Full text data of ST13
ST13
(AAG2, FAM10A1, HIP, SNC6)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Hsc70-interacting protein; Hip (Aging-associated protein 2; Progesterone receptor-associated p48 protein; Protein FAM10A1; Putative tumor suppressor ST13; Renal carcinoma antigen NY-REN-33; Suppression of tumorigenicity 13 protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Hsc70-interacting protein; Hip (Aging-associated protein 2; Progesterone receptor-associated p48 protein; Protein FAM10A1; Putative tumor suppressor ST13; Renal carcinoma antigen NY-REN-33; Suppression of tumorigenicity 13 protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00032826
IPI00032826 Hsc70-interacting protein chaperone activity, it may contribute to the interaction of HSC70 with various target proteins, Stabilizes the ADP state of HSC70 that has a high affinity for substrate protein soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
IPI00032826 Hsc70-interacting protein chaperone activity, it may contribute to the interaction of HSC70 with various target proteins, Stabilizes the ADP state of HSC70 that has a high affinity for substrate protein soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
UniProt
P50502
ID F10A1_HUMAN Reviewed; 369 AA.
AC P50502; O14999; Q2TU77;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 30-MAY-2000, sequence version 2.
DT 22-JAN-2014, entry version 148.
DE RecName: Full=Hsc70-interacting protein;
DE Short=Hip;
DE AltName: Full=Aging-associated protein 2;
DE AltName: Full=Progesterone receptor-associated p48 protein;
DE AltName: Full=Protein FAM10A1;
DE AltName: Full=Putative tumor suppressor ST13;
DE AltName: Full=Renal carcinoma antigen NY-REN-33;
DE AltName: Full=Suppression of tumorigenicity 13 protein;
GN Name=ST13; Synonyms=AAG2, FAM10A1, HIP, SNC6;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=8721986; DOI=10.1210/me.10.4.420;
RA Prapapanich V., Chen S., Nair S.C., Rimerman R.A., Smith D.F.;
RT "Molecular cloning of human p48, a transient component of progesterone
RT receptor complexes and an Hsp70-binding protein.";
RL Mol. Endocrinol. 10:420-431(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Colon mucosa;
RX PubMed=9387309;
RA Mo Y., Zheng S., Shen D.;
RT "Differential expression of HSU17714 gene in colorectal cancer and
RT normal colonic mucosa.";
RL Zhonghua Zhong Liu Za Zhi 18:241-243(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Colon mucosa;
RX PubMed=9292708; DOI=10.1007/s004320050085;
RA Cao J., Cai X., Zheng L., Geng L., Shi Z., Pao C.C., Zheng S.;
RT "Characterization of colorectal-cancer-related cDNA clones obtained by
RT subtractive hybridization screening.";
RL J. Cancer Res. Clin. Oncol. 123:447-451(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kim J.W.;
RT "Identification of human aging-associated gene.";
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
RA Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
RA Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
RA Khan A.S., Lane L., Tilahun Y., Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin, and 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP PROTEIN SEQUENCE OF 119-142; 147-153; 174-186 AND 211-222, AND MASS
RP SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [10]
RP IDENTIFICATION AS A RENAL CANCER ANTIGEN.
RC TISSUE=Renal cell carcinoma;
RX PubMed=10508479;
RX DOI=10.1002/(SICI)1097-0215(19991112)83:4<456::AID-IJC4>3.0.CO;2-5;
RA Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
RA Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
RA Old L.J.;
RT "Antigens recognized by autologous antibody in patients with renal-
RT cell carcinoma.";
RL Int. J. Cancer 83:456-464(1999).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP PHOSPHORYLATION AT SER-346, AND INTERACTION WITH GRK5.
RX PubMed=21728385; DOI=10.1021/bi2005202;
RA Barker B.L., Benovic J.L.;
RT "G protein-coupled receptor kinase 5 phosphorylation of Hip regulates
RT internalization of the chemokine receptor CXCR4.";
RL Biochemistry 50:6933-6941(2011).
