="ECO:0000250"
REGION 1..25
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 46..319
/note="Interaction with SEPTIN7"
/evidence="ECO:0000269|PubMed:25588830"
REGION 56..63
/note="G1 motif"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
REGION 112..115
/note="G3 motif"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
REGION 194..197
/note="G4 motif"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
REGION 258..358
/note="Self-association (via N-terminus) to polymerize
octomeric septin 12-7-6-2/4-2/4-6-7-12 filaments"
BINDING 89
/note="GTP"
/evidence="ECO:0000250"
BINDING 115
/note="GTP; via amide nitrogen"
/evidence="ECO:0000250"
BINDING 251
/note="GTP; via amide nitrogen and carbonyl oxygen"
/evidence="ECO:0000250"
BINDING 266
/note="GTP"
/evidence="ECO:0000250"
VAR_SEQ 125..170
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:17685441,
ECO:0000303|PubMed:18047794"
/id="VSP_029918"
VARIANT 89
/note="T -> M (in SPGF10; results in significantly reduced
GTP hydrolysis; disrupts interaction with SEPTIN7, SEPTIN6
and SEPTIN2; decreases interaction with SPAG4;
dbSNP:rs199696526)"
/evidence="ECO:0000269|PubMed:22275165,
ECO:0000269|PubMed:25588830, ECO:0000269|PubMed:25775403"
/id="VAR_068097"
VARIANT 197
/note="D -> N (in SPGF10; results in significantly reduced
GTP hydrolysis due to impaired GTP binding; disrupts
interaction with SEPTIN7, SEPTIN6 and SEPTIN2; absence of
SEPTIN12, SEPTIN7, SEPTIN6, SEPTIN2 and SEPTIN4 from the
sperm annulus; disrupts interaction with LMNB1;
dbSNP:rs371195126)"
/evidence="ECO:0000269|PubMed:22275165,
ECO:0000269|PubMed:25588830, ECO:0000269|PubMed:25775403"
/id="VAR_068098"
VARIANT 213
/note="Q -> R (in dbSNP:rs6500633)"
/id="VAR_057176"
MUTAGEN 56
/note="G->N: Abolishes binding to GTP and to SEPTIN11, and
also abolishes the ability of SEPTIN12 to form filamentous
structures."
/evidence="ECO:0000269|PubMed:18443421"
CONFLICT 22
/note="P -> T (in Ref. 6; AAH24017)"
/evidence="ECO:0000305"
CONFLICT 258
/note="V -> M (in Ref. 4; BAB71681)"
/evidence="ECO:0000305"
CONFLICT 280
/note="H -> L (in Ref. 6; AAH24017)"
/evidence="ECO:0000305"
STRAND 49..57
/evidence="ECO:0007829|PDB:6MQ9"
HELIX 62..71
/evidence="ECO:0007829|PDB:6MQ9"
STRAND 93..101
/evidence="ECO:0007829|PDB:6MQ9"
STRAND 104..112
/evidence="ECO:0007829|PDB:6MQ9"
STRAND 119..121
/evidence="ECO:0007829|PDB:6MQ9"
TURN 123..126
/evidence="ECO:0007829|PDB:6MQ9"
HELIX 127..147
/evidence="ECO:0007829|PDB:6MQ9"
HELIX 150..152
/evidence="ECO:0007829|PDB:6MQ9"
STRAND 160..165
/evidence="ECO:0007829|PDB:6MQ9"
HELIX 174..184
/evidence="ECO:0007829|PDB:6MQ9"
STRAND 189..193
/evidence="ECO:0007829|PDB:6MQ9"
HELIX 196..198
/evidence="ECO:0007829|PDB:6MQ9"
HELIX 201..217
/evidence="ECO:0007829|PDB:6MQ9"
HELIX 226..228
/evidence="ECO:0007829|PDB:6MQ9"
HELIX 232..244
/evidence="ECO:0007829|PDB:6MQ9"
STRAND 246..248
/evidence="ECO:0007829|PDB:6MQ9"
STRAND 255..258
/evidence="ECO:0007829|PDB:6MQ9"
STRAND 261..268
/evidence="ECO:0007829|PDB:6MQ9"
STRAND 271..274
/evidence="ECO:0007829|PDB:6MQ9"
TURN 278..280
/evidence="ECO:0007829|PDB:6MQ9"
HELIX 283..291
/evidence="ECO:0007829|PDB:6MQ9"
HELIX 295..304
/evidence="ECO:0007829|PDB:6MQ9"
HELIX 306..314
/evidence="ECO:0007829|PDB:6MQ9"
SEQUENCE 358 AA; 40748 MW; 31968F366DEFB4FD CRC64;
MDPLRRSPSP CLSSQPSSPS TPPCEMLGPV GIEAVLDQLK IKAMKMGFEF NIMVVGQSGL
GKSTMVNTLF KSKVWKSNPP GLGVPTPQTL QLHSLTHVIE EKGVKLKLTV TDTPGFGDQI
NNDNCWDPIL GYINEQYEQY LQEEILITRQ RHIPDTRVHC CVYFVPPTGH CLRPLDIEFL
QRLCRTVNVV PVIARADSLT MEEREAFRRR IQQNLRTHCI DVYPQMCFDE DINDKILNSK
LRDRIPFAVV GADQEHLVNG RCVLGRKTKW GIIEVENMAH CEFPLLRDLL IRSHLQDLKD
ITHNIHYENY RVIRLNESHL LPRGPGWVNL APASPGQLTT PRTFKVCRGA HDDSDDEF


