SHOT1_HUMAN
ID SHOT1_HUMAN Reviewed; 631 AA.
AC A0MZ66; A8MYU7; B3KRD3; B3KRH2; B3KTE0; B3KTJ7; B3KTJ8; B4E3U1; B7Z7Z9;
AC Q68DG1; Q6PIM5; Q9HCH4; Q9NUV0;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 4.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Shootin-1 {ECO:0000312|HGNC:HGNC:29319};
DE AltName: Full=Shootin1 {ECO:0000250|UniProtKB:A0MZ67};
GN Name=SHTN1 {ECO:0000312|HGNC:HGNC:29319}; Synonyms=KIAA1598;
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 2).
RX PubMed=17030985; DOI=10.1083/jcb.200604160;
RA Toriyama M., Shimada T., Kim K.B., Mitsuba M., Nomura E., Katsuta K.,
RA Sakumura Y., Roepstorff P., Inagaki N.;
RT "Shootin1: a protein involved in the organization of an asymmetric signal
RT for neuronal polarization.";
RL J. Cell Biol. 175:147-157(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 5; 6; 7 AND 8), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 349-631 (ISOFORM 1).
RC TISSUE=Brain, Placenta, Testis, and Uterus;
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 MRNA] (ISOFORM 3).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [5]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 388-631 (ISOFORM 1).
RC TISSUE=Brain;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 11-631 (ISOFORM 2).
RX PubMed=10997877; DOI=10.1093/dnares/7.4.271;
RA Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:273-281(2000).
RN [8]
RP PROTEIN SEQUENCE OF 9-17; 160-169; 187-197 AND 467-479, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (JAN-2009) to UniProtKB.
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-506; SER-515; SER-532 AND
RP THR-537, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-506, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249; THR-496; SER-506;
RP SER-532 AND THR-537, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-506, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-249; SER-375; SER-473;
RP THR-487; SER-494; SER-506; SER-532; SER-534 AND THR-537, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375; SER-494 AND SER-506, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Involved in the generation of internal asymmetric signals
CC required for neuronal polarization and neurite outgrowth. Mediates
CC netrin-1-induced F-actin-substrate coupling or 'clutch engagement'
CC within the axon growth cone through activation of CDC42, RAC1 and PAK1-
CC dependent signaling pathway, thereby converting the F-actin retrograde
CC flow into traction forces, concomitantly with filopodium extension and
CC axon outgrowth. Plays a role in cytoskeletal organization by regulating
CC the subcellular localization of phosphoinositide 3-kinase (PI3K)
CC activity at the axonal growth cone. Also plays a role in regenerative
CC neurite outgrowth. In the developing cortex, cooperates with KIF20B to
CC promote both the transition from the multipolar to the bipolar stage
CC and the radial migration of cortical neurons from the ventricular zone
CC toward the superficial layer of the neocortex. Involved in the
CC accumulation of phosphatidylinositol 3,4,5-trisphosphate (PIP3) in the
CC growth cone of primary hippocampal neurons.
CC {ECO:0000250|UniProtKB:A0MZ67, ECO:0000250|UniProtKB:Q8K2Q9}.
CC -!- SUBUNIT: Interacts with L1CAM; this interaction occurs in axonal growth
CC cones. Interacts with actin filament retrograde flow; this interaction
CC is enhanced in a netrin-1- and PAK1-dependent manner and promotes F-
CC actin-substrate coupling and concomitant formation of traction forces
CC at axonal growth cones. Interacts with RUFY3. Interacts with PFN2.
CC Interacts (via N-terminus) with KIF20B; this interaction is direct and
CC promotes the association of SHTN1 to microtubules in primary neurons.
CC Associates with microtubule. {ECO:0000250|UniProtKB:A0MZ67,
CC ECO:0000250|UniProtKB:Q8K2Q9}.