CC -!- FUNCTION: One HIP oligomer binds the ATPase domains of at least
CC two HSC70 molecules dependent on activation of the HSC70 ATPase by
CC HSP40. Stabilizes the ADP state of HSC70 that has a high affinity
CC for substrate protein. Through its own chaperone activity, it may
CC contribute to the interaction of HSC70 with various target
CC proteins (By similarity).
CC -!- SUBUNIT: Homotetramer. Interacts with HSC70 as well as DNAJ
CC homologs and HSP90 (By similarity). Interacts (via the C-terminus
CC 303- 319 AA) with GRK5.
CC -!- INTERACTION:
CC P02649:APOE; NbExp=3; IntAct=EBI-357285, EBI-1222467;
CC P29474:NOS3; NbExp=3; IntAct=EBI-357285, EBI-1391623;
CC P49768:PSEN1; NbExp=3; IntAct=EBI-357285, EBI-297277;
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the FAM10 family.
CC -!- SIMILARITY: Contains 1 STI1 domain.
CC -!- SIMILARITY: Contains 3 TPR repeats.
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DR EMBL; U28918; AAB38382.1; -; mRNA.
DR EMBL; U17714; AAC97526.1; -; mRNA.
DR EMBL; AY513286; AAT08039.1; -; mRNA.
DR EMBL; CR456586; CAG30472.1; -; mRNA.
DR EMBL; Z98048; CAB10844.1; -; Genomic_DNA.
DR EMBL; CH471095; EAW60394.1; -; Genomic_DNA.
DR EMBL; BC052982; AAH52982.1; -; mRNA.
DR EMBL; BC071629; AAH71629.1; -; mRNA.
DR EMBL; BC139724; AAI39725.1; -; mRNA.
DR RefSeq; NP_003923.2; NM_003932.4.
DR UniGene; Hs.712713; -.
DR PDB; 1UZS; Model; -; A=98-244.
DR PDBsum; 1UZS; -.
DR ProteinModelPortal; P50502; -.
DR SMR; P50502; 113-275.
DR IntAct; P50502; 21.
DR MINT; MINT-4999606; -.
DR STRING; 9606.ENSP00000216218; -.
DR PhosphoSite; P50502; -.
DR DMDM; 6686278; -.
DR OGP; P50502; -.
DR REPRODUCTION-2DPAGE; IPI00032826; -.
DR PaxDb; P50502; -.
DR PeptideAtlas; P50502; -.
DR PRIDE; P50502; -.
DR DNASU; 6767; -.
DR Ensembl; ENST00000216218; ENSP00000216218; ENSG00000100380.
DR GeneID; 6767; -.
DR KEGG; hsa:6767; -.
DR UCSC; uc003aze.3; human.
DR CTD; 6767; -.
DR GeneCards; GC22M041220; -.
DR HGNC; HGNC:11343; ST13.
DR HPA; HPA043233; -.
DR HPA; HPA046412; -.
DR HPA; HPA047114; -.
DR HPA; HPA047116; -.
DR MIM; 606796; gene.
DR neXtProt; NX_P50502; -.
DR PharmGKB; PA36167; -.
DR eggNOG; NOG260098; -.
DR HOGENOM; HOG000001586; -.
DR HOVERGEN; HBG002482; -.
DR InParanoid; P50502; -.
DR KO; K09560; -.
DR OMA; AQNPANI; -.
DR OrthoDB; EOG77M8P3; -.
DR PhylomeDB; P50502; -.
DR ChiTaRS; ST13; human.
DR GeneWiki; ST13; -.
DR GenomeRNAi; 6767; -.
DR NextBio; 26408; -.
DR PMAP-CutDB; P50502; -.
DR PRO; PR:P50502; -.
DR ArrayExpress; P50502; -.
DR Bgee; P50502; -.
DR CleanEx; HS_ST13; -.
DR Genevestigator; P50502; -.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0043234; C:protein complex; IEA:Ensembl.
DR GO; GO:0032564; F:dATP binding; IEA:Ensembl.
DR GO; GO:0030674; F:protein binding, bridging; TAS:ProtInc.
DR GO; GO:0070389; P:chaperone cofactor-dependent protein refolding; IEA:Ensembl.