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WP104: Alanine and aspartate metabolism
WP1354: B Cell Receptor Signaling Pathway
WP444: Signaling of Hepatocyte Growth Factor Receptor
WP240: Alanine and aspartate metabolism
WP465: Tryptophan metabolism
WP2085: miRNAs involved in DDR
WP1337: MAPK signaling pathway
WP426: Urea cycle and metabolism of amino groups
WP1367: TGF-beta Receptor Signaling Pathway
WP1345: T Cell Receptor Signaling Pathway
WP1386: Integrin-mediated cell adhesion
WP2359: Parkin-Ubiquitin Proteasomal System pathway
WP270: Tryptophan metabolism
WP1545: miRNAs involved in DDR
WP2233: Immune responses in the epidermis
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WP1323: EGFR1 Signaling Pathway
WP1315: IL-5 Signaling Pathway
WP1359: IL-3 Signaling Pathway
WP106: Alanine and aspartate metabolism
WP1126: Tryptophan metabolism
WP1530: miRNA regulation of DNA Damage Response
WP2087: miRNA regulation of DNA Damage Response
WP79: Tryptophan metabolism
WP497: Urea cycle and metabolism of amino groups

Related Genes :
[SEPTIN12 SEPT12] Septin-12
[CDC12 CLA10 PSL7 YHR107C] Cell division control protein 12 (Septin)
[Septin12 Sept12] Septin-12
[spn6 SPCC188.12 SPCC584.09] Septin homolog spn6
[SEPTIN9 KIAA0991 MSF SEPT9] Septin-9 (MLL septin-like fusion protein MSF-A) (MLL septin-like fusion protein) (Ovarian/Breast septin) (Ov/Br septin) (Septin D1)
[Septin9 Sept9] Septin-9 (Eighth septin) (Eseptin) (Septin-like protein) (SLP)
[SEPTIN7 CDC10 SEPT7] Septin-7 (CDC10 protein homolog)
[SEPTIN6 KIAA0128 SEP2 SEPT6] Septin-6
[SEPTIN2 DIFF6 KIAA0158 NEDD5 SEPT2] Septin-2 (Neural precursor cell expressed developmentally down-regulated protein 5) (NEDD-5)
[Septin7 Cdc10 Sept7] Septin-7 (CDC10 protein homolog)
[Septin7 Cdc10 Sept7] Septin-7 (CDC10 protein homolog)
[Septin6 Kiaa0128 Sept6] Septin-6
[Septin2 Sept2 Vesp11] Septin-2 (Vascular endothelial cell specific protein 11)
[Septin2 Nedd5 Sept2] Septin-2 (Neural precursor cell expressed developmentally down-regulated protein 5) (NEDD-5)
[SEPTIN2 SEPT2] Septin-2
[SEPTIN5 PNUTL1 SEPT5] Septin-5 (Cell division control-related protein 1) (CDCrel-1) (Peanut-like protein 1)
[SEPTIN4 ARTS C17orf47 PNUTL2 SEP4 SEPT4 hucep-7] Septin-4 (Apoptosis-related protein in the TGF-beta signaling pathway) (ARTS) (Bradeion beta) (Brain protein H5) (CE5B3 beta) (Cell division control-related protein 2) (hCDCREL-2) (Cerebral protein 7) (Peanut-like protein 2)
[Septin4 Pnutl2 Sept4] Septin-4 (Brain protein H5) (Peanut-like protein 2)
[SEPTIN11 SEPT11] Septin-11
[SEPTIN1 DIFF6 PNUTL3 SEPT1] Septin-1 (LARP) (Peanut-like protein 3) (Serologically defined breast cancer antigen NY-BR-24)
[SEPTIN8 KIAA0202 SEPT8] Septin-8
[Septin8 Sept8] Septin-8
[Septin5 Pnutl1 Sept5] Septin-5 (Cell division control-related protein 1) (CDCrel-1) (Peanut-like protein 1)
[Septin3 Sept3] Neuronal-specific septin-3 (G-septin) (P40)
[SEPTIN7 CDC10 SEPT7] Septin-7 (CDC10 protein homolog)
[Septin5 Pnutl1 Sept5] Septin-5 (Cell division control-related protein 1) (CDCrel-1) (Peanut-like protein 1)
[Septin11 Sept11] Septin-11
[Septin9 Kiaa0991 Sept9 Sint1] Septin-9 (SL3-3 integration site 1 protein)
[Septin8 Kiaa0202 Sept8] Septin-8
[Septin11 D5Ertd606e Sept11] Septin-11

Bibliography :
[30488758] Association of single nucleotide polymorphism c.673C>A/p.Gln225Lys in SEPT12 gene with spermatogenesis failure in male idiopathic infertility in Northeast China.
[22275165] SEPT12 mutations cause male infertility with defective sperm annulus.
[20801438] SEPT12 deficiency causes sperm nucleus damage and developmental arrest of preimplantation embryos.