CD34_HUMAN
ID CD34_HUMAN Reviewed; 385 AA.
AC P28906; A8K664; Q15970; Q15971; Q5JTA3; Q5JTA4; Q9UJB1;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Hematopoietic progenitor cell antigen CD34;
DE AltName: CD_antigen=CD34;
DE Flags: Precursor;
GN Name=CD34;
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 CD34-F), AND PROTEIN SEQUENCE OF 32-43.
RC TISSUE=Bone marrow;
RX PubMed=1370171;
RA Simmons D.L., Satterthwaite A.B., Tenen D.G., Seed B.;
RT "Molecular cloning of a cDNA encoding CD34, a sialomucin of human
RT hematopoietic stem cells.";
RL J. Immunol. 148:267-271(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM CD34-F).
RX PubMed=1374051; DOI=10.1016/0888-7543(92)90310-o;
RA Satterthwaite A.B., Burn T.C., le Beau M.M., Tenen D.G.;
RT "Structure of the gene encoding CD34, a human hematopoietic stem cell
RT antigen.";
RL Genomics 12:788-794(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS CD34-F AND CD34-T).
RC TISSUE=Megakaryoblast;
RX PubMed=7678811;
RA Nakamura Y., Komano H., Nakauchi H.;
RT "Two alternative forms of cDNA encoding CD34.";
RL Exp. Hematol. 21:236-242(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CD34-F).
RC TISSUE=Heart;
RA Freund D., Wiebe G.J., Ehninger G., Corbeil D.;
RT "Sequence analysis of the human CD34 antigen.";
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM CD34-F).
RC TISSUE=Placenta;
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 [6]
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 [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM CD34-F).
RC TISSUE=Skin;
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 [9]
RP PROTEIN SEQUENCE OF 32-47 AND 175-191, AND CHARACTERIZATION.
RX PubMed=2462139;
RA Sutherland D.R., Watt S.M., Dowden G., Karhi K., Baker M.A., Greaves M.F.,
RA Smart J.E.;
RT "Structural and partial amino acid sequence analysis of the human
RT hemopoietic progenitor cell antigen CD34.";
RL Leukemia 2:793-803(1988).
RN [10]
RP PHOSPHORYLATION BY PKC.
RX PubMed=1694174; DOI=10.1016/s0021-9258(19)38556-4;
RA Fackler M.J., Civin C.I., Sutherland D.R., Baker M.A., May W.S.;
RT "Activated protein kinase C directly phosphorylates the CD34 antigen on
RT hematopoietic cells.";
RL J. Biol. Chem. 265:11056-11061(1990).
CC -!- FUNCTION: Possible adhesion molecule with a role in early hematopoiesis
CC by mediating the attachment of stem cells to the bone marrow
CC extracellular matrix or directly to stromal cells. Could act as a
CC scaffold for the attachment of lineage specific glycans, allowing stem
CC cells to bind to lectins expressed by stromal cells or other marrow
CC components. Presents carbohydrate ligands to selectins.
CC -!- INTERACTION:
CC P28906; O95994: AGR2; NbExp=3; IntAct=EBI-2836676, EBI-712648;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Both isoforms are expressed on the cell surface.
CC CD34-T/CD34-F ratio increases with cell differentiation.;
CC Name=CD34-F;
CC IsoId=P28906-1; Sequence=Displayed;
CC Name=CD34-T;
CC IsoId=P28906-2; Sequence=VSP_004159, VSP_004160;
CC -!- TISSUE SPECIFICITY: Selectively expressed on hematopoietic progenitor
CC cells and the small vessel endothelium of a variety of tissues.
CC -!- DEVELOPMENTAL STAGE: On early hematopoietic progenitor cells.
CC -!- PTM: Highly glycosylated.
CC -!- PTM: Phosphorylated on serine residues by PKC.
CC {ECO:0000269|PubMed:1694174}.
CC -!- SIMILARITY: Belongs to the CD34 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA03181.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Wikipedia; Note=CD34 entry;
CC URL="https://en.wikipedia.org/wiki/CD34";
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DR EMBL; M81104; AAA03181.1; ALT_INIT; mRNA.
DR EMBL; M81945; AAA03659.1; -; Genomic_DNA.
DR EMBL; M81938; AAA03659.1; JOINED; Genomic_DNA.
DR EMBL; M81939; AAA03659.1; JOINED; Genomic_DNA.
DR EMBL; M81940; AAA03659.1; JOINED; Genomic_DNA.
DR EMBL; M81941; AAA03659.1; JOINED; Genomic_DNA.
DR EMBL; M81942; AAA03659.1; JOINED; Genomic_DNA.
DR EMBL; M81943; AAA03659.1; JOINED; Genomic_DNA.
DR EMBL; M81944; AAA03659.1; JOINED; Genomic_DNA.
DR EMBL; S53910; AAB25222.1; -; mRNA.