DR GO; GO:0061084; P:negative regulation of protein refolding; IEA:Ensembl.
DR GO; GO:0006457; P:protein folding; TAS:ProtInc.
DR GO; GO:0051260; P:protein homooligomerization; IEA:Ensembl.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR006636; STI1_HS-bd.
DR InterPro; IPR013026; TPR-contain_dom.
DR InterPro; IPR011990; TPR-like_helical.
DR InterPro; IPR001440; TPR_1.
DR InterPro; IPR013105; TPR_2.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF00515; TPR_1; 1.
DR Pfam; PF07719; TPR_2; 2.
DR SMART; SM00727; STI1; 1.
DR SMART; SM00028; TPR; 3.
DR PROSITE; PS50005; TPR; 3.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Phosphoprotein; Polymorphism;
KW Reference proteome; Repeat; TPR repeat.
FT CHAIN 1 369 Hsc70-interacting protein.
FT /FTId=PRO_0000190811.
FT REPEAT 114 147 TPR 1.
FT REPEAT 148 181 TPR 2.
FT REPEAT 182 215 TPR 3.
FT DOMAIN 319 358 STI1.
FT COMPBIAS 279 312 Gly/Met/Pro-rich.
FT MOD_RES 346 346 Phosphoserine; by GRK5.
FT VARIANT 297 297 M -> I (in dbSNP:rs710193).
FT /FTId=VAR_011900.
FT CONFLICT 24 24 H -> Y (in Ref. 1; AAB38382).
FT CONFLICT 38 38 M -> I (in Ref. 1; AAB38382).
FT CONFLICT 50 50 K -> I (in Ref. 1; AAB38382).
SQ SEQUENCE 369 AA; 41332 MW; 98FCC65BEE14CDD7 CRC64;
MDPRKVNELR AFVKMCKQDP SVLHTEEMRF LREWVESMGG KVPPATQKAK SEENTKEEKP
DSKKVEEDLK ADEPSSEESD LEIDKEGVIE PDTDAPQEMG DENAEITEEM MDQANDKKVA
AIEALNDGEL QKAIDLFTDA IKLNPRLAIL YAKRASVFVK LQKPNAAIRD CDRAIEINPD
SAQPYKWRGK AHRLLGHWEE AAHDLALACK LDYDEDASAM LKEVQPRAQK IAEHRRKYER
KREEREIKER IERVKKAREE HERAQREEEA RRQSGAQYGS FPGGFPGGMP GNFPGGMPGM
GGGMPGMAGM PGLNEILSDP EVLAAMQDPE VMVAFQDVAQ NPANMSKYQS NPKVMNLISK
LSAKFGGQA
//
ID F10A1_HUMAN Reviewed; 369 AA.
AC P50502; O14999; Q2TU77;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 30-MAY-2000, sequence version 2.
DT 22-JAN-2014, entry version 148.
DE RecName: Full=Hsc70-interacting protein;
DE Short=Hip;
DE AltName: Full=Aging-associated protein 2;
DE AltName: Full=Progesterone receptor-associated p48 protein;
DE AltName: Full=Protein FAM10A1;
DE AltName: Full=Putative tumor suppressor ST13;
DE AltName: Full=Renal carcinoma antigen NY-REN-33;
DE AltName: Full=Suppression of tumorigenicity 13 protein;
GN Name=ST13; Synonyms=AAG2, FAM10A1, HIP, SNC6;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=8721986; DOI=10.1210/me.10.4.420;
RA Prapapanich V., Chen S., Nair S.C., Rimerman R.A., Smith D.F.;
RT "Molecular cloning of human p48, a transient component of progesterone
RT receptor complexes and an Hsp70-binding protein.";
RL Mol. Endocrinol. 10:420-431(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Colon mucosa;
RX PubMed=9387309;
RA Mo Y., Zheng S., Shen D.;
RT "Differential expression of HSU17714 gene in colorectal cancer and
RT normal colonic mucosa.";
RL Zhonghua Zhong Liu Za Zhi 18:241-243(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Colon mucosa;
RX PubMed=9292708; DOI=10.1007/s004320050085;
RA Cao J., Cai X., Zheng L., Geng L., Shi Z., Pao C.C., Zheng S.;
RT "Characterization of colorectal-cancer-related cDNA clones obtained by
RT subtractive hybridization screening.";
RL J. Cancer Res. Clin. Oncol. 123:447-451(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kim J.W.;
RT "Identification of human aging-associated gene.";
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
RA Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
RA Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
RA Khan A.S., Lane L., Tilahun Y., Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin, and 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP PROTEIN SEQUENCE OF 119-142; 147-153; 174-186 AND 211-222, AND MASS
RP SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [10]
RP IDENTIFICATION AS A RENAL CANCER ANTIGEN.