CC -!- INTERACTION:
CC A0MZ66; P62508: ESRRG; NbExp=3; IntAct=EBI-308778, EBI-2834260;
CC A0MZ66; P05413: FABP3; NbExp=3; IntAct=EBI-308778, EBI-704216;
CC A0MZ66; Q6PJR7: IGL@; NbExp=3; IntAct=EBI-308778, EBI-10254102;
CC A0MZ66; Q9Y5B8: NME7; NbExp=3; IntAct=EBI-308778, EBI-744782;
CC A0MZ66-4; P62508-3: ESRRG; NbExp=3; IntAct=EBI-12097232, EBI-12001340;
CC A0MZ66-4; Q9Y2D4: EXOC6B; NbExp=3; IntAct=EBI-12097232, EBI-2690026;
CC A0MZ66-4; P05413: FABP3; NbExp=3; IntAct=EBI-12097232, EBI-704216;
CC A0MZ66-4; Q9Y5B8: NME7; NbExp=3; IntAct=EBI-12097232, EBI-744782;
CC A0MZ66-4; A0MZ66-4: SHTN1; NbExp=3; IntAct=EBI-12097232, EBI-12097232;
CC A0MZ66-4; Q15025: TNIP1; NbExp=3; IntAct=EBI-12097232, EBI-357849;
CC A0MZ66-4; Q05BL1: TP53BP2; NbExp=3; IntAct=EBI-12097232, EBI-11952721;
CC A0MZ66-4; Q9NP64: ZCCHC17; NbExp=3; IntAct=EBI-12097232, EBI-746345;
CC A0MZ66-7; O75936: BBOX1; NbExp=3; IntAct=EBI-10171490, EBI-715662;
CC A0MZ66-7; Q12800: TFCP2; NbExp=3; IntAct=EBI-10171490, EBI-717422;
CC -!- SUBCELLULAR LOCATION: Perikaryon {ECO:0000250|UniProtKB:Q8K2Q9}. Cell
CC projection, axon {ECO:0000250|UniProtKB:Q8K2Q9}. Cell projection,
CC growth cone {ECO:0000250|UniProtKB:Q8K2Q9}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q8K2Q9}. Cell projection, filopodium
CC {ECO:0000250|UniProtKB:A0MZ67}. Cell projection, lamellipodium
CC {ECO:0000250|UniProtKB:A0MZ67}. Note=Localizes in multiple growth cones
CC at neurite tips before the neuronal symmetry-breaking step. Accumulates
CC in growth cones of a single nascent axon in a neurite length-dependent
CC manner during the neuronal symmetry-breaking step; when absent from the
CC nascent axon's siblings, probably due to competitive transport,
CC prevents the formation of surplus axons. Transported anterogradely from
CC the soma to the axon growth cone in an actin and myosin-dependent
CC manner and passively diffuses back to the cell bodies. Colocalized with
CC L1CAM in close apposition with actin filaments in filopodia and
CC lamellipodia of axonal growth cones in hippocampal neurons. Exhibits
CC retrograde movements in filopodia and lamellopodia of axonal growth
CC cones. Colocalized with KIF20B along microtubules to the tip of the
CC growing cone in primary hippocampal neurons. Recruited to the growth
CC cone of developing axon in a KIF20B- and microtubule-dependent manner.
CC {ECO:0000250|UniProtKB:A0MZ67, ECO:0000250|UniProtKB:Q8K2Q9}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Name=1;
CC IsoId=A0MZ66-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A0MZ66-2; Sequence=VSP_027050, VSP_027051;
CC Name=3;
CC IsoId=A0MZ66-3; Sequence=VSP_027053;
CC Name=4;
CC IsoId=A0MZ66-4; Sequence=VSP_027052;
CC Name=5;
CC IsoId=A0MZ66-5; Sequence=VSP_036498;
CC Name=6;
CC IsoId=A0MZ66-6; Sequence=VSP_036499;
CC Name=7;
CC IsoId=A0MZ66-7; Sequence=VSP_036497;
CC Name=8;
CC IsoId=A0MZ66-8; Sequence=VSP_036498, VSP_027052;
CC -!- DOMAIN: The N-terminus region is necessary for interaction with actin
CC retrograde filament flow and accumulation in neuronal growth cones.
