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NBL1_HUMAN
ID   NBL1_HUMAN              Reviewed;         181 AA.
AC   P41271; A3KFI7; Q5TGZ2; Q5U0N4; Q96L68;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 2.
DT   03-AUG-2022, entry version 181.
DE   RecName: Full=Neuroblastoma suppressor of tumorigenicity 1;
DE   AltName: Full=DAN domain family member 1;
DE   AltName: Full=Protein N03;
DE   AltName: Full=Zinc finger protein DAN;
DE   Flags: Precursor;
GN   Name=NBL1; Synonyms=DAN, DAND1;
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).
RC   TISSUE=Lung;
RX   PubMed=8084583;
RA   Enomoto H., Ozaki T., Takahashi E., Nomura N., Tabata S., Takahashi H.,
RA   Ohnuma N., Tanabe M., Iwai J., Yoshida H., Matsunaga T., Sakiyama S.;
RT   "Identification of human DAN gene, mapping to the putative neuroblastoma
RT   tumor suppressor locus.";
RL   Oncogene 9:2785-2791(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RA   Ozaki T., Nakamura Y., Kondo K., Seki N., Ohira M., Nomura N., Ohki M.,
RA   Nakagawara A., Sakiyama S.;
RT   "The genomic structure of human DAN gene.";
RL   Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Wu J., Peng X., Yuan J., Qiang B.;
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Glial tumor, Prostate, Small intestine, and Synovium;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [6]
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   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Eye;
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   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-181 (ISOFORM 1).
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   PROTEIN SEQUENCE OF 17-37.
RC   TISSUE=Foreskin keratinocyte;
RX   PubMed=11594460; DOI=10.1023/a:1010902815953;
RA   Ahmed A., Kandola P., Ziada G., Parenteau N.;
RT   "Purification and partial amino acid sequence of proteins from human
RT   epidermal keratinocyte conditioned medium.";
RL   J. Protein Chem. 20:273-278(2001).
CC   -!- FUNCTION: Possible candidate as a tumor suppressor gene of
CC       neuroblastoma. May play an important role in preventing cells from
CC       entering the final stage (G1/S) of the transformation process.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- INTERACTION:
CC       P41271; P62166: NCS1; NbExp=3; IntAct=EBI-10208650, EBI-746987;
CC       P41271; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-10208650, EBI-741480;
CC       P41271; Q9UMX0-2: UBQLN1; NbExp=3; IntAct=EBI-10208650, EBI-10173939;
CC       P41271; Q8NF64-2: ZMIZ2; NbExp=3; IntAct=EBI-10208650, EBI-10182121;
CC       P41271-2; P05067: APP; NbExp=3; IntAct=EBI-12135485, EBI-77613;
CC       P41271-2; Q9UQM7: CAMK2A; NbExp=3; IntAct=EBI-12135485, EBI-1383687;
CC       P41271-2; P28329-3: CHAT; NbExp=3; IntAct=EBI-12135485, EBI-25837549;
CC       P41271-2; G5E9A7: DMWD; NbExp=3; IntAct=EBI-12135485, EBI-10976677;
CC       P41271-2; A0A0U1RQF7: DPEP2NB; NbExp=3; IntAct=EBI-12135485, EBI-18398199;
CC       P41271-2; P22607: FGFR3; NbExp=3; IntAct=EBI-12135485, EBI-348399;
CC       P41271-2; Q14957: GRIN2C; NbExp=3; IntAct=EBI-12135485, EBI-8285963;
CC       P41271-2; P37235: HPCAL1; NbExp=3; IntAct=EBI-12135485, EBI-749311;
CC       P41271-2; Q8IUC1: KRTAP11-1; NbExp=3; IntAct=EBI-12135485, EBI-1052037;
CC       P41271-2; Q96JA1-2: LRIG1; NbExp=3; IntAct=EBI-12135485, EBI-13067910;
CC       P41271-2; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-12135485, EBI-16439278;
CC       P41271-2; P52815: MRPL12; NbExp=3; IntAct=EBI-12135485, EBI-358272;
CC       P41271-2; P61601: NCALD; NbExp=3; IntAct=EBI-12135485, EBI-749635;
CC       P41271-2; Q9BZM2-2: PLA2G2F; NbExp=3; IntAct=EBI-12135485, EBI-12826629;
CC       P41271-2; P04271: S100B; NbExp=3; IntAct=EBI-12135485, EBI-458391;
CC       P41271-2; P34741: SDC2; NbExp=3; IntAct=EBI-12135485, EBI-1172957;
CC       P41271-2; P03973: SLPI; NbExp=3; IntAct=EBI-12135485, EBI-355293;
CC       P41271-2; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-12135485, EBI-5235340;
CC       P41271-2; P43405-2: SYK; NbExp=3; IntAct=EBI-12135485, EBI-25892332;
CC       P41271-2; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-12135485, EBI-741480;
CC       P41271-2; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-12135485, EBI-947187;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P41271-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P41271-2; Sequence=VSP_036438;
CC   -!- TISSUE SPECIFICITY: Most abundant in normal lung and meningioma.
