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CB39L_HUMAN
ID   CB39L_HUMAN             Reviewed;         337 AA.
AC   Q9H9S4; Q5TAW6; Q6WG71; Q96FG1; Q9BZ33;
DT   14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 3.
DT   03-AUG-2022, entry version 167.
DE   RecName: Full=Calcium-binding protein 39-like;
DE   AltName: Full=Antigen MLAA-34;
DE   AltName: Full=MO25beta;
DE   AltName: Full=Mo25-like protein;
GN   Name=CAB39L;
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].
RC   TISSUE=Monocytic leukemia;
RX   PubMed=15755502; DOI=10.1016/j.leukres.2004.09.013;
RA   Chen G., Zhang W.G., Cao X.M., Li F.Y., Liu X.P., Yao L.B.;
RT   "Serological identification of immunogenic antigens in acute monocytic
RT   leukemia.";
RL   Leuk. Res. 29:503-509(2005).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Placenta;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 7-337.
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   [5]
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).
CC   -!- FUNCTION: Component of a complex that binds and activates STK11/LKB1.
CC       In the complex, required to stabilize the interaction between
CC       CAB39/MO25 (CAB39/MO25alpha or CAB39L/MO25beta) and STK11/LKB1 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of a trimeric complex composed of STK11/LKB1, STRAD
CC       (STRADA or STRADB) and CAB39/MO25 (CAB39/MO25alpha or CAB39L/MO25beta):
CC       the complex tethers STK11/LKB1 in the cytoplasm and stimulates its
CC       catalytic activity. {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q9H9S4; P20591: MX1; NbExp=3; IntAct=EBI-1047244, EBI-929476;
CC       Q9H9S4; Q9UQR0: SCML2; NbExp=3; IntAct=EBI-1047244, EBI-2513111;
CC       Q9H9S4; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-1047244, EBI-5235340;
CC   -!- MISCELLANEOUS: Found in serum of 50% of patients with acute monocytic
CC       leukemia.
CC   -!- SIMILARITY: Belongs to the Mo25 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB14147.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AY288977; AAQ93064.2; -; mRNA.
DR   EMBL; AL136218; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL138875; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC010993; AAH10993.2; -; mRNA.
DR   EMBL; AK022639; BAB14147.1; ALT_INIT; mRNA.
DR   CCDS; CCDS9416.2; -.
DR   RefSeq; NP_001073138.1; NM_001079670.2.
DR   RefSeq; NP_001274266.1; NM_001287337.1.
DR   RefSeq; NP_001274267.1; NM_001287338.1.
DR   RefSeq; NP_001274268.1; NM_001287339.1.
DR   RefSeq; NP_112187.2; NM_030925.3.
DR   RefSeq; XP_011533556.1; XM_011535254.2.
DR   RefSeq; XP_011533557.1; XM_011535255.2.
DR   RefSeq; XP_011533558.1; XM_011535256.2.
DR   RefSeq; XP_016876274.1; XM_017020785.1.
DR   RefSeq; XP_016876275.1; XM_017020786.1.
DR   RefSeq; XP_016876276.1; XM_017020787.1.
DR   RefSeq; XP_016876277.1; XM_017020788.1.
DR   PDB; 3ZHP; X-ray; 2.90 A; A/B=5-337.
DR   PDBsum; 3ZHP; -.
DR   AlphaFoldDB; Q9H9S4; -.
DR   SMR; Q9H9S4; -.
DR   BioGRID; 123552; 32.
DR   ComplexPortal; CPX-2431; LKB1-STRAD-MO25 serine/threonine protein kinase complex, CAB39L-STRADA variant.
DR   ComplexPortal; CPX-2869; LKB1-STRAD-MO25 serine/threonine protein kinase complex, CAB39L-STRADB variant.
DR   IntAct; Q9H9S4; 7.
DR   MINT; Q9H9S4; -.
DR   STRING; 9606.ENSP00000479669; -.
DR   iPTMnet; Q9H9S4; -.
DR   PhosphoSitePlus; Q9H9S4; -.
DR   SwissPalm; Q9H9S4; -.
DR   BioMuta; CAB39L; -.
DR   DMDM; 51338824; -.
DR   EPD; Q9H9S4; -.
DR   jPOST; Q9H9S4; -.
DR   MassIVE; Q9H9S4; -.
DR   MaxQB; Q9H9S4; -.
DR   PaxDb; Q9H9S4; -.
DR   PeptideAtlas; Q9H9S4; -.
DR   PRIDE; Q9H9S4; -.
DR   ProteomicsDB; 81359; -.
DR   Antibodypedia; 23903; 192 antibodies from 30 providers.
DR   DNASU; 81617; -.
DR   Ensembl; ENST00000347776.9; ENSP00000261669.7; ENSG00000102547.19.
DR   Ensembl; ENST00000355854.8; ENSP00000348113.4; ENSG00000102547.19.
DR   Ensembl; ENST00000409308.6; ENSP00000386375.1; ENSG00000102547.19.
DR   Ensembl; ENST00000410043.5; ENSP00000386328.1; ENSG00000102547.19.
DR   Ensembl; ENST00000610540.4; ENSP00000479669.1; ENSG00000102547.19.
DR   GeneID; 81617; -.
DR   KEGG; hsa:81617; -.
DR   MANE-Select; ENST00000409308.6; ENSP00000386375.1; NM_001079670.3; NP_001073138.1.
DR   UCSC; uc001vcw.5; human.
DR   CTD; 81617; -.
DR   DisGeNET; 81617; -.
DR   GeneCards; CAB39L; -.
DR   HGNC; HGNC:20290; CAB39L.
DR   HPA; ENSG00000102547; Low tissue specificity.