CC {ECO:0000250|UniProtKB:A0MZ67}.
CC -!- PTM: Phosphorylated on Ser-101 and Ser-249 by PAK1 through a CDC42- and
CC RAC1-dependent signaling pathway, which enhances its association with
CC F-actin retrograde flow in filopodia and lamellipodia of axonal growth
CC cones. Phosphorylation on Ser-101 and Ser-249 is increased by netrin-1.
CC {ECO:0000250|UniProtKB:A0MZ67}.
CC -!- SIMILARITY: Belongs to the shootin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH22348.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA92019.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAG53052.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAG53110.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; EF055487; ABK56022.1; -; mRNA.
DR EMBL; AK001984; BAA92019.1; ALT_INIT; mRNA.
DR EMBL; AK091381; BAG52345.1; -; mRNA.
DR EMBL; AK091578; BAG52384.1; -; mRNA.
DR EMBL; AK095419; BAG53052.1; ALT_INIT; mRNA.
DR EMBL; AK095703; BAG53109.1; -; mRNA.
DR EMBL; AK095709; BAG53110.1; ALT_INIT; mRNA.
DR EMBL; AK302705; BAH13785.1; -; mRNA.
DR EMBL; AK304865; BAG65603.1; -; mRNA.
DR EMBL; CR749417; CAH18259.1; -; mRNA.
DR EMBL; AC012308; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC023283; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL731557; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471066; EAW49434.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49438.1; -; Genomic_DNA.
DR EMBL; BC022348; AAH22348.1; ALT_INIT; mRNA.
DR EMBL; BC032303; AAH32303.1; -; mRNA.
DR EMBL; AB046818; BAB13424.1; -; mRNA.
DR CCDS; CCDS31293.1; -. [A0MZ66-2]
DR CCDS; CCDS44482.1; -. [A0MZ66-1]
DR CCDS; CCDS58097.1; -. [A0MZ66-8]
DR CCDS; CCDS73207.1; -. [A0MZ66-5]
DR CCDS; CCDS73208.1; -. [A0MZ66-4]
DR RefSeq; NP_001120683.1; NM_001127211.2. [A0MZ66-1]
DR RefSeq; NP_001245227.1; NM_001258298.1. [A0MZ66-5]
DR RefSeq; NP_001245228.1; NM_001258299.1. [A0MZ66-4]
DR RefSeq; NP_001245229.1; NM_001258300.1. [A0MZ66-8]
DR RefSeq; NP_060800.2; NM_018330.6. [A0MZ66-2]
DR RefSeq; XP_016871951.1; XM_017016462.1.
DR AlphaFoldDB; A0MZ66; -.
DR SMR; A0MZ66; -.
DR BioGRID; 121723; 83.
DR IntAct; A0MZ66; 30.
DR MINT; A0MZ66; -.
DR STRING; 9606.ENSP00000347532; -.
DR GlyGen; A0MZ66; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; A0MZ66; -.
DR PhosphoSitePlus; A0MZ66; -.
DR BioMuta; SHTN1; -.
DR EPD; A0MZ66; -.
DR jPOST; A0MZ66; -.
DR MassIVE; A0MZ66; -.
DR MaxQB; A0MZ66; -.
DR PaxDb; A0MZ66; -.
DR PeptideAtlas; A0MZ66; -.
DR PRIDE; A0MZ66; -.
DR ProteomicsDB; 45; -. [A0MZ66-1]
DR ProteomicsDB; 46; -. [A0MZ66-2]
DR ProteomicsDB; 47; -. [A0MZ66-3]
DR ProteomicsDB; 48; -. [A0MZ66-4]
DR ProteomicsDB; 49; -. [A0MZ66-5]
DR ProteomicsDB; 50; -. [A0MZ66-6]
DR ProteomicsDB; 51; -. [A0MZ66-7]
DR ProteomicsDB; 6909; -.
