P20839 (IMDH1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Inosine-5'-monophosphate dehydrogenase 1
Short name=IMP dehydrogenase 1
Short name=IMPD 1
Short name=IMPDH 1
EC=1.1.1.205

Alternative name(s):
IMPDH-I

Gene names

Name:	IMPDH1
Synonyms:	IMPD1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	514 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. Could also have a single-stranded nucleic acid-binding activity and could play a role in RNA and/or DNA metabolism. It may also have a role in the development of malignancy and the growth progression of some tumors. HAMAP-Rule MF_03156
Catalytic activity	Inosine 5'-phosphate + NAD+ + H2O = xanthosine 5'-phosphate + NADH. HAMAP-Rule MF_03156
Cofactor	Potassium By similarity.
Enzyme regulation	Mycophenolic acid (MPA) is a non-competitive inhibitor that prevents formation of the closed enzyme conformation by binding to the same site as the amobile flap. In contrast, mizoribine monophosphate (MZP) is a competitive inhibitor that induces the closed conformation. MPA is a potent inhibitor of mammalian IMPDHs but a poor inhibitor of the bacterial enzymes. MZP is a more potent inhibitor of bacterial IMPDH. Subject to product inhibition by XMP and NADH. Also inhibited by ADP. Ref.6
Pathway	Purine metabolism; XMP biosynthesis via de novo pathway; XMP from IMP: step 1/1. HAMAP-Rule MF_03156
Subunit structure	Homotetramer. Ref.6
Subcellular location	Cytoplasm. Nucleus Ref.8.
Tissue specificity	IMP type I is the main species in normal leukocytes and type II predominates over type I in the tumor.
Induction	Constitutively expressed. Ref.6
Involvement in disease	Retinitis pigmentosa 10 (RP10) [MIM:180105]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.11 Ref.12 Ref.13 Leber congenital amaurosis 11 (LCA11) [MIM:613837]: A severe dystrophy of the retina, typically becoming evident in the first years of life. Visual function is usually poor and often accompanied by nystagmus, sluggish or near-absent pupillary responses, photophobia, high hyperopia and keratoconus. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.13
Miscellaneous	Because IMPDH activity is tightly linked with cell proliferation, it has been recognized as a target for cancer and viral chemotherapy and as a target for immunosuppressive drugs. The activities of the antitumor drug tiazofurin, the antiviral drug ribavirin, and the immunosuppressive drugs mizoribine and mycophenolic acid (MPA) are attributed to the inhibition of IMPDH. In addition, bacterial and parasitic IMPDH's differ significantly from mammalian enzymes, which makes it a suitable target for anti-infective drugs. HAMAP-Rule MF_03156
Sequence similarities	Belongs to the IMPDH/GMPR family. Contains 2 CBS domains.
Biophysicochemical properties	Kinetic parameters: KM=18 µM for Inosine 5'-phosphate Ref.6 Ref.7 KM=46 µM for NAD+

Ontologies

Keywords
Biological process	GMP biosynthesis Purine biosynthesis
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Disease	Disease mutation Leber congenital amaurosis Retinitis pigmentosa
Domain	CBS domain Repeat
Ligand	DNA-binding Metal-binding NAD Potassium RNA-binding
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	GMP biosynthetic process Inferred from electronic annotation. Source: HAMAP purine nucleobase metabolic process Traceable author statement. Source: Reactome purine ribonucleoside monophosphate biosynthetic process Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome nucleus Inferred from direct assay Ref.8. Source: UniProtKB
Molecular_function	DNA binding Inferred from direct assay Ref.8. Source: UniProtKB IMP dehydrogenase activity Traceable author statement Ref.1. Source: ProtInc RNA binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: HAMAP nucleotide binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P20839-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P20839-2)

The sequence of this isoform differs from the canonical sequence as follows:
     84-108: Missing.

Note: No experimental confirmation available.