DR   MIM; 612175; gene.
DR   neXtProt; NX_Q9H9S4; -.
DR   OpenTargets; ENSG00000102547; -.
DR   PharmGKB; PA134913801; -.
DR   VEuPathDB; HostDB:ENSG00000102547; -.
DR   eggNOG; KOG1566; Eukaryota.
DR   GeneTree; ENSGT00390000004360; -.
DR   InParanoid; Q9H9S4; -.
DR   OMA; NFAVMTK; -.
DR   OrthoDB; 865327at2759; -.
DR   PhylomeDB; Q9H9S4; -.
DR   TreeFam; TF314910; -.
DR   PathwayCommons; Q9H9S4; -.
DR   Reactome; R-HSA-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
DR   SignaLink; Q9H9S4; -.
DR   BioGRID-ORCS; 81617; 8 hits in 1028 CRISPR screens.
DR   ChiTaRS; CAB39L; human.
DR   GeneWiki; CAB39L; -.
DR   GenomeRNAi; 81617; -.
DR   Pharos; Q9H9S4; Tbio.
DR   PRO; PR:Q9H9S4; -.
DR   Proteomes; UP000005640; Chromosome 13.
DR   RNAct; Q9H9S4; protein.
DR   Bgee; ENSG00000102547; Expressed in decidua and 178 other tissues.
DR   ExpressionAtlas; Q9H9S4; baseline and differential.
DR   Genevisible; Q9H9S4; HS.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0043539; F:protein serine/threonine kinase activator activity; IBA:GO_Central.
DR   GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR   Gene3D; 1.25.10.10; -; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR013878; Mo25.
DR   PANTHER; PTHR10182; PTHR10182; 1.
DR   Pfam; PF08569; Mo25; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Reference proteome.
FT   CHAIN           1..337
FT                   /note="Calcium-binding protein 39-like"
FT                   /id="PRO_0000209826"
FT   CONFLICT        93
FT                   /note="G -> E (in Ref. 3; AAH10993)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        156
FT                   /note="A -> V (in Ref. 4; BAB14147)"
FT                   /evidence="ECO:0000305"
FT   HELIX           16..29
FT                   /evidence="ECO:0007829|PDB:3ZHP"
FT   HELIX           33..36
FT                   /evidence="ECO:0007829|PDB:3ZHP"
FT   HELIX           38..53
FT                   /evidence="ECO:0007829|PDB:3ZHP"
FT   HELIX           66..76
FT                   /evidence="ECO:0007829|PDB:3ZHP"
FT   HELIX           78..84
FT                   /evidence="ECO:0007829|PDB:3ZHP"
FT   HELIX           91..105
FT                   /evidence="ECO:0007829|PDB:3ZHP"
FT   HELIX           114..121
FT                   /evidence="ECO:0007829|PDB:3ZHP"
FT   HELIX           124..131
FT                   /evidence="ECO:0007829|PDB:3ZHP"
FT   HELIX           132..134
FT                   /evidence="ECO:0007829|PDB:3ZHP"
FT   TURN            136..138
FT                   /evidence="ECO:0007829|PDB:3ZHP"
FT   HELIX           139..149
FT                   /evidence="ECO:0007829|PDB:3ZHP"
FT   HELIX           153..160
FT                   /evidence="ECO:0007829|PDB:3ZHP"
FT   HELIX           163..167
FT                   /evidence="ECO:0007829|PDB:3ZHP"
FT   HELIX           168..171
FT                   /evidence="ECO:0007829|PDB:3ZHP"
FT   HELIX           177..192
FT                   /evidence="ECO:0007829|PDB:3ZHP"
FT   HELIX           195..204
FT                   /evidence="ECO:0007829|PDB:3ZHP"
FT   HELIX           206..217
FT                   /evidence="ECO:0007829|PDB:3ZHP"
FT   HELIX           222..237
FT                   /evidence="ECO:0007829|PDB:3ZHP"
FT   HELIX           239..241
FT                   /evidence="ECO:0007829|PDB:3ZHP"
FT   HELIX           242..248
FT                   /evidence="ECO:0007829|PDB:3ZHP"
FT   HELIX           252..261
FT                   /evidence="ECO:0007829|PDB:3ZHP"
FT   HELIX           267..282
FT                   /evidence="ECO:0007829|PDB:3ZHP"
FT   HELIX           288..296
FT                   /evidence="ECO:0007829|PDB:3ZHP"
FT   HELIX           298..307
FT                   /evidence="ECO:0007829|PDB:3ZHP"
FT   TURN            308..311
FT                   /evidence="ECO:0007829|PDB:3ZHP"
FT   HELIX           316..330
FT                   /evidence="ECO:0007829|PDB:3ZHP"
SQ   SEQUENCE   337 AA;  39088 MW;  5C6C7A83B9B4CA2D CRC64;
     MKKMPLFSKS HKNPAEIVKI LKDNLAILEK QDKKTDKASE EVSKSLQAMK EILCGTNEKE
     PPTEAVAQLA QELYSSGLLV TLIADLQLID FEGKKDVTQI FNNILRRQIG TRSPTVEYIS
     AHPHILFMLL KGYEAPQIAL RCGIMLRECI RHEPLAKIIL FSNQFRDFFK YVELSTFDIA
     SDAFATFKDL LTRHKVLVAD FLEQNYDTIF EDYEKLLQSE NYVTKRQSLK LLGELILDRH
     NFAIMTKYIS KPENLKLMMN LLRDKSPNIQ FEAFHVFKVF VASPHKTQPI VEILLKNQPK
     LIEFLSSFQK ERTDDEQFAD EKNYLIKQIR DLKKTAP
 
 
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