DR Antibodypedia; 46270; 44 antibodies from 15 providers.
DR DNASU; 57698; -.
DR Ensembl; ENST00000260777.14; ENSP00000260777.11; ENSG00000187164.20. [A0MZ66-5]
DR Ensembl; ENST00000355371.9; ENSP00000347532.4; ENSG00000187164.20. [A0MZ66-1]
DR Ensembl; ENST00000392901.10; ENSP00000376635.4; ENSG00000187164.20. [A0MZ66-8]
DR Ensembl; ENST00000392903.3; ENSP00000376636.3; ENSG00000187164.20. [A0MZ66-4]
DR Ensembl; ENST00000615301.4; ENSP00000480109.1; ENSG00000187164.20. [A0MZ66-2]
DR GeneID; 57698; -.
DR KEGG; hsa:57698; -.
DR MANE-Select; ENST00000355371.9; ENSP00000347532.4; NM_001127211.3; NP_001120683.1.
DR UCSC; uc001lcz.6; human. [A0MZ66-1]
DR CTD; 57698; -.
DR DisGeNET; 57698; -.
DR GeneCards; SHTN1; -.
DR HGNC; HGNC:29319; SHTN1.
DR HPA; ENSG00000187164; Tissue enriched (brain).
DR MIM; 611171; gene.
DR neXtProt; NX_A0MZ66; -.
DR OpenTargets; ENSG00000187164; -.
DR PharmGKB; PA134973737; -.
DR VEuPathDB; HostDB:ENSG00000187164; -.
DR eggNOG; ENOG502QVVT; Eukaryota.
DR GeneTree; ENSGT00510000048167; -.
DR HOGENOM; CLU_027649_1_1_1; -.
DR InParanoid; A0MZ66; -.
DR OMA; NLMDAAI; -.
DR OrthoDB; 744654at2759; -.
DR PhylomeDB; A0MZ66; -.
DR TreeFam; TF326250; -.
DR PathwayCommons; A0MZ66; -.
DR Reactome; R-HSA-437239; Recycling pathway of L1.
DR SignaLink; A0MZ66; -.
DR BioGRID-ORCS; 57698; 10 hits in 1076 CRISPR screens.
DR ChiTaRS; SHTN1; human.
DR GenomeRNAi; 57698; -.
DR Pharos; A0MZ66; Tbio.
DR PRO; PR:A0MZ66; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; A0MZ66; protein.
DR Bgee; ENSG00000187164; Expressed in medial globus pallidus and 192 other tissues.
DR Genevisible; A0MZ66; HS.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0044295; C:axonal growth cone; ISS:UniProtKB.
DR GO; GO:0031252; C:cell leading edge; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0030175; C:filopodium; ISS:UniProtKB.
DR GO; GO:0030426; C:growth cone; ISS:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0005874; C:microtubule; IEA:Ensembl.
DR GO; GO:0005875; C:microtubule associated complex; ISS:UniProtKB.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISS:UniProtKB.
DR GO; GO:0043204; C:perikaryon; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0019894; F:kinesin binding; IEA:Ensembl.
DR GO; GO:0061573; P:actin filament bundle retrograde transport; ISS:UniProtKB.
DR GO; GO:0007409; P:axonogenesis; ISS:UniProtKB.
DR GO; GO:0032488; P:Cdc42 protein signal transduction; ISS:UniProtKB.
DR GO; GO:0060327; P:cytoplasmic actin-based contraction involved in cell motility; ISS:UniProtKB.
DR GO; GO:0061163; P:endoplasmic reticulum polarization; ISS:UniProtKB.
DR GO; GO:0038007; P:netrin-activated signaling pathway; ISS:UniProtKB.
DR GO; GO:0048812; P:neuron projection morphogenesis; ISS:UniProtKB.
DR GO; GO:0045773; P:positive regulation of axon extension; ISS:UniProtKB.
DR GO; GO:2001224; P:positive regulation of neuron migration; IDA:UniProtKB.
DR GO; GO:0007265; P:Ras protein signal transduction; ISS:UniProtKB.
DR GO; GO:2000114; P:regulation of establishment of cell polarity; ISS:UniProtKB.
DR GO; GO:0006930; P:substrate-dependent cell migration, cell extension; ISS:UniProtKB.
DR InterPro; IPR024849; Shootin-1.
DR PANTHER; PTHR46606; PTHR46606; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell projection; Coiled coil; Cytoplasm;
KW Cytoskeleton; Developmental protein; Direct protein sequencing;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..631
FT /note="Shootin-1"
FT /id="PRO_0000295740"
FT REGION 343..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 7..353
FT /evidence="ECO:0000255"
FT COMPBIAS 350..371
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..422
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..468
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..489
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..511
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..624
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q8K2Q9"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K2Q9"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 101
FT /note="Phosphoserine; by PAK1"
FT /evidence="ECO:0000250|UniProtKB:A0MZ67"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 375
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 473
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 487
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 494
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 496
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 506
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 515
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 532
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 534
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 537
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..412
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036497"
FT VAR_SEQ 1..60
FT /note="Missing (in isoform 5 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036498"
FT VAR_SEQ 1..37
FT /note="MNSSDEEKQLQLITSLKEQAIGEYEDLRAENQKTKEK -> MPRILKQ (in
FT isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036499"
FT VAR_SEQ 454..456
FT /note="GTL -> ASQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10997877,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:17030985"
FT /id="VSP_027050"
FT VAR_SEQ 457..631
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10997877,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:17030985"
FT /id="VSP_027051"
FT VAR_SEQ 559..631
FT /note="Missing (in isoform 4 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_027052"
FT VAR_SEQ 623..631
FT /note="VRETDSSNC -> FFPFHFGFEGVLPLAGVTLSTKARDPK (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_027053"
FT CONFLICT 399
FT /note="T -> A (in Ref. 4; AC023283)"
FT /evidence="ECO:0000305"
FT CONFLICT 417
FT /note="I -> V (in Ref. 2; BAG52345)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 631 AA; 71640 MW; 826B88F18151228D CRC64;
MNSSDEEKQL QLITSLKEQA IGEYEDLRAE NQKTKEKCDK IRQERDEAVK KLEEFQKISH
MVIEEVNFMQ NHLEIEKTCR ESAEALATKL NKENKTLKRI SMLYMAKLGP DVITEEINID
DEDSTTDTDG AAETCVSVQC QKQIKELRDQ IVSVQEEKKI LAIELENLKS KLVEVIEEVN
KVKQEKTVLN SEVLEQRKVL EKCNRVSMLA VEEYEEMQVN LELEKDLRKK AESFAQEMFI
EQNKLKRQSH LLLQSSIPDQ QLLKALDENA KLTQQLEEER IQHQQKVKEL EEQLENETLH
KEIHNLKQQL ELLEEDKKEL ELKYQNSEEK ARNLKHSVDE LQKRVNQSEN SVPPPPPPPP
PLPPPPPNPI RSLMSMIRKR SHPSGSGAKK EKATQPETTE EVTDLKRQAV EEMMDRIKKG
VHLRPVNQTA RPKTKPESSK GCESAVDELK GILGTLNKST SSRSLKSLDP ENSETELERI
LRRRKVTAEA DSSSPTGILA TSESKSMPVL GSVSSVTKTA LNKKTLEAEF NSPSPPTPEP
GEGPRKLEGC TSSKVTFQPP SSIGCRKKYI DGEKQAEPVV VLDPVSTHEP QTKDQVAEKD
PTQHKEDEGE IQPENKEDSI ENVRETDSSN C