Isoform 3 (identifier: P20839-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MEGPLTPPPLQGGGAAAVPEPGARQHPGHETAAQRYSARLLQAGYEPESM

Isoform 4 (identifier: P20839-4)

The sequence of this isoform differs from the canonical sequence as follows:
     104-108: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.6

Chain

2 – 514

513

Inosine-5'-monophosphate dehydrogenase 1 HAMAP-Rule MF_03156

PRO_0000093670

Regions

Domain

114 – 173

60

CBS 1

Domain

179 – 237

59

CBS 2

Nucleotide binding

274 – 276

3

NAD By similarity

Nucleotide binding

324 – 326

3

NAD By similarity

Region

364 – 366

3

IMP binding HAMAP-Rule MF_03156

Region

387 – 388

2

IMP binding HAMAP-Rule MF_03156

Region

411 – 415

5

IMP binding By similarity

Sites

Active site

331

1

Thioimidate intermediate By similarity

Metal binding

326

1

Potassium; via carbonyl oxygen By similarity

Metal binding

328

1

Potassium; via carbonyl oxygen By similarity

Metal binding

331

1

Potassium; via carbonyl oxygen By similarity

Metal binding

500

1

Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity

Metal binding

501

1

Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity

Metal binding

502

1

Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity

Binding site

329

1

IMP

Binding site

441

1

IMP By similarity

Natural variations

Alternative sequence

1

1

M → MEGPLTPPPLQGGGAAAVPE PGARQHPGHETAAQRYSARL LQAGYEPESM in isoform 3.

VSP_014363

Alternative sequence

84 – 108

25

Missing in isoform 2.

VSP_002674

Alternative sequence

104 – 108

5

Missing in isoform 4.

VSP_043485

Natural variant

105

1

R → W in LCA11; does not alter the enzymatic affinity of the corresponding enzyme; alters the affinity and/or the specificity of single-stranded nucleic acid. Ref.13

VAR_065616

Natural variant

116

1

T → M in RP10; does not alter the enzymatic affinity of the corresponding enzyme; alters the affinity and/or the specificity of single-stranded nucleic acid. Ref.13

VAR_065617

Natural variant

198

1

N → K in LCA11; does not alter the enzymatic affinity of the corresponding enzyme; alters the affinity and/or the specificity of single-stranded nucleic acid. Ref.13

VAR_065618

Natural variant

224

1

R → P in RP10. Ref.11

VAR_017031

Natural variant

226

1

D → N in RP10. Ref.12 Ref.13

VAR_017032

Natural variant

268

1

V → I in RP10. Ref.12 Ref.13

VAR_017033

Natural variant

285

1

A → T. Ref.13

VAR_065619

Natural variant

324

1

G → D Does not alter the enzymatic affinity of the corresponding enzyme; does not affect the affinity for single-stranded nucleic acid. Ref.13

VAR_065620

Natural variant

372

1

H → P in RP10; alters the affinity and/or the specificity of single-stranded nucleic acid. Ref.13

VAR_065621

Experimental info

Sequence conflict

29

1

G → D in AAA36114. Ref.1

Sequence conflict

109

1

K → N in AAA36114. Ref.1

Sequence conflict

273 – 274

2

LD → FH in AAA36114. Ref.1

Sequence conflict

419

1

A → P in AAA36114. Ref.1

Sequence conflict

497

1

A → P in AAA36114. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

514

Helix Strand Turn

Details...