RC TISSUE=Renal cell carcinoma;
RX PubMed=10508479;
RX DOI=10.1002/(SICI)1097-0215(19991112)83:4<456::AID-IJC4>3.0.CO;2-5;
RA Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
RA Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
RA Old L.J.;
RT "Antigens recognized by autologous antibody in patients with renal-
RT cell carcinoma.";
RL Int. J. Cancer 83:456-464(1999).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP PHOSPHORYLATION AT SER-346, AND INTERACTION WITH GRK5.
RX PubMed=21728385; DOI=10.1021/bi2005202;
RA Barker B.L., Benovic J.L.;
RT "G protein-coupled receptor kinase 5 phosphorylation of Hip regulates
RT internalization of the chemokine receptor CXCR4.";
RL Biochemistry 50:6933-6941(2011).
CC -!- FUNCTION: One HIP oligomer binds the ATPase domains of at least
CC two HSC70 molecules dependent on activation of the HSC70 ATPase by
CC HSP40. Stabilizes the ADP state of HSC70 that has a high affinity
CC for substrate protein. Through its own chaperone activity, it may
CC contribute to the interaction of HSC70 with various target
CC proteins (By similarity).
CC -!- SUBUNIT: Homotetramer. Interacts with HSC70 as well as DNAJ
CC homologs and HSP90 (By similarity). Interacts (via the C-terminus
CC 303- 319 AA) with GRK5.
CC -!- INTERACTION:
CC P02649:APOE; NbExp=3; IntAct=EBI-357285, EBI-1222467;
CC P29474:NOS3; NbExp=3; IntAct=EBI-357285, EBI-1391623;
CC P49768:PSEN1; NbExp=3; IntAct=EBI-357285, EBI-297277;
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the FAM10 family.
CC -!- SIMILARITY: Contains 1 STI1 domain.
CC -!- SIMILARITY: Contains 3 TPR repeats.
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DR EMBL; U28918; AAB38382.1; -; mRNA.
DR EMBL; U17714; AAC97526.1; -; mRNA.
DR EMBL; AY513286; AAT08039.1; -; mRNA.
DR EMBL; CR456586; CAG30472.1; -; mRNA.
DR EMBL; Z98048; CAB10844.1; -; Genomic_DNA.
DR EMBL; CH471095; EAW60394.1; -; Genomic_DNA.
DR EMBL; BC052982; AAH52982.1; -; mRNA.
DR EMBL; BC071629; AAH71629.1; -; mRNA.
DR EMBL; BC139724; AAI39725.1; -; mRNA.
DR RefSeq; NP_003923.2; NM_003932.4.
DR UniGene; Hs.712713; -.
DR PDB; 1UZS; Model; -; A=98-244.
DR PDBsum; 1UZS; -.
DR ProteinModelPortal; P50502; -.
DR SMR; P50502; 113-275.
DR IntAct; P50502; 21.
DR MINT; MINT-4999606; -.
DR STRING; 9606.ENSP00000216218; -.
DR PhosphoSite; P50502; -.
DR DMDM; 6686278; -.
DR OGP; P50502; -.
DR REPRODUCTION-2DPAGE; IPI00032826; -.
DR PaxDb; P50502; -.
DR PeptideAtlas; P50502; -.
DR PRIDE; P50502; -.
DR DNASU; 6767; -.
DR Ensembl; ENST00000216218; ENSP00000216218; ENSG00000100380.
DR GeneID; 6767; -.
DR KEGG; hsa:6767; -.
DR UCSC; uc003aze.3; human.
DR CTD; 6767; -.
DR GeneCards; GC22M041220; -.
DR HGNC; HGNC:11343; ST13.
DR HPA; HPA043233; -.
DR HPA; HPA046412; -.
DR HPA; HPA047114; -.
DR HPA; HPA047116; -.
DR MIM; 606796; gene.
DR neXtProt; NX_P50502; -.
DR PharmGKB; PA36167; -.
DR eggNOG; NOG260098; -.
DR HOGENOM; HOG000001586; -.
DR HOVERGEN; HBG002482; -.
DR InParanoid; P50502; -.
DR KO; K09560; -.
DR OMA; AQNPANI; -.
DR OrthoDB; EOG77M8P3; -.
DR PhylomeDB; P50502; -.
DR ChiTaRS; ST13; human.
DR GeneWiki; ST13; -.
DR GenomeRNAi; 6767; -.
DR NextBio; 26408; -.
DR PMAP-CutDB; P50502; -.
DR PRO; PR:P50502; -.
DR ArrayExpress; P50502; -.
DR Bgee; P50502; -.
DR CleanEx; HS_ST13; -.
DR Genevestigator; P50502; -.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0043234; C:protein complex; IEA:Ensembl.
DR GO; GO:0032564; F:dATP binding; IEA:Ensembl.
DR GO; GO:0030674; F:protein binding, bridging; TAS:ProtInc.
DR GO; GO:0070389; P:chaperone cofactor-dependent protein refolding; IEA:Ensembl.
DR GO; GO:0061084; P:negative regulation of protein refolding; IEA:Ensembl.
DR GO; GO:0006457; P:protein folding; TAS:ProtInc.
DR GO; GO:0051260; P:protein homooligomerization; IEA:Ensembl.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR006636; STI1_HS-bd.
DR InterPro; IPR013026; TPR-contain_dom.
DR InterPro; IPR011990; TPR-like_helical.
DR InterPro; IPR001440; TPR_1.
DR InterPro; IPR013105; TPR_2.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF00515; TPR_1; 1.
DR Pfam; PF07719; TPR_2; 2.
DR SMART; SM00727; STI1; 1.
DR SMART; SM00028; TPR; 3.
DR PROSITE; PS50005; TPR; 3.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Phosphoprotein; Polymorphism;
KW Reference proteome; Repeat; TPR repeat.
FT CHAIN 1 369 Hsc70-interacting protein.
FT /FTId=PRO_0000190811.
FT REPEAT 114 147 TPR 1.
FT REPEAT 148 181 TPR 2.
FT REPEAT 182 215 TPR 3.
FT DOMAIN 319 358 STI1.
FT COMPBIAS 279 312 Gly/Met/Pro-rich.
FT MOD_RES 346 346 Phosphoserine; by GRK5.
FT VARIANT 297 297 M -> I (in dbSNP:rs710193).
FT /FTId=VAR_011900.
FT CONFLICT 24 24 H -> Y (in Ref. 1; AAB38382).
FT CONFLICT 38 38 M -> I (in Ref. 1; AAB38382).
FT CONFLICT 50 50 K -> I (in Ref. 1; AAB38382).
SQ SEQUENCE 369 AA; 41332 MW; 98FCC65BEE14CDD7 CRC64;
MDPRKVNELR AFVKMCKQDP SVLHTEEMRF LREWVESMGG KVPPATQKAK SEENTKEEKP
DSKKVEEDLK ADEPSSEESD LEIDKEGVIE PDTDAPQEMG DENAEITEEM MDQANDKKVA
AIEALNDGEL QKAIDLFTDA IKLNPRLAIL YAKRASVFVK LQKPNAAIRD CDRAIEINPD
SAQPYKWRGK AHRLLGHWEE AAHDLALACK LDYDEDASAM LKEVQPRAQK IAEHRRKYER
KREEREIKER IERVKKAREE HERAQREEEA RRQSGAQYGS FPGGFPGGMP GNFPGGMPGM
GGGMPGMAGM PGLNEILSDP EVLAAMQDPE VMVAFQDVAQ NPANMSKYQS NPKVMNLISK
LSAKFGGQA
//
MIM
606796
*RECORD*
*FIELD* NO
606796
*FIELD* TI
*606796 SUPPRESSION OF TUMORIGENICITY 13; ST13
;;P48;;
HSC70-INTERACTING PROTEIN; HIP
read more*FIELD* TX
DESCRIPTION
ST13 is an abundant, highly conserved protein that binds the major
cytosolic chaperones heat-shock protein 70-kD (HSP70; see 140550) and
HSP90 (see 140571) during an intermediate stage of steroid receptor
assembly, but is absent from the mature receptor complex.
CLONING
Prapapanich et al. (1996) isolated a 48-kD protein that transiently
associates with progesterone receptor (607311) during cell-free assembly
in rabbit reticulocyte lysate. Using an antibody developed against the
purified protein, Prapapanich et al. (1996) cloned ST13 cDNA from a HeLa
cell cDNA library. The deduced 369-amino acid protein has a calculated
molecular mass of approximately 41 kD and an apparent molecular mass of
48 kD by SDS-PAGE. By Northern blot analysis, Prapapanich et al. (1996)
identified 4 ST13 mRNAs, ranging in size from about 1.3 kb to 3.2 kb,
with expression in all tissues examined.
GENE FUNCTION
Using a yeast 2-hybrid assay, Hohfeld et al. (1995) showed that rat Hip
bound Hsc70 (HSPA8; 600816). One Hip oligomer bound the ATPase domains
of at least 2 Hsc70 molecules, and binding was dependent on activation
of the Hsc70 ATPase by Hsp40 (DNAJB1; 604572). Hip stabilized the
ADP-bound form of Hsc70, which had a high affinity for a test protein
substrate. Hohfeld et al. (1995) concluded that HIP contributes to
interactions of HSC70 with target proteins through its own chaperone
activity.
Prapapanich et al. (1996) coimmunoprecipitated progesterone receptor
assembly complexes with in vitro translated ST13. By Western blot
analysis, they identified HSP70 and HSP90 in these complexes.
Using subtractive hybridization between cDNA of normal mucosal tissues
and mRNA of colorectal carcinoma tissues, Cao et al. (1997) found
downregulated expression of ST13 in the cancer tissues.
Using a yeast expression system, Nelson et al. (2004) found that human
HIP enhanced hormone-dependent activation of a reporter gene by rat
glucocorticoid receptor (GCCR; 138040). HIP promoted functional
maturation of Gccr by enhancing formation of its ligand-binding domain.
HIP did not affect the steady-state levels of Gccr protein, and its
activity did not require yeast Hsp70 proteins. N-terminal truncation of
HIP reduced its ability to enhance Gccr signaling, likely due to loss of
HIP homooligomerization. HOP (STIP1; 605063) also appeared to have an
HSP70-independent role in GCCR maturation.
Polyglutamine disorders, such as spinal and bulbar muscular atrophy
(SBMA, or SMAX1; 313200) and Huntington disease (143100), are caused by
an expansion in the glutamine trinucleotide (CAG) repeat in the affected
genes, resulting in mutant proteins that aggregate into insoluble
inclusions within affected neurons. Howarth et al. (2009) showed that
overexpression of human HIP significantly reduced inclusion formation in
an in vitro mouse model of SBMA and in a rat primary neuronal model of
polyglutamine disease. The activity of denatured luciferase, a measure
of protein refolding, was not increased in the presence of HIP alone,
but it was increased when HIP was coexpressed with HSP70 or HSC70.
Howarth et al. (2009) concluded that HIP may prevent inclusion formation
by facilitating the constitutive HSC70 refolding cycle and possibly by
preventing aggregation.
MAPPING
Zhang et al. (1998) mapped the ST13 gene to chromosome 22q13 by
fluorescence in situ hybridization. They noted that colorectal, breast,
and ovarian carcinomas frequently show loss of heterozygosity at this
site.
