Q16671 (AMHR2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Anti-Muellerian hormone type-2 receptor
EC=2.7.11.30

Alternative name(s):
Anti-Muellerian hormone type II receptor
Short name=AMH type II receptor
MIS type II receptor
Short name=MISRII
Short name=MRII

Gene names

Name:	AMHR2
Synonyms:	AMHR, MISR2

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	573 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	On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for anti-Muellerian hormone.
Catalytic activity	ATP + [receptor-protein] = ADP + [receptor-protein] phosphate.
Cofactor	Magnesium or manganese By similarity.
Subcellular location	Membrane; Single-pass type I membrane protein.
Involvement in disease	Persistent Muellerian duct syndrome 2 (PMDS2) [MIM:261550]: A form of male pseudohermaphroditism characterized by a failure of Muellerian duct regression in otherwise normal males. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.8 Ref.9
Sequence similarities	Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. TGFB receptor subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Cellular component	Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Pseudohermaphroditism
Domain	Signal Transmembrane Transmembrane helix
Ligand	ATP-binding Magnesium Manganese Metal-binding Nucleotide-binding
Molecular function	Kinase Receptor Serine/threonine-protein kinase Transferase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Mullerian duct regression Non-traceable author statement PubMed 14750901. Source: UniProtKB signal transduction Inferred from mutant phenotype Ref.1. Source: UniProtKB transforming growth factor beta receptor signaling pathway Inferred from electronic annotation. Source: Compara
Cellular_component	integral to plasma membrane Inferred from electronic annotation. Source: Compara
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW hormone binding Inferred from physical interaction PubMed 14750901. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW receptor activity Inferred from mutant phenotype Ref.1. Source: UniProtKB transforming growth factor beta receptor activity, type II Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HSP90AB1	P08238	2	EBI-6423788,EBI-352572

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q16671-1)

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: Q16671-2)

The sequence of this isoform differs from the canonical sequence as follows:
     430-573: DSSPPPFQLA...PQPACTLSPV → AVHHPSNWPM...GAALPQTLMG

Note: No experimental confirmation available.

Isoform 3 (identifier: Q16671-3)

