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SPT13_HUMAN
ID   SPT13_HUMAN             Reviewed;         652 AA.
AC   Q96N96; A2VEA9; A6NF85; B4DQB1; B4DSZ0; B4DVM8; J3KPJ7; J3KQH2; Q5VX68;
AC   Q6ZML1; Q8N873; Q8TEK6;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 170.
DE   RecName: Full=Spermatogenesis-associated protein 13;
DE   AltName: Full=APC-stimulated guanine nucleotide exchange factor 2;
DE            Short=Asef2;
GN   Name=SPATA13 {ECO:0000303|PubMed:28397838, ECO:0000312|HGNC:HGNC:23222};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH APC AND
RP   RAC1, TISSUE SPECIFICITY, AND ACTIVITY REGULATION.
RX   PubMed=17145773; DOI=10.1128/mcb.01608-06;
RA   Hamann M.J., Lubking C.M., Luchini D.N., Billadeau D.D.;
RT   "Asef2 functions as a Cdc42 exchange factor and is stimulated by the
RT   release of an autoinhibitory module from a concealed C-terminal activation
RT   element.";
RL   Mol. Cell. Biol. 27:1380-1393(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3; 4 AND 5).
RC   TISSUE=Kidney, Lung, and Spleen;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057823; DOI=10.1038/nature02379;
RA   Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA   Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA   Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA   Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA   Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA   Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA   Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA   Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA   Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA   Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA   Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA   Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA   Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA   Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA   Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA   Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA   Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA   Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA   Rogers J., Ross M.T.;
RT   "The DNA sequence and analysis of human chromosome 13.";
RL   Nature 428:522-528(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 126-652.
RC   TISSUE=Spleen;
RA   Jikuya H., Takano J., Nomura N., Kikuno R., Nagase T., Ohara O.;
RT   "The nucleotide sequence of a long cDNA clone isolated from human spleen.";
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   FUNCTION, INTERACTION WITH APC, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP   AND ALTERNATIVE SPLICING.
RX   PubMed=17599059; DOI=10.1038/sj.onc.1210574;
RA   Kawasaki Y., Sagara M., Shibata Y., Shirouzu M., Yokoyama S., Akiyama T.;
RT   "Identification and characterization of Asef2, a guanine-nucleotide
RT   exchange factor specific for Rac1 and Cdc42.";
RL   Oncogene 26:7620-7627(2007).
RN   [8]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=19893577; DOI=10.1038/embor.2009.233;
RA   Kawasaki Y., Tsuji S., Muroya K., Furukawa S., Shibata Y., Okuno M.,
RA   Ohwada S., Akiyama T.;
RT   "The adenomatous polyposis coli-associated exchange factors Asef and Asef2
RT   are required for adenoma formation in Apc(Min/+)mice.";
RL   EMBO Rep. 10:1355-1362(2009).
RN   [9]
RP   FUNCTION.
RX   PubMed=19934221; DOI=10.1242/jcs.053728;
RA   Bristow J.M., Sellers M.H., Majumdar D., Anderson B., Hu L., Webb D.J.;
RT   "The Rho-family GEF Asef2 activates Rac to modulate adhesion and actin
RT   dynamics and thereby regulate cell migration.";
RL   J. Cell Sci. 122:4535-4546(2009).
RN   [10]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PPP1R9B.
RX   PubMed=19151759; DOI=10.1038/onc.2008.478;
RA   Sagara M., Kawasaki Y., Iemura S.I., Natsume T., Takai Y., Akiyama T.;
RT   "Asef2 and Neurabin2 cooperatively regulate actin cytoskeletal organization
RT   and are involved in HGF-induced cell migration.";
RL   Oncogene 28:1357-1365(2009).
RN   [11]
RP   VARIANT TRP-89.
RX   PubMed=28397838; DOI=10.1038/mp.2017.60;
RA   Harripaul R., Vasli N., Mikhailov A., Rafiq M.A., Mittal K.,
RA   Windpassinger C., Sheikh T.I., Noor A., Mahmood H., Downey S., Johnson M.,
RA   Vleuten K., Bell L., Ilyas M., Khan F.S., Khan V., Moradi M., Ayaz M.,
RA   Naeem F., Heidari A., Ahmed I., Ghadami S., Agha Z., Zeinali S., Qamar R.,
RA   Mozhdehipanah H., John P., Mir A., Ansar M., French L., Ayub M.,
RA   Vincent J.B.;
RT   "Mapping autosomal recessive intellectual disability: combined microarray
RT   and exome sequencing identifies 26 novel candidate genes in 192
RT   consanguineous families.";
RL   Mol. Psychiatry 23:973-984(2018).