Beta strand

12 – 14

3

Helix

20 – 23

4

Beta strand

26 – 28

3

Helix

32 – 34

3

Beta strand

35 – 37

3

Helix

46 – 48

3

Beta strand

53 – 58

6

Beta strand

60 – 63

4

Beta strand

65 – 67

3

Turn

71 – 73

3

Helix

76 – 84

9

Beta strand

88 – 91

4

Helix

97 – 108

12

Beta strand

142 – 144

3

Turn

160 – 163

4

Turn

195 – 199

5

Helix

200 – 204

5

Beta strand

211 – 216

6

Beta strand

247 – 250

4

Helix

256 – 265

10

Beta strand

269 – 273

5

Helix

281 – 293

13

Beta strand

298 – 304

7

Helix

307 – 316

10

Beta strand

319 – 323

5

Helix

343 – 354

12

Helix

355 – 357

3

Beta strand

361 – 365

5

Helix

370 – 378

9

Beta strand

382 – 387

6

Turn

388 – 392

5

Helix

453 – 471

19

Helix

476 – 484

9

Beta strand

490 – 492

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 8, 2002. Version 2. Checksum: ABAC654A9091BE62	FASTA	514	55,406
	10 20 30 40 50 60 MADYLISGGT GYVPEDGLTA QQLFASADGL TYNDFLILPG FIDFIADEVD LTSALTRKIT 70 80 90 100 110 120 LKTPLISSPM DTVTEADMAI AMALMGGIGF IHHNCTPEFQ ANEVRKVKKF EQGFITDPVV 130 140 150 160 170 180 LSPSHTVGDV LEAKMRHGFS GIPITETGTM GSKLVGIVTS RDIDFLAEKD HTTLLSEVMT 190 200 210 220 230 240 PRIELVVAPA GVTLKEANEI LQRSKKGKLP IVNDCDELVA IIARTDLKKN RDYPLASKDS 250 260 270 280 290 300 QKQLLCGAAV GTREDDKYRL DLLTQAGVDV IVLDSSQGNS VYQIAMVHYI KQKYPHLQVI 310 320 330 340 350 360 GGNVVTAAQA KNLIDAGVDG LRVGMGCGSI CITQEVMACG RPQGTAVYKV AEYARRFGVP 370 380 390 400 410 420 IIADGGIQTV GHVVKALALG ASTVMMGSLL AATTEAPGEY FFSDGVRLKK YRGMGSLDAM 430 440 450 460 470 480 EKSSSSQKRY FSEGDKVKIA QGVSGSIQDK GSIQKFVPYL IAGIQHGCQD IGARSLSVLR 490 500 510 SMMYSGELKF EKRTMSAQIE GGVHGLHSYE KRLY
	Isoform 2 [UniParc]. Checksum: 47A1273662A8C39B	FASTA	489	52,598
	10 20 30 40 50 60 MADYLISGGT GYVPEDGLTA QQLFASADGL TYNDFLILPG FIDFIADEVD LTSALTRKIT 70 80 90 100 110 120 LKTPLISSPM DTVTEADMAI AMAKFEQGFI TDPVVLSPSH TVGDVLEAKM RHGFSGIPIT 130 140 150 160 170 180 ETGTMGSKLV GIVTSRDIDF LAEKDHTTLL SEVMTPRIEL VVAPAGVTLK EANEILQRSK 190 200 210 220 230 240 KGKLPIVNDC DELVAIIART DLKKNRDYPL ASKDSQKQLL CGAAVGTRED DKYRLDLLTQ 250 260 270 280 290 300 AGVDVIVLDS SQGNSVYQIA MVHYIKQKYP HLQVIGGNVV TAAQAKNLID AGVDGLRVGM 310 320 330 340 350 360 GCGSICITQE VMACGRPQGT AVYKVAEYAR RFGVPIIADG GIQTVGHVVK ALALGASTVM 370 380 390 400 410 420 MGSLLAATTE APGEYFFSDG VRLKKYRGMG SLDAMEKSSS SQKRYFSEGD KVKIAQGVSG 430 440 450 460 470 480 SIQDKGSIQK FVPYLIAGIQ HGCQDIGARS LSVLRSMMYS GELKFEKRTM SAQIEGGVHG LHSYEKRLY
	Isoform 3 [UniParc]. Checksum: EB370370B77CD0DA	FASTA	563	60,437
	10 20 30 40 50 60 MEGPLTPPPL QGGGAAAVPE PGARQHPGHE TAAQRYSARL LQAGYEPESM ADYLISGGTG 70 80 90 100 110 120 YVPEDGLTAQ QLFASADGLT YNDFLILPGF IDFIADEVDL TSALTRKITL KTPLISSPMD 130 140 150 160 170 180 TVTEADMAIA MALMGGIGFI HHNCTPEFQA NEVRKVKKFE QGFITDPVVL SPSHTVGDVL 190 200 210 220 230 240 EAKMRHGFSG IPITETGTMG SKLVGIVTSR DIDFLAEKDH TTLLSEVMTP RIELVVAPAG 250 260 270 280 290 300 VTLKEANEIL QRSKKGKLPI VNDCDELVAI IARTDLKKNR DYPLASKDSQ KQLLCGAAVG 310 320 330 340 350 360 TREDDKYRLD LLTQAGVDVI VLDSSQGNSV YQIAMVHYIK QKYPHLQVIG GNVVTAAQAK 370 380 390 400 410 420 NLIDAGVDGL RVGMGCGSIC ITQEVMACGR PQGTAVYKVA EYARRFGVPI IADGGIQTVG 430 440 450 460 470 480 HVVKALALGA STVMMGSLLA ATTEAPGEYF FSDGVRLKKY RGMGSLDAME KSSSSQKRYF 490 500 510 520 530 540 SEGDKVKIAQ GVSGSIQDKG SIQKFVPYLI AGIQHGCQDI GARSLSVLRS MMYSGELKFE 550 560 KRTMSAQIEG GVHGLHSYEK RLY
	Isoform 4 [UniParc]. Checksum: 83819A210AAAB3CA	FASTA	509	54,795
