HEMGN_RAT
ID HEMGN_RAT Reviewed; 514 AA.
AC Q6AZ54; Q9ER23;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Hemogen;
DE AltName: Full=Hemopoietic gene protein;
DE AltName: Full=Protein RP59;
GN Name=Hemgn; Synonyms=Rp59;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Bone marrow;
RX PubMed=11161722; DOI=10.1006/excr.2000.5114;
RA Wurtz T., Krueger A., Christersson C., Lundmark C.;
RT "A new protein expressed in bone marrow cells and osteoblasts with
RT implication in osteoblast recruitment.";
RL Exp. Cell Res. 263:236-242(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [3]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=11891990; DOI=10.1002/dvdy.10067;
RA Krueger A., Ellerstroem C., Lundmark C., Christersson C., Wurtz T.;
RT "RP59, a marker for osteoblast recruitment, is also detected in primitive
RT mesenchymal cells, erythroid cells, and megakaryocytes.";
RL Dev. Dyn. 223:414-418(2002).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=15726423; DOI=10.1007/s00441-004-1043-y;
RA Krueger A., Somogyi E., Christersson C., Lundmark C., Hultenby K.,
RA Wurtz T.;
RT "Rat enamel contains RP59: a new context for a protein from osteogenic and
RT haematopoietic precursor cells.";
RL Cell Tissue Res. 320:141-148(2005).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90; SER-179; SER-207;
RP SER-221; SER-415 AND SER-422, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Regulates the proliferation and differentiation of
CC hematopoietic cells. Overexpression block the TPA-induced
CC megakaryocytic differentiation in the K562 cell model. May also prevent
CC cell apoptosis through the activation of the nuclear factor-kappa B
CC (NF-kB) (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed by bone marrow cells and osteoblasts.
CC Also expressed by ameloblasts in tooth enamel (at protein level).
CC Expressed in enamel organ, ameloblasts, spleen, bone marrow cells and
CC osteoblasts. {ECO:0000269|PubMed:11161722, ECO:0000269|PubMed:11891990,
CC ECO:0000269|PubMed:15726423}.
CC -!- DEVELOPMENTAL STAGE: At 9 dpc expressed in extraembryonic mesodermal
CC layers with its prospective blood islands. Expressed in blood islands
CC at day 12 dpc. Expressed by the intraembryonic primary ectoderm
CC including the primitive streak at day 9 dpc. Expressed in the fetal
CC liver and in circulating cells at 17 dpc, the liver expression
CC disappear around birth (at protein level).
CC {ECO:0000269|PubMed:11891990}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC16090.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ302650; CAC16090.1; ALT_SEQ; mRNA.
DR EMBL; BC078739; AAH78739.1; -; mRNA.
DR RefSeq; NP_579828.1; NM_133294.1.
DR RefSeq; XP_008761915.1; XM_008763693.2.
DR RefSeq; XP_008761916.1; XM_008763694.2.
DR RefSeq; XP_017448603.1; XM_017593114.1.
DR AlphaFoldDB; Q6AZ54; -.
DR IntAct; Q6AZ54; 1.
DR STRING; 10116.ENSRNOP00000042341; -.
DR iPTMnet; Q6AZ54; -.
DR PhosphoSitePlus; Q6AZ54; -.
DR PaxDb; Q6AZ54; -.
DR GeneID; 113882; -.
DR KEGG; rno:113882; -.
DR UCSC; RGD:621569; rat.
DR CTD; 55363; -.
DR RGD; 621569; Hemgn.
DR VEuPathDB; HostDB:ENSRNOG00000009436; -.
DR eggNOG; ENOG502SBFR; Eukaryota.
DR HOGENOM; CLU_569802_0_0_1; -.
DR InParanoid; Q6AZ54; -.
DR OMA; EIHQETP; -.
DR OrthoDB; 801077at2759; -.
DR PhylomeDB; Q6AZ54; -.
DR TreeFam; TF338654; -.
DR PRO; PR:Q6AZ54; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000009436; Expressed in testis and 10 other tissues.
DR GO; GO:0005654; C:nucleoplasm; ISO:RGD.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0045667; P:regulation of osteoblast differentiation; IDA:RGD.
DR InterPro; IPR033272; Hemogen.
DR PANTHER; PTHR15993; PTHR15993; 3.
PE 1: Evidence at protein level;
KW Developmental protein; Differentiation; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..514
FT /note="Hemogen"
FT /id="PRO_0000245363"
FT REGION 1..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 7..87
FT /note="Necessary for nuclear localization"
FT /evidence="ECO:0000250"
FT REGION 408..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..450
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXL5"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERZ0"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERZ0"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 207
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 221
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERZ0"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXL5"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXL5"
FT MOD_RES 305
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERZ0"
FT MOD_RES 322
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERZ0"
FT MOD_RES 415
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 422
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CONFLICT 431
FT /note="G -> E (in Ref. 1; CAC16090)"
FT /evidence="ECO:0000305"
FT CONFLICT 503
FT /note="C -> F (in Ref. 1; CAC16090)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 514 AA; 56573 MW; 45E9AE48ACFAEF52 CRC64;
MDVRKDQSHL TLNQTPEAHV EKSHAPDIIG SWSLRNREQL KKRKAEAQGR QTSQWQLGEQ
KKRKYQRTGK GNRRGRKRQG NVEQKAESWS QTENERVQEV LVPAEEETEY SGNTATQALP
LRASPTKAVP TEHCSEVPQE SLQCQEITIQ NHSQTHQRRD KAEALSPTTC QEIGVLQYSP
KMCQDMAEPE ARSPKMCQET AVPQTYSPKA HEDMAEYEAL SPKMCRETPV PQYHSSKIPQ
DMTGPEALAP DMCQETTVSQ NHSSKVPQDM AGPEALSLKM CQEPTVLQEH TLKICQDVAR
PDVLSSKTHQ EMTVPKALPC ITPGDAAGPE GCSPKTLPQS DVTPMSVTPG KNTSHPDLGT
AVAEGCFSEA GECIVSEDIS TKTHQEAVEP KFLSHKTYKE FTVPIVSSHK TIQESPGPEE
YSPGSRHEMS GPEDLSIKTC KNRDGPKHSL PEGAQEVGGA QRQDPDAQDI EDAGAFSQDL
EEGNKADQDP ETPAGPQGPQ KICPENDVHS SALF