DR EMBL; S53911; AAB25223.1; -; mRNA.
DR EMBL; AF523361; AAM82157.1; -; mRNA.
DR EMBL; AK291529; BAF84218.1; -; mRNA.
DR EMBL; AL356275; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471100; EAW93459.1; -; Genomic_DNA.
DR EMBL; BC039146; AAH39146.2; -; mRNA.
DR CCDS; CCDS31011.1; -. [P28906-1]
DR CCDS; CCDS31012.1; -. [P28906-2]
DR PIR; A38078; A38078.
DR PIR; I67604; I67604.
DR RefSeq; NP_001020280.1; NM_001025109.1. [P28906-1]
DR RefSeq; NP_001764.1; NM_001773.2. [P28906-2]
DR AlphaFoldDB; P28906; -.
DR BioGRID; 107385; 2.
DR IntAct; P28906; 2.
DR STRING; 9606.ENSP00000310036; -.
DR GlyConnect; 1305; 3 N-Linked glycans (1 site).
DR GlyGen; P28906; 10 sites, 3 N-linked glycans (1 site), 2 O-linked glycans (1 site).
DR iPTMnet; P28906; -.
DR PhosphoSitePlus; P28906; -.
DR BioMuta; CD34; -.
DR DMDM; 3183511; -.
DR EPD; P28906; -.
DR jPOST; P28906; -.
DR MassIVE; P28906; -.
DR MaxQB; P28906; -.
DR PaxDb; P28906; -.
DR PeptideAtlas; P28906; -.
DR PRIDE; P28906; -.
DR ProteomicsDB; 54505; -. [P28906-1]
DR ProteomicsDB; 54506; -. [P28906-2]
DR ABCD; P28906; 7 sequenced antibodies.
DR Antibodypedia; 3498; 3264 antibodies from 61 providers.
DR DNASU; 947; -.
DR Ensembl; ENST00000310833.12; ENSP00000310036.7; ENSG00000174059.17. [P28906-1]
DR Ensembl; ENST00000356522.4; ENSP00000348916.4; ENSG00000174059.17. [P28906-2]
DR GeneID; 947; -.
DR KEGG; hsa:947; -.
DR MANE-Select; ENST00000310833.12; ENSP00000310036.7; NM_001025109.2; NP_001020280.1.
DR UCSC; uc001hgw.2; human. [P28906-1]
DR CTD; 947; -.
DR DisGeNET; 947; -.
DR GeneCards; CD34; -.
DR HGNC; HGNC:1662; CD34.
DR HPA; ENSG00000174059; Low tissue specificity.
DR MIM; 142230; gene.
DR neXtProt; NX_P28906; -.
DR OpenTargets; ENSG00000174059; -.
DR PharmGKB; PA26211; -.
DR VEuPathDB; HostDB:ENSG00000174059; -.
DR eggNOG; ENOG502RYP9; Eukaryota.
DR GeneTree; ENSGT00390000008414; -.
DR HOGENOM; CLU_060339_0_0_1; -.
DR InParanoid; P28906; -.
DR OMA; GEIKCAG; -.
DR OrthoDB; 1303808at2759; -.
DR PhylomeDB; P28906; -.
DR TreeFam; TF335795; -.
DR PathwayCommons; P28906; -.
DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell. [P28906-1]
DR SignaLink; P28906; -.
DR SIGNOR; P28906; -.
DR BioGRID-ORCS; 947; 18 hits in 1073 CRISPR screens.
DR ChiTaRS; CD34; human.
DR GeneWiki; CD34; -.
DR GenomeRNAi; 947; -.
DR Pharos; P28906; Tbio.
DR PRO; PR:P28906; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P28906; protein.
DR Bgee; ENSG00000174059; Expressed in apex of heart and 144 other tissues.
DR ExpressionAtlas; P28906; baseline and differential.
DR Genevisible; P28906; HS.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0009925; C:basal plasma membrane; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0036053; C:glomerular endothelium fenestra; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:UniProtKB.
DR GO; GO:0045171; C:intercellular bridge; IDA:UniProtKB.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; IDA:HGNC-UCL.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0043199; F:sulfate binding; IEA:Ensembl.
DR GO; GO:0048870; P:cell motility; IEP:UniProtKB.
DR GO; GO:0098609; P:cell-cell adhesion; IDA:HGNC-UCL.
DR GO; GO:0007160; P:cell-matrix adhesion; IBA:GO_Central.
DR GO; GO:0001935; P:endothelial cell proliferation; IDA:UniProtKB.
DR GO; GO:0003158; P:endothelium development; IEP:UniProtKB.
DR GO; GO:0071971; P:extracellular exosome assembly; IDA:UniProtKB.
DR GO; GO:0072011; P:glomerular endothelium development; IEP:UniProtKB.
DR GO; GO:0003094; P:glomerular filtration; IEP:UniProtKB.