CC   -!- SIMILARITY: Belongs to the DAN family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH12037.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAA05671.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAA92265.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAG36074.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; D28124; BAA05671.1; ALT_INIT; mRNA.
DR   EMBL; D89013; BAA92265.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AY049783; AAL15440.1; -; mRNA.
DR   EMBL; AK289456; BAF82145.1; -; mRNA.
DR   EMBL; AK292101; BAF84790.1; -; mRNA.
DR   EMBL; AK300872; BAG62517.1; -; mRNA.
DR   EMBL; AK313265; BAG36074.1; ALT_INIT; mRNA.
DR   EMBL; AL031727; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471134; EAW94894.1; -; Genomic_DNA.
DR   EMBL; CH471134; EAW94895.1; -; Genomic_DNA.
DR   EMBL; BC012037; AAH12037.1; ALT_INIT; mRNA.
DR   EMBL; BT019423; AAV38230.1; -; mRNA.
DR   CCDS; CCDS196.2; -. [P41271-1]
DR   CCDS; CCDS41278.1; -. [P41271-2]
DR   RefSeq; NP_001191013.1; NM_001204084.2. [P41271-1]
DR   RefSeq; NP_001191014.1; NM_001204085.1. [P41271-1]
DR   RefSeq; NP_001191017.1; NM_001204088.1.
DR   RefSeq; NP_001191018.1; NM_001204089.1. [P41271-1]
DR   RefSeq; NP_001265093.1; NM_001278164.1. [P41271-1]
DR   RefSeq; NP_001265094.1; NM_001278165.1. [P41271-1]
DR   RefSeq; NP_001265095.1; NM_001278166.1. [P41271-1]
DR   RefSeq; NP_005371.2; NM_005380.7. [P41271-1]
DR   RefSeq; NP_877421.2; NM_182744.3. [P41271-2]
DR   PDB; 4X1J; X-ray; 2.50 A; A/B=17-132.
DR   PDB; 4YU8; X-ray; 1.80 A; A=2-140.
DR   PDBsum; 4X1J; -.
DR   PDBsum; 4YU8; -.
DR   AlphaFoldDB; P41271; -.
DR   SMR; P41271; -.
DR   BioGRID; 110761; 15.
DR   BioGRID; 1529413; 32.
DR   IntAct; P41271; 23.
DR   STRING; 9606.ENSP00000289749; -.
DR   GlyConnect; 1549; 7 N-Linked glycans (1 site).
DR   GlyGen; P41271; 2 sites, 8 N-linked glycans (1 site), 1 O-linked glycan (1 site).
DR   iPTMnet; P41271; -.
DR   PhosphoSitePlus; P41271; -.
DR   BioMuta; NBL1; -.
DR   DMDM; 729293; -.
DR   jPOST; P41271; -.
DR   MassIVE; P41271; -.
DR   MaxQB; P41271; -.
DR   PaxDb; P41271; -.
DR   PeptideAtlas; P41271; -.
DR   PRIDE; P41271; -.
DR   ProteomicsDB; 55455; -. [P41271-1]
DR   ProteomicsDB; 55456; -. [P41271-2]
DR   Antibodypedia; 29695; 313 antibodies from 33 providers.
DR   DNASU; 4681; -.
DR   Ensembl; ENST00000289749.6; ENSP00000289749.2; ENSG00000158747.15. [P41271-2]
DR   Ensembl; ENST00000375136.8; ENSP00000364278.4; ENSG00000158747.15. [P41271-1]
DR   Ensembl; ENST00000548815.2; ENSP00000449007.2; ENSG00000158747.15. [P41271-1]
DR   Ensembl; ENST00000602662.1; ENSP00000473411.1; ENSG00000158747.15. [P41271-1]
DR   Ensembl; ENST00000618761.4; ENSP00000483061.1; ENSG00000158747.15. [P41271-1]
DR   Ensembl; ENST00000621723.4; ENSP00000478885.1; ENSG00000158747.15. [P41271-1]
DR   Ensembl; ENST00000622566.4; ENSP00000480391.1; ENSG00000158747.15. [P41271-1]
DR   GeneID; 100532736; -.
DR   GeneID; 4681; -.
DR   KEGG; hsa:100532736; -.
DR   KEGG; hsa:4681; -.
DR   MANE-Select; ENST00000375136.8; ENSP00000364278.4; NM_005380.8; NP_005371.2.
DR   UCSC; uc001bcj.3; human. [P41271-1]
DR   CTD; 100532736; -.
DR   CTD; 4681; -.
DR   DisGeNET; 100532736; -.
DR   DisGeNET; 4681; -.
DR   GeneCards; NBL1; -.
DR   HGNC; HGNC:7650; NBL1.
DR   HPA; ENSG00000158747; Low tissue specificity.
DR   MIM; 600613; gene.
DR   neXtProt; NX_P41271; -.
DR   OpenTargets; ENSG00000158747; -.
DR   PharmGKB; PA31456; -.
DR   VEuPathDB; HostDB:ENSG00000158747; -.
DR   eggNOG; ENOG502RYP0; Eukaryota.
DR   GeneTree; ENSGT00940000154209; -.
DR   InParanoid; P41271; -.
DR   OMA; GLNVYVQ; -.
DR   OrthoDB; 1517793at2759; -.
DR   TreeFam; TF106445; -.
DR   PathwayCommons; P41271; -.
DR   SignaLink; P41271; -.
DR   BioGRID-ORCS; 100532736; 15 hits in 186 CRISPR screens.
DR   BioGRID-ORCS; 4681; 10 hits in 1003 CRISPR screens.
DR   Pharos; P41271; Tbio.
DR   PRO; PR:P41271; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; P41271; protein.
DR   Bgee; ENSG00000158747; Expressed in endocervix and 209 other tissues.
DR   ExpressionAtlas; P41271; baseline and differential.
DR   Genevisible; P41271; HS.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0036122; F:BMP binding; ISS:BHF-UCL.
DR   GO; GO:0042802; F:identical protein binding; IMP:UniProtKB.
DR   GO; GO:0016015; F:morphogen activity; ISS:BHF-UCL.
DR   GO; GO:0048018; F:receptor ligand activity; IBA:GO_Central.
DR   GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR   GO; GO:0048263; P:determination of dorsal identity; ISS:BHF-UCL.
DR   GO; GO:0030514; P:negative regulation of BMP signaling pathway; IDA:UniProtKB.
DR   GO; GO:0090027; P:negative regulation of monocyte chemotaxis; ISS:BHF-UCL.
DR   GO; GO:0007399; P:nervous system development; ISS:BHF-UCL.
DR   GO; GO:0048812; P:neuron projection morphogenesis; ISS:BHF-UCL.
DR   GO; GO:0045666; P:positive regulation of neuron differentiation; ISS:BHF-UCL.
DR   GO; GO:0038098; P:sequestering of BMP from receptor via BMP binding; IDA:UniProtKB.
DR   GO; GO:0035582; P:sequestering of BMP in extracellular matrix; ISS:BHF-UCL.
DR   Gene3D; 2.10.90.10; -; 1.
DR   InterPro; IPR006207; Cys_knot_C.
DR   InterPro; IPR029034; Cystine-knot_cytokine.
DR   InterPro; IPR004133; DAN.
DR   InterPro; IPR016728; Neuroblast_suppress_tumour_1.
DR   Pfam; PF03045; DAN; 1.
DR   PIRSF; PIRSF018557; DAN_sub; 1.
DR   SMART; SM00041; CT; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Direct protein sequencing;
KW   Disulfide bond; Reference proteome; Secreted; Signal; Tumor suppressor.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000269|PubMed:11594460"
FT   CHAIN           17..181
FT                   /note="Neuroblastoma suppressor of tumorigenicity 1"
FT                   /id="PRO_0000006722"
FT   DOMAIN          35..124
FT                   /note="CTCK"
FT   REGION          132..181
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        147..168
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        35..85
FT                   /evidence="ECO:0000250"
FT   DISULFID        49..99
FT                   /evidence="ECO:0000250"
FT   DISULFID        59..118
FT                   /evidence="ECO:0000250"
FT   DISULFID        63..120
FT                   /evidence="ECO:0000250"
FT   DISULFID        82..123
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1
FT                   /note="M -> MPGNLMSQTSRAVSIWKFPAKLGKTHGHRALEATGM (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_036438"
FT   STRAND          34..44
FT                   /evidence="ECO:0007829|PDB:4YU8"
FT   STRAND          47..50
FT                   /evidence="ECO:0007829|PDB:4X1J"
FT   STRAND          52..62
FT                   /evidence="ECO:0007829|PDB:4YU8"
FT   STRAND          85..98
FT                   /evidence="ECO:0007829|PDB:4YU8"
FT   STRAND          103..105
FT                   /evidence="ECO:0007829|PDB:4YU8"
FT   STRAND          107..120
FT                   /evidence="ECO:0007829|PDB:4YU8"
SQ   SEQUENCE   181 AA;  19408 MW;  AE9E3264EF38DAD7 CRC64;
     MMLRVLVGAV LPAMLLAAPP PINKLALFPD KSAWCEAKNI TQIVGHSGCE AKSIQNRACL
     GQCFSYSVPN TFPQSTESLV HCDSCMPAQS MWEIVTLECP GHEEVPRVDK LVEKILHCSC
     QACGKEPSHE GLSVYVQGED GPGSQPGTHP HPHPHPHPGG QTPEPEDPPG APHTEEEGAE
     D
 
 
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