	10 20 30 40 50 60 MADYLISGGT GYVPEDGLTA QQLFASADGL TYNDFLILPG FIDFIADEVD LTSALTRKIT 70 80 90 100 110 120 LKTPLISSPM DTVTEADMAI AMALMGGIGF IHHNCTPEFQ ANEKFEQGFI TDPVVLSPSH 130 140 150 160 170 180 TVGDVLEAKM RHGFSGIPIT ETGTMGSKLV GIVTSRDIDF LAEKDHTTLL SEVMTPRIEL 190 200 210 220 230 240 VVAPAGVTLK EANEILQRSK KGKLPIVNDC DELVAIIART DLKKNRDYPL ASKDSQKQLL 250 260 270 280 290 300 CGAAVGTRED DKYRLDLLTQ AGVDVIVLDS SQGNSVYQIA MVHYIKQKYP HLQVIGGNVV 310 320 330 340 350 360 TAAQAKNLID AGVDGLRVGM GCGSICITQE VMACGRPQGT AVYKVAEYAR RFGVPIIADG 370 380 390 400 410 420 GIQTVGHVVK ALALGASTVM MGSLLAATTE APGEYFFSDG VRLKKYRGMG SLDAMEKSSS 430 440 450 460 470 480 SQKRYFSEGD KVKIAQGVSG SIQDKGSIQK FVPYLIAGIQ HGCQDIGARS LSVLRSMMYS 490 500 GELKFEKRTM SAQIEGGVHG LHSYEKRLY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Two distinct cDNAs for human IMP dehydrogenase." Natsumeda Y., Ohno S., Kawasaki H., Konno Y., Weber G., Suzuki K. J. Biol. Chem. 265:5292-5295(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Spleen.
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4).
[3]	"The DNA sequence of human chromosome 7." Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K. Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"Human chromosome 7: DNA sequence and biology." Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S. , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C. Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). Tissue: Blood.
[6]	"Characterization of human type I and type II IMP dehydrogenases." Carr S.F., Papp E., Wu J.C., Natsumeda Y. J. Biol. Chem. 268:27286-27290(1993) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-11, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ENZYME REGULATION.
[7]	"Recombinant human inosine monophosphate dehydrogenase type I and type II proteins. Purification and characterization of inhibitor binding." Hager P.W., Collart F.R., Huberman E., Mitchell B.S. Biochem. Pharmacol. 49:1323-1329(1995) [PubMed] [Europe PMC] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
[8]	"Inosine 5'-monophosphate dehydrogenase binds nucleic acids in vitro and in vivo." McLean J.E., Hamaguchi N., Belenky P., Mortimer S.E., Stanton M., Hedstrom L. Biochem. J. 379:243-251(2004) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, NUCLEIC ACID-BINDING.
[9]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]	"Crystal structure of the human type I inosine monophosphate dehydrogenase and implications for isoform specificity." Risal D., Strickler M.D., Goldstein B.M. Submitted (FEB-2009) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG.
[11]	"Identification of an IMPDH1 mutation in autosomal dominant retinitis pigmentosa (RP10) revealed following comparative microarray analysis of transcripts derived from retinas of wild-type and Rho(-/-) mice." Kennan A., Aherne A., Palfi A., Humphries M., McKee A., Stitt A., Simpson D.A., Demtroder K., Orntoft T., Ayuso C., Kenna P.F., Farrar G.J., Humphries P. Hum. Mol. Genet. 11:547-557(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT RP10 PRO-224.
[12]	"Mutations in the inosine monophosphate dehydrogenase 1 gene (IMPDH1) cause the RP10 form of autosomal dominant retinitis pigmentosa." Bowne S.J., Sullivan L.S., Blanton S.H., Cepko C.L., Blackshaw S., Birch D.G., Hughbanks-Wheaton D., Heckenlively J.R., Daiger S.P. Hum. Mol. Genet. 11:559-568(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS RP10 ASN-226 AND ILE-268.
[13]	"Spectrum and frequency of mutations in IMPDH1 associated with autosomal dominant retinitis pigmentosa and Leber congenital amaurosis." Bowne S.J., Sullivan L.S., Mortimer S.E., Hedstrom L., Zhu J., Spellicy C.J., Gire A.I., Hughbanks-Wheaton D., Birch D.G., Lewis R.A., Heckenlively J.R., Daiger S.P. Invest. Ophthalmol. Vis. Sci. 47:34-42(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS RP10 MET-116; ASN-226; ILE-268 AND PRO-372, VARIANTS LCA11 TRP-105 AND LYS-198, VARIANTS THR-285 AND ASP-324, CHARACTERIZATION OF VARIANTS RP10 MET-116 AND PRO-372, CHARACTERIZATION OF VARIANTS LCA11 TRP-105 AND LYS-198, CHARACTERIZATION OF VARIANT ASP-324.
+	Additional computationally mapped references.

Web resources

Mutations of the IMPDH1 gene

Retina International's Scientific Newsletter

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J05272 mRNA. Translation: AAA36114.1.
AK054640 mRNA. Translation: BAB70780.1.
AK054667 mRNA. Translation: BAG51409.1.
AK293413 mRNA. Translation: BAG56920.1.
AC010655 Genomic DNA. No translation available.
CH236947 Genomic DNA. Translation: EAL24311.1.
BC033622 mRNA. Translation: AAH33622.2.

IPI

IPI00644730.
IPI00647813.
IPI00916378.
IPI00916697.

PIR

A35566.

RefSeq

NP_001096075.1. NM_001102605.1.
NP_001136045.1. NM_001142573.1.
NP_001136046.1. NM_001142574.1.
NP_001136047.1. NM_001142575.1.
NP_899066.1. NM_183243.2.

UniGene

Hs.654401.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1JCN	X-ray	2.50	A/B	1-514	[»]

ProteinModelPortal

P20839.

ModBase

Search...

Protein-protein interaction databases

IntAct

P20839. 3 interactions.

STRING

9606.ENSP00000345096.

PTM databases

PhosphoSite

P20839.

Polymorphism databases

DMDM

25014074.

Proteomic databases

PaxDb

P20839.

PRIDE

P20839.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000343214; ENSP00000342438; ENSG00000106348.
ENST00000348127; ENSP00000265385; ENSG00000106348.
ENST00000480861; ENSP00000420185; ENSG00000106348.
ENST00000496200; ENSP00000420803; ENSG00000106348.

GeneID

3614.

KEGG

hsa:3614.

UCSC

uc003vmt.2. human.
uc003vmv.2. human.
uc011kol.1. human.

Organism-specific databases

CTD

3614.

GeneCards

GC07M128032.

HGNC

HGNC:6052. IMPDH1.

HPA

HPA001400.

MIM

146690. gene.
180105. phenotype.
613837. phenotype.

neXtProt

NX_P20839.

Orphanet

65. Leber congenital amaurosis.
791. Retinitis pigmentosa.

PharmGKB

PA29862.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0517.

HOGENOM

HOG000165752.

HOVERGEN

HBG052122.

InParanoid

P20839.

KO

K00088.

Enzyme and pathway databases

BioCyc

MetaCyc:HS02896-MONOMER.

Reactome

REACT_111217. Metabolism.

SABIO-RK

P20839.

UniPathway

UPA00601; UER00295.

Gene expression databases

ArrayExpress

P20839.

Bgee

P20839.

CleanEx

HS_IMPDH1.

Genevestigator

P20839.

GermOnline

ENSG00000106348. Homo sapiens.

Family and domain databases

Gene3D

3.20.20.70. 1 hit.

HAMAP

MF_01964. IMPDH.

InterPro

IPR013785. Aldolase_TIM.
IPR000644. Cysta_beta_synth_core.
IPR005990. IMP_DH.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view]

PANTHER

PTHR11911:SF6. PTHR11911:SF6. 1 hit.

Pfam

PF00571. CBS. 2 hits.
PF00478. IMPDH. 1 hit.
[Graphical view]

PIRSF

PIRSF000130. IMPDH. 1 hit.

SMART

SM00116. CBS. 2 hits.
[Graphical view]

TIGRFAMs

TIGR01302. IMP_dehydrog. 1 hit.

PROSITE

PS51371. CBS. 2 hits.
PS00487. IMP_DH_GMP_RED. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P20839.

ChEMBL

CHEMBL1822.

ChiTaRS

IMPDH1. human.

DrugBank

DB00688. Mycophenolate mofetil.
DB01024. Mycophenolic acid.
DB00157. NADH.
DB00811. Ribavirin.
DB00352. Thioguanine.

EvolutionaryTrace

P20839.

GenomeRNAi

3614.

NextBio

14135.

SOURCE

Search...

Entry information

Entry name

IMDH1_HUMAN

Accession

Primary (citable) accession number: P20839
Secondary accession number(s): A4D0Z7 , A6NDW5, B3KNP7, B4DE09, Q8N194, Q96NU2

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	November 8, 2002
Last modified:	May 1, 2013
This is version 164 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.