DR GO; GO:0071425; P:hematopoietic stem cell proliferation; IMP:UniProtKB.
DR GO; GO:0030097; P:hemopoiesis; IMP:UniProtKB.
DR GO; GO:0050900; P:leukocyte migration; ISS:HGNC-UCL.
DR GO; GO:0035759; P:mesangial cell-matrix adhesion; ISS:UniProtKB.
DR GO; GO:0072254; P:metanephric glomerular mesangial cell differentiation; IEP:UniProtKB.
DR GO; GO:0030195; P:negative regulation of blood coagulation; IDA:UniProtKB.
DR GO; GO:1900035; P:negative regulation of cellular response to heat; IDA:UniProtKB.
DR GO; GO:1900038; P:negative regulation of cellular response to hypoxia; IDA:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0032703; P:negative regulation of interleukin-2 production; IMP:UniProtKB.
DR GO; GO:1901215; P:negative regulation of neuron death; IDA:UniProtKB.
DR GO; GO:0045019; P:negative regulation of nitric oxide biosynthetic process; IDA:UniProtKB.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IDA:UniProtKB.
DR GO; GO:0038001; P:paracrine signaling; IDA:UniProtKB.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IDA:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IEP:UniProtKB.
DR GO; GO:1900168; P:positive regulation of glial cell-derived neurotrophic factor production; IDA:UniProtKB.
DR GO; GO:0071657; P:positive regulation of granulocyte colony-stimulating factor production; IDA:UniProtKB.
DR GO; GO:0032733; P:positive regulation of interleukin-10 production; IDA:UniProtKB.
DR GO; GO:0042482; P:positive regulation of odontogenesis; IDA:UniProtKB.
DR GO; GO:0071636; P:positive regulation of transforming growth factor beta production; IDA:UniProtKB.
DR GO; GO:2001214; P:positive regulation of vasculogenesis; IDA:UniProtKB.
DR GO; GO:0008217; P:regulation of blood pressure; IDA:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IEP:UniProtKB.
DR GO; GO:0072089; P:stem cell proliferation; IEP:UniProtKB.
DR GO; GO:0001894; P:tissue homeostasis; IDA:UniProtKB.
DR GO; GO:0060290; P:transdifferentiation; IEP:UniProtKB.
DR GO; GO:0061042; P:vascular wound healing; IEP:UniProtKB.
DR InterPro; IPR008083; CD34.
DR InterPro; IPR013836; CD34/Podocalyxin.
DR PANTHER; PTHR16677; PTHR16677; 1.
DR Pfam; PF06365; CD34_antigen; 1.
DR PRINTS; PR01700; CD34ANTIGEN.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Direct protein sequencing;
KW Glycoprotein; Membrane; Phosphoprotein; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..31
FT /evidence="ECO:0000269|PubMed:1370171,
FT ECO:0000269|PubMed:2462139"
FT CHAIN 32..385
FT /note="Hematopoietic progenitor cell antigen CD34"
FT /id="PRO_0000020900"
FT TOPO_DOM 32..290
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 291..311
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 312..385
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 127..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 321..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 329
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q64314"
FT MOD_RES 339
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q64314"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64314"
FT CARBOHYD 36
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 325..328
FT /note="GEDP -> ELEP (in isoform CD34-T)"
FT /evidence="ECO:0000303|PubMed:7678811"
FT /id="VSP_004159"
FT VAR_SEQ 329..385
FT /note="Missing (in isoform CD34-T)"
FT /evidence="ECO:0000303|PubMed:7678811"
FT /id="VSP_004160"
FT VARIANT 367
FT /note="A -> S (in dbSNP:rs28362497)"
FT /id="VAR_050774"
FT CONFLICT 187
FT /note="Q -> E (in Ref. 9; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 325..327
FT /note="GED -> ELE (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 361
FT /note="E -> K (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 385 AA; 40716 MW; BC581A8FCFFE2BB3 CRC64;
MLVRRGARAG PRMPRGWTAL CLLSLLPSGF MSLDNNGTAT PELPTQGTFS NVSTNVSYQE
TTTPSTLGST SLHPVSQHGN EATTNITETT VKFTSTSVIT SVYGNTNSSV QSQTSVISTV
FTTPANVSTP ETTLKPSLSP GNVSDLSTTS TSLATSPTKP YTSSSPILSD IKAEIKCSGI
REVKLTQGIC LEQNKTSSCA EFKKDRGEGL ARVLCGEEQA DADAGAQVCS LLLAQSEVRP
QCLLLVLANR TEISSKLQLM KKHQSDLKKL GILDFTEQDV ASHQSYSQKT LIALVTSGAL
LAVLGITGYF LMNRRSWSPT GERLGEDPYY TENGGGQGYS SGPGTSPEAQ GKASVNRGAQ
ENGTGQATSR NGHSARQHVV ADTEL