*FIELD* RF
1. Cao, J.; Cai, X.; Zheng, L.; Geng, L.; Shi, Z.; Pao, C. C.; Zheng,
S.: Characterization of colorectal-cancer-related cDNA clones obtained
by subtractive hybridization screening. J. Cancer Res. Clin. Oncol. 123:
447-451, 1997.
2. Hohfeld, J.; Minami, Y.; Hartl, F.-U.: Hip, a novel cochaperone
involved in the eukaryotic Hsc70/Hsp40 reaction cycle. Cell 83:
589-598, 1995.
3. Howarth, J. L.; Glover, C. P. J.; Uney, J. B.: HSP70 interacting
protein prevents the accumulation of inclusions in polyglutamine disease. J.
Neurochem. 108: 945-951, 2009.
4. Nelson, G. M.; Prapapanich, V.; Carrigan, P. E.; Roberts, P. J.;
Riggs, D. L.; Smith, D. F.: The heat shock protein 70 cochaperone
Hip enhances functional maturation of glucocorticoid receptor. Molec.
Endocr. 18: 1620-1630, 2004.
5. Prapapanich, V.; Chen, S.; Nair, S. C.; Rimerman, R. A.; Smith,
D. F.: Molecular cloning of human p48, a transient component of progesterone
receptor complexes and an Hsp70-binding protein. Molec. Endocr. 10:
420-431, 1996.
6. Zhang, Y.; Cai, X.; Schlegelberger, B.; Zheng, S.: Assignment
of human putative tumor suppressor genes ST13 (alias SNC6) and ST14
(alias SNC19) to human chromosome bands 22q13 and 11q24-q25 by in
situ hybridization. Cytogenet. Cell Genet. 83: 56-57, 1998.
*FIELD* CN
Patricia A. Hartz - updated: 7/17/2009
*FIELD* CD
Patricia A. Hartz: 3/26/2002
*FIELD* ED
mgross: 07/20/2009
terry: 7/17/2009
terry: 12/17/2007
wwang: 7/17/2007
mgross: 2/12/2007
mgross: 10/18/2002
carol: 3/29/2002
carol: 3/28/2002
*RECORD*
*FIELD* NO
606796
*FIELD* TI
*606796 SUPPRESSION OF TUMORIGENICITY 13; ST13
;;P48;;
HSC70-INTERACTING PROTEIN; HIP
read more*FIELD* TX
DESCRIPTION
ST13 is an abundant, highly conserved protein that binds the major
cytosolic chaperones heat-shock protein 70-kD (HSP70; see 140550) and
HSP90 (see 140571) during an intermediate stage of steroid receptor
assembly, but is absent from the mature receptor complex.
CLONING
Prapapanich et al. (1996) isolated a 48-kD protein that transiently
associates with progesterone receptor (607311) during cell-free assembly
in rabbit reticulocyte lysate. Using an antibody developed against the
purified protein, Prapapanich et al. (1996) cloned ST13 cDNA from a HeLa
cell cDNA library. The deduced 369-amino acid protein has a calculated
molecular mass of approximately 41 kD and an apparent molecular mass of
48 kD by SDS-PAGE. By Northern blot analysis, Prapapanich et al. (1996)
identified 4 ST13 mRNAs, ranging in size from about 1.3 kb to 3.2 kb,
with expression in all tissues examined.
GENE FUNCTION
Using a yeast 2-hybrid assay, Hohfeld et al. (1995) showed that rat Hip
bound Hsc70 (HSPA8; 600816). One Hip oligomer bound the ATPase domains
of at least 2 Hsc70 molecules, and binding was dependent on activation
of the Hsc70 ATPase by Hsp40 (DNAJB1; 604572). Hip stabilized the
ADP-bound form of Hsc70, which had a high affinity for a test protein
substrate. Hohfeld et al. (1995) concluded that HIP contributes to
interactions of HSC70 with target proteins through its own chaperone
activity.
Prapapanich et al. (1996) coimmunoprecipitated progesterone receptor
assembly complexes with in vitro translated ST13. By Western blot
analysis, they identified HSP70 and HSP90 in these complexes.
Using subtractive hybridization between cDNA of normal mucosal tissues
and mRNA of colorectal carcinoma tissues, Cao et al. (1997) found
downregulated expression of ST13 in the cancer tissues.
Using a yeast expression system, Nelson et al. (2004) found that human
HIP enhanced hormone-dependent activation of a reporter gene by rat
glucocorticoid receptor (GCCR; 138040). HIP promoted functional
maturation of Gccr by enhancing formation of its ligand-binding domain.
HIP did not affect the steady-state levels of Gccr protein, and its
activity did not require yeast Hsp70 proteins. N-terminal truncation of
HIP reduced its ability to enhance Gccr signaling, likely due to loss of
HIP homooligomerization. HOP (STIP1; 605063) also appeared to have an
HSP70-independent role in GCCR maturation.
Polyglutamine disorders, such as spinal and bulbar muscular atrophy
(SBMA, or SMAX1; 313200) and Huntington disease (143100), are caused by
an expansion in the glutamine trinucleotide (CAG) repeat in the affected
genes, resulting in mutant proteins that aggregate into insoluble
inclusions within affected neurons. Howarth et al. (2009) showed that
overexpression of human HIP significantly reduced inclusion formation in
an in vitro mouse model of SBMA and in a rat primary neuronal model of
polyglutamine disease. The activity of denatured luciferase, a measure
of protein refolding, was not increased in the presence of HIP alone,
but it was increased when HIP was coexpressed with HSP70 or HSC70.
Howarth et al. (2009) concluded that HIP may prevent inclusion formation
by facilitating the constitutive HSC70 refolding cycle and possibly by
preventing aggregation.
MAPPING
Zhang et al. (1998) mapped the ST13 gene to chromosome 22q13 by
fluorescence in situ hybridization. They noted that colorectal, breast,
and ovarian carcinomas frequently show loss of heterozygosity at this
site.
*FIELD* RF
1. Cao, J.; Cai, X.; Zheng, L.; Geng, L.; Shi, Z.; Pao, C. C.; Zheng,
S.: Characterization of colorectal-cancer-related cDNA clones obtained
by subtractive hybridization screening. J. Cancer Res. Clin. Oncol. 123:
447-451, 1997.
2. Hohfeld, J.; Minami, Y.; Hartl, F.-U.: Hip, a novel cochaperone
involved in the eukaryotic Hsc70/Hsp40 reaction cycle. Cell 83:
589-598, 1995.
3. Howarth, J. L.; Glover, C. P. J.; Uney, J. B.: HSP70 interacting
protein prevents the accumulation of inclusions in polyglutamine disease. J.
Neurochem. 108: 945-951, 2009.
4. Nelson, G. M.; Prapapanich, V.; Carrigan, P. E.; Roberts, P. J.;
Riggs, D. L.; Smith, D. F.: The heat shock protein 70 cochaperone
Hip enhances functional maturation of glucocorticoid receptor. Molec.
Endocr. 18: 1620-1630, 2004.
5. Prapapanich, V.; Chen, S.; Nair, S. C.; Rimerman, R. A.; Smith,
D. F.: Molecular cloning of human p48, a transient component of progesterone
receptor complexes and an Hsp70-binding protein. Molec. Endocr. 10:
420-431, 1996.
6. Zhang, Y.; Cai, X.; Schlegelberger, B.; Zheng, S.: Assignment
of human putative tumor suppressor genes ST13 (alias SNC6) and ST14
(alias SNC19) to human chromosome bands 22q13 and 11q24-q25 by in
situ hybridization. Cytogenet. Cell Genet. 83: 56-57, 1998.
*FIELD* CN
Patricia A. Hartz - updated: 7/17/2009
*FIELD* CD
Patricia A. Hartz: 3/26/2002
*FIELD* ED
mgross: 07/20/2009
terry: 7/17/2009
terry: 12/17/2007
wwang: 7/17/2007
mgross: 2/12/2007
mgross: 10/18/2002
carol: 3/29/2002
carol: 3/28/2002