The sequence of this isoform differs from the canonical sequence as follows:
     381-475: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 17	17	Potential
	Chain	18 – 573	556	Anti-Muellerian hormone type-2 receptor		PRO_0000024408
Regions
	Topological domain	18 – 149	132	Extracellular Potential
	Transmembrane	150 – 170	21	Helical; Potential
	Topological domain	171 – 573	403	Cytoplasmic Potential
	Domain	203 – 518	316	Protein kinase
	Nucleotide binding	209 – 217	9	ATP By similarity
Sites
	Active site	333	1	Proton acceptor By similarity
	Binding site	230	1	ATP By similarity
Amino acid modifications
	Glycosylation	66	1	N-linked (GlcNAc...) Potential
	Glycosylation	119	1	N-linked (GlcNAc...) Potential
Natural variations
	Alternative sequence	381 – 475	95	Missing in isoform 3.		VSP_045281
	Alternative sequence	430 – 573	144	DSSPP…TLSPV → AVHHPSNWPMRQNWAIPLPL MSYGPWQCRRGGVPTSHPPG AALPQTLMG in isoform 2.		VSP_044548
	Natural variant	54	1	R → C in PMDS2. Ref.8		VAR_015525
	Natural variant	142	1	G → V in PMDS2. Ref.8		VAR_015526
	Natural variant	282	1	H → Q in PMDS2. Ref.8		VAR_015527
	Natural variant	319	1	R → H. Ref.4 Corresponds to variant rs144236183 [ dbSNP | Ensembl ].		VAR_069048
	Natural variant	406	1	R → Q in PMDS2. Ref.9		VAR_015528
	Natural variant	426	1	D → G in PMDS2. Ref.8		VAR_015529
	Natural variant	444 – 452	9	Missing in PMDS2.		VAR_031057
	Natural variant	458	1	V → A in PMDS2. Ref.8		VAR_015530
	Natural variant	491	1	D → H in PMDS2. Ref.8		VAR_015531
	Natural variant	504	1	R → C in PMDS2. Ref.8		VAR_015532
Experimental info
	Sequence conflict	121	1	S → N in AAU21221. Ref.4
	Sequence conflict	161	1	L → V in CAA62593. Ref.2
	Sequence conflict	501	1	V → A in AAU21221. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 1347C10C2942FDBA	FASTA	573	62,750
	10 20 30 40 50 60 MLGSLGLWAL LPTAVEAPPN RRTCVFFEAP GVRGSTKTLG ELLDTGTELP RAIRCLYSRC 70 80 90 100 110 120 CFGIWNLTQD RAQVEMQGCR DSDEPGCESL HCDPSPRAHP SPGSTLFTCS CGTDFCNANY 130 140 150 160 170 180 SHLPPPGSPG TPGSQGPQAA PGESIWMALV LLGLFLLLLL LLGSIILALL QRKNYRVRGE 190 200 210 220 230 240 PVPEPRPDSG RDWSVELQEL PELCFSQVIR EGGHAVVWAG QLQGKLVAIK AFPPRSVAQF 250 260 270 280 290 300 QAERALYELP GLQHDHIVRF ITASRGGPGR LLSGPLLVLE LHPKGSLCHY LTQYTSDWGS 310 320 330 340 350 360 SLRMALSLAQ GLAFLHEERW QNGQYKPGIA HRDLSSQNVL IREDGSCAIG DLGLALVLPG 370 380 390 400 410 420 LTQPPAWTPT QPQGPAAIME AGTQRYMAPE LLDKTLDLQD WGMALRRADI YSLALLLWEI 430 440 450 460 470 480 LSRCPDLRPD SSPPPFQLAY EAELGNTPTS DELWALAVQE RRRPYIPSTW RCFATDPDGL 490 500 510 520 530 540 RELLEDCWDA DPEARLTAEC VQQRLAALAH PQESHPFPES CPRGCPPLCP EDCTSIPAPT 550 560 570 ILPCRPQRSA CHFSVQQGPC SRNPQPACTL SPV
	Isoform 2 [UniParc]. Checksum: ADCA1BB6AC850665	FASTA	478	52,241
	10 20 30 40 50 60 MLGSLGLWAL LPTAVEAPPN RRTCVFFEAP GVRGSTKTLG ELLDTGTELP RAIRCLYSRC 70 80 90 100 110 120 CFGIWNLTQD RAQVEMQGCR DSDEPGCESL HCDPSPRAHP SPGSTLFTCS CGTDFCNANY 130 140 150 160 170 180 SHLPPPGSPG TPGSQGPQAA PGESIWMALV LLGLFLLLLL LLGSIILALL QRKNYRVRGE 190 200 210 220 230 240 PVPEPRPDSG RDWSVELQEL PELCFSQVIR EGGHAVVWAG QLQGKLVAIK AFPPRSVAQF 250 260 270 280 290 300 QAERALYELP GLQHDHIVRF ITASRGGPGR LLSGPLLVLE LHPKGSLCHY LTQYTSDWGS 310 320 330 340 350 360 SLRMALSLAQ GLAFLHEERW QNGQYKPGIA HRDLSSQNVL IREDGSCAIG DLGLALVLPG 370 380 390 400 410 420 LTQPPAWTPT QPQGPAAIME AGTQRYMAPE LLDKTLDLQD WGMALRRADI YSLALLLWEI 430 440 450 460 470 LSRCPDLRPA VHHPSNWPMR QNWAIPLPLM SYGPWQCRRG GVPTSHPPGA ALPQTLMG