CC   -!- FUNCTION: Acts as guanine nucleotide exchange factor (GEF) for RHOA,
CC       RAC1 and CDC42 GTPases. Regulates cell migration and adhesion assembly
CC       and disassembly through a RAC1, PI3K, RHOA and AKT1-dependent
CC       mechanism. Increases both RAC1 and CDC42 activity, but decreases the
CC       amount of active RHOA. Required for MMP9 up-regulation via the JNK
CC       signaling pathway in colorectal tumor cells. Involved in tumor
CC       angiogenesis and may play a role in intestinal adenoma formation and
CC       tumor progression. {ECO:0000269|PubMed:17145773,
CC       ECO:0000269|PubMed:17599059, ECO:0000269|PubMed:19151759,
CC       ECO:0000269|PubMed:19893577, ECO:0000269|PubMed:19934221}.
CC   -!- ACTIVITY REGULATION: Both the ABR and the SH3 domains contribute to
CC       maintaining the protein in an inhibited conformation by associating
CC       with the C-terminal tail. Binding of these domains to the C-terminal
CC       tail inhibits the activity of the protein by blocking a region that is
CC       required for its GEF activity. {ECO:0000269|PubMed:17145773}.
CC   -!- SUBUNIT: Interacts (via ABR and SH3 domain) with APC. The binding of
CC       APC enhances its GEF activity by relieving it from an autoinhibitory
CC       conformation, in which the ABR and SH3 domains are associated with the
CC       C-terminal tail. Interacts (via C-terminal tail) with PPP1R9B (via C-
CC       terminus). Interacts with RAC1. {ECO:0000269|PubMed:17145773,
CC       ECO:0000269|PubMed:17599059, ECO:0000269|PubMed:19151759}.
CC   -!- INTERACTION:
CC       Q96N96; P25054: APC; NbExp=5; IntAct=EBI-13618641, EBI-727707;
CC       Q96N96-1; P25054: APC; NbExp=5; IntAct=EBI-13638906, EBI-727707;
CC       Q96N96-1; Q96N96-1: SPATA13; NbExp=4; IntAct=EBI-13638906, EBI-13638906;
CC       Q96N96-2; P25054: APC; NbExp=2; IntAct=EBI-13639118, EBI-727707;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cell projection, filopodium. Cell
CC       projection, lamellipodium. Cell projection, ruffle membrane.
CC       Note=Accumulates in the lamellipodium and ruffle membrane in response
CC       to hepatocyte growth factor (HGF) treatment.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC         Comment=Additional isoforms seem to exist.;
CC       Name=1; Synonyms=ASEF-2b;
CC         IsoId=Q96N96-1; Sequence=Displayed;
CC       Name=2; Synonyms=ASEF-2a;
CC         IsoId=Q96N96-2; Sequence=VSP_041030;
CC       Name=3;
CC         IsoId=Q96N96-3; Sequence=VSP_041031;
CC       Name=4;
CC         IsoId=Q96N96-4; Sequence=VSP_041032, VSP_041034;
CC       Name=5;
CC         IsoId=Q96N96-5; Sequence=VSP_041032, VSP_041033;
CC       Name=6;
CC         IsoId=Q96N96-6; Sequence=VSP_054112;
CC   -!- TISSUE SPECIFICITY: Expressed at high levels in the placenta, spleen
CC       and kidney, at moderate levels in lung, small intestine, liver, brain
CC       and heart, and at low levels in skeletal muscle. Expression is
CC       aberrantly enhanced in most colorectal tumors.
CC       {ECO:0000269|PubMed:17145773, ECO:0000269|PubMed:17599059,
CC       ECO:0000269|PubMed:19893577}.
CC   -!- DOMAIN: The C-terminal tail is required for its GEF activity.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC04977.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; BK006072; DAA05848.1; -; mRNA.
DR   EMBL; AK055770; BAB71009.1; -; mRNA.
DR   EMBL; AK097217; BAC04977.1; ALT_INIT; mRNA.
DR   EMBL; AK123031; BAG53856.1; -; mRNA.
DR   EMBL; AK298717; BAG60873.1; -; mRNA.
DR   EMBL; AK299981; BAG61802.1; -; mRNA.
DR   EMBL; AK301149; BAG62740.1; -; mRNA.
DR   EMBL; AL136963; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL139324; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL359736; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL445985; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471075; EAX08331.1; -; Genomic_DNA.
DR   EMBL; BC109290; AAI09291.1; -; mRNA.
DR   EMBL; BC109291; AAI09292.1; -; mRNA.
DR   EMBL; AK074117; BAB84943.1; -; mRNA.
DR   EMBL; AK160371; BAD18714.1; -; mRNA.
DR   CCDS; CCDS53857.1; -. [Q96N96-6]
DR   CCDS; CCDS66517.1; -. [Q96N96-2]
DR   CCDS; CCDS66518.1; -. [Q96N96-3]
DR   CCDS; CCDS9305.1; -. [Q96N96-1]
DR   RefSeq; NP_001159743.1; NM_001166271.2. [Q96N96-6]
DR   RefSeq; NP_001273721.1; NM_001286792.1.
DR   RefSeq; NP_001273722.1; NM_001286793.1.
DR   RefSeq; NP_001273723.1; NM_001286794.1. [Q96N96-3]
DR   RefSeq; NP_001273724.1; NM_001286795.1. [Q96N96-2]
DR   RefSeq; NP_694568.1; NM_153023.3. [Q96N96-1]
DR   AlphaFoldDB; Q96N96; -.
DR   SMR; Q96N96; -.
DR   BioGRID; 128693; 17.
DR   IntAct; Q96N96; 12.
DR   STRING; 9606.ENSP00000398560; -.
DR   iPTMnet; Q96N96; -.
DR   PhosphoSitePlus; Q96N96; -.
DR   BioMuta; SPATA13; -.
DR   DMDM; 74752049; -.
DR   jPOST; Q96N96; -.
DR   MassIVE; Q96N96; -.
DR   MaxQB; Q96N96; -.
DR   PaxDb; Q96N96; -.
DR   PeptideAtlas; Q96N96; -.
DR   PRIDE; Q96N96; -.
DR   ProteomicsDB; 77489; -. [Q96N96-1]
DR   ProteomicsDB; 77490; -. [Q96N96-2]
DR   ProteomicsDB; 77491; -. [Q96N96-3]
DR   ProteomicsDB; 77492; -. [Q96N96-4]
DR   ProteomicsDB; 77493; -. [Q96N96-5]
DR   Antibodypedia; 49852; 102 antibodies from 23 providers.
DR   DNASU; 221178; -.
DR   Ensembl; ENST00000343003.10; ENSP00000343631.6; ENSG00000182957.16. [Q96N96-3]
DR   Ensembl; ENST00000382095.8; ENSP00000371527.4; ENSG00000182957.16. [Q96N96-1]
DR   Ensembl; ENST00000382108.8; ENSP00000371542.3; ENSG00000182957.16. [Q96N96-6]
DR   Ensembl; ENST00000399949.6; ENSP00000382830.2; ENSG00000182957.16. [Q96N96-2]
DR   Ensembl; ENST00000424834.6; ENSP00000398560.2; ENSG00000182957.16. [Q96N96-6]
DR   GeneID; 221178; -.
DR   KEGG; hsa:221178; -.
DR   MANE-Select; ENST00000382108.8; ENSP00000371542.3; NM_001166271.3; NP_001159743.1. [Q96N96-6]
DR   UCSC; uc001upg.4; human. [Q96N96-1]
DR   CTD; 221178; -.
DR   DisGeNET; 221178; -.
DR   GeneCards; SPATA13; -.
DR   HGNC; HGNC:23222; SPATA13.
DR   HPA; ENSG00000182957; Tissue enhanced (lymphoid).
DR   MIM; 613324; gene.
DR   neXtProt; NX_Q96N96; -.
DR   OpenTargets; ENSG00000182957; -.
DR   PharmGKB; PA134912609; -.
DR   VEuPathDB; HostDB:ENSG00000182957; -.
DR   eggNOG; KOG3519; Eukaryota.
DR   GeneTree; ENSGT00940000154103; -.
DR   HOGENOM; CLU_008436_0_0_1; -.
DR   InParanoid; Q96N96; -.
DR   OMA; PETECQK; -.
DR   OrthoDB; 65769at2759; -.
DR   PhylomeDB; Q96N96; -.
DR   TreeFam; TF316832; -.
DR   PathwayCommons; Q96N96; -.
DR   Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR   Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR   SignaLink; Q96N96; -.
DR   SIGNOR; Q96N96; -.
DR   BioGRID-ORCS; 221178; 16 hits in 1073 CRISPR screens.
DR   ChiTaRS; SPATA13; human.
DR   GenomeRNAi; 221178; -.
DR   Pharos; Q96N96; Tbio.
DR   PRO; PR:Q96N96; -.
DR   Proteomes; UP000005640; Chromosome 13.
DR   RNAct; Q96N96; protein.
DR   Bgee; ENSG00000182957; Expressed in epithelial cell of pancreas and 189 other tissues.
DR   ExpressionAtlas; Q96N96; baseline and differential.
DR   Genevisible; Q96N96; HS.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0030175; C:filopodium; IDA:UniProtKB.
DR   GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0032587; C:ruffle membrane; IDA:UniProtKB.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0016477; P:cell migration; IMP:UniProtKB.
DR   GO; GO:0046847; P:filopodium assembly; IMP:UniProtKB.
DR   GO; GO:0030032; P:lamellipodium assembly; IMP:UniProtKB.
DR   GO; GO:0030334; P:regulation of cell migration; IMP:UniProtKB.
DR   GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR   CDD; cd00160; RhoGEF; 1.
DR   Gene3D; 1.20.900.10; -; 1.
DR   Gene3D; 2.30.29.30; -; 1.
DR   InterPro; IPR035899; DBL_dom_sf.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00621; RhoGEF; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00325; RhoGEF; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF48065; SSF48065; 1.
DR   SUPFAM; SSF50044; SSF50044; 1.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Cell projection; Cytoplasm;
KW   Guanine-nucleotide releasing factor; Membrane; Phosphoprotein;
KW   Reference proteome; SH3 domain.
FT   CHAIN           1..652
FT                   /note="Spermatogenesis-associated protein 13"
FT                   /id="PRO_0000278448"
FT   DOMAIN          147..206
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   DOMAIN          240..424
FT                   /note="DH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT   DOMAIN          455..561
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          81..108
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          98..150
FT                   /note="ABR (APC-binding region) domain"
FT   REGION          209..235
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          561..652
FT                   /note="C-terminal tail"
FT   MOD_RES         78
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5DU57"
FT   MOD_RES         114
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5DU57"
FT   VAR_SEQ         1..96
FT                   /note="MTSASPEDQNAPVGCPKGARRRRPISVIGGVSLYGTNQTEELDNLLTQPASR
FT                   PPMPAHQVPPYKAVSARFRPFTFSQSTPIGLDRVGRRRQMRASN -> MVARGEIARFW
FT                   SLESLHL (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_041030"
FT   VAR_SEQ         1..96
FT                   /note="MTSASPEDQNAPVGCPKGARRRRPISVIGGVSLYGTNQTEELDNLLTQPASR
FT                   PPMPAHQVPPYKAVSARFRPFTFSQSTPIGLDRVGRRRQMRASN -> MGFIIHIQQVK
FT                   KQRKKLDQGLILKKEKYRKEKKCASLSFE (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_041031"
FT   VAR_SEQ         1..54
FT                   /note="Missing (in isoform 4 and isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_041032"
FT   VAR_SEQ         1
FT                   /note="M -> MTQAAVRPWAPCLENMTTAPNGLGPGPAAPCAGSDLKDAKMVTSLAC
FT                   GNGVCGCSPGGDTDTQEAKLSPAKLVRLFSTSRKRTGAHPERPHSMVLVGNSSTWNTLA
FT                   SFRKMGSFKKLKSSVLKGIQSREGSNACSKGEASEHGLGKSIPNGAVPGAQASRGSPLA
FT                   PGPACGALRPAEWGTLDGSDLEDTDDAFQRSTHRSRSLRRAYGLGRICLLDAPQNHATP
FT                   TIATGQVPAVCEILVRDPENNSMGYRRSKSTDNLAFLKKSSFKRKSTSNLADLRTAHDA
FT                   RVPQRTLSSSSTDSQKLGSGRTKRWRSPIRAKDFDRVFKLVSNVTEAAWRRESPRSGAP
FT                   SPGEASLRLQAHSRLHDDYSRRVSRSTEQDSRRGGAVMHGTTATCTVAPGFGSATSKGP
FT                   HLDADTAVFPLETKSSWAVESDSSCTCSSLPSPIVQDVLSKDSCDPNAGSQLTFDPEQP
FT                   PTPLRPTTPKPQSPQSPQSPGAGSASCHSNHSALSANSEESEGRAEEPAQREPGPVSLQ
FT                   DPLEATHGDEGSKDLLVNIGVAAGPEEKEKEEVVPDGPWRRSSSQDEERTEAQRTPKRR
FT                   WGSGRRPRPRPFSDYGQLASRSLSIPEDSVAADPQKEDRVDEDPQASM (in
FT                   isoform 6)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_054112"
FT   VAR_SEQ         203..264
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_041033"
FT   VAR_SEQ         595..652
FT                   /note="GYNRCPVAPPHQGLHPIHQRHITMPTSVPQQQVFGLAEPKRKSSLFWHTFNR
FT                   LTPFRK -> VRLQQVPRGPTAPGPAPHPPAPHHYAHKRPPAAGLWPGGTQEEVLALLA
FT                   HLQQAHPLPEMKTGGCASMELGVKRRN (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_041034"
FT   VARIANT         20
FT                   /note="R -> W (in dbSNP:rs7330736)"
FT                   /id="VAR_030776"
FT   VARIANT         89
FT                   /note="R -> W (found in two consanguineous families with
FT                   intellectual disability; unknown pathological significance;
FT                   dbSNP:rs201402934)"
FT                   /evidence="ECO:0000269|PubMed:28397838"
FT                   /id="VAR_080767"
FT   CONFLICT        304
FT                   /note="E -> G (in Ref. 2; BAG61802)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        520
FT                   /note="C -> R (in Ref. 2; BAG62740)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        537
FT                   /note="E -> G (in Ref. 2; BAG62740)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   652 AA;  74820 MW;  7C922E8AF0A9C836 CRC64;
     MTSASPEDQN APVGCPKGAR RRRPISVIGG VSLYGTNQTE ELDNLLTQPA SRPPMPAHQV
     PPYKAVSARF RPFTFSQSTP IGLDRVGRRR QMRASNVSSD GGTEPSALVD DNGSEEDFSY
     EDLCQASPRY LQPGGEQLAI NELISDGNVV CAEALWDHVT MDDQELGFKA GDVIQVLEAS
     NKDWWWGRSE DKEAWFPASF VRLRVNQEEL SENSSSTPSE EQDEEASQSR HRHCENKQQM
     RTNVIREIMD TERVYIKHLR DICEGYIRQC RKHTGMFTVA QLATIFGNIE DIYKFQRKFL
     KDLEKQYNKE EPHLSEIGSC FLQNQEGFAI YSEYCNNHPG ACLELANLMK QGKYRHFFEA
     CRLLQQMIDI AIDGFLLTPV QKICKYPLQL AELLKYTTQE HGDYSNIKAA YEAMKNVACL
     INERKRKLES IDKIARWQVS IVGWEGLDIL DRSSELIHSG ELTKITKQGK SQQRTFFLFD
     HQLVSCKKDL LRRDMLYYKG RLDMDEMELV DLGDGRDKDC NLSVKNAFKL VSRTTDEVYL
     FCAKKQEDKA RWLQACADER RRVQEDKEMG MEISENQKKL AMLNAQKAGH GKSKGYNRCP
     VAPPHQGLHP IHQRHITMPT SVPQQQVFGL AEPKRKSSLF WHTFNRLTPF RK
 
 
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