	Isoform 3 [UniParc]. Checksum: C0FA484B50E52A97	FASTA	478	51,827
	10 20 30 40 50 60 MLGSLGLWAL LPTAVEAPPN RRTCVFFEAP GVRGSTKTLG ELLDTGTELP RAIRCLYSRC 70 80 90 100 110 120 CFGIWNLTQD RAQVEMQGCR DSDEPGCESL HCDPSPRAHP SPGSTLFTCS CGTDFCNANY 130 140 150 160 170 180 SHLPPPGSPG TPGSQGPQAA PGESIWMALV LLGLFLLLLL LLGSIILALL QRKNYRVRGE 190 200 210 220 230 240 PVPEPRPDSG RDWSVELQEL PELCFSQVIR EGGHAVVWAG QLQGKLVAIK AFPPRSVAQF 250 260 270 280 290 300 QAERALYELP GLQHDHIVRF ITASRGGPGR LLSGPLLVLE LHPKGSLCHY LTQYTSDWGS 310 320 330 340 350 360 SLRMALSLAQ GLAFLHEERW QNGQYKPGIA HRDLSSQNVL IREDGSCAIG DLGLALVLPG 370 380 390 400 410 420 LTQPPAWTPT QPQGPAAIME DPDGLRELLE DCWDADPEAR LTAECVQQRL AALAHPQESH 430 440 450 460 470 PFPESCPRGC PPLCPEDCTS IPAPTILPCR PQRSACHFSV QQGPCSRNPQ PACTLSPV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Insensitivity to anti-Muellerian hormone due to a mutation in the human anti-Muellerian hormone receptor." Imbeaud S., Faure E., Lamarre I., Mattei M.-G., di Clemente N., Tizard R., Carre-Eusebe D., Belville C., Tragethon L., Tonkin C., Nelson J., McAuliffe M., Bidart J.-M., Lababidi A., Josso N., Cate R.L., Picard J.-Y. Nat. Genet. 11:382-388(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Structure and chromosomal localization of the human anti-Muellerian hormone type II receptor gene." Visser J.A., McLuskey A., van Beers T., Weghuis D.O., van Kessel A.G., Grootegoed J.A., Themmen A.P.N. Biochem. Biophys. Res. Commun. 215:1029-1036(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Human ovarian cancer, cell lines, and primary ascites cells express the human Muellerian inhibiting substance (MIS) type II receptor, bind, and are responsive to MIS." Masiakos P.T., MacLaughlin D.T., Maheswaran S., Teixeira J., Fuller A.F. Jr., Shah P.C., Kehas D.J., Kenneally M.K., Dombkowski D.M., Ha T.U., Preffer F.I., Donahoe P.K. Clin. Cancer Res. 5:3488-3499(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Testis.
[4]	Li H., Ke R., Shen C., Zhou G., Zhong G., Lin L., Yang S. Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), VARIANT HIS-319.
[5]	"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] (ISOFORM 2). Tissue: Testis.
[6]	"The finished DNA sequence of human chromosome 12." Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A. Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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 1). Tissue: Testis.
[8]	"A 27 base-pair deletion of the anti-Muellerian type II receptor gene is the most common cause of the persistent Muellerian duct syndrome." Imbeaud S., Belville C., Messika-Zeitoun L., Rey R., di Clemente N., Josso N., Picard J.-Y. Hum. Mol. Genet. 5:1269-1277(1996) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS PMDS2 CYS-54; VAL-142; GLN-282; GLY-426; 444-LEU--GLU-452 DEL; ALA-458; HIS-491 AND CYS-504.
[9]	"Autosomal recessive segregation of a truncating mutation of anti-Muellerian type II receptor in a family affected by the persistent Muellerian duct syndrome contrasts with its dominant negative activity in vitro." Messika-Zeitoun L., Gouedard L., Belville C., Dutertre M., Lins L., Imbeaud S., Hughes I.A., Picard J.-Y., Josso N., di Clemente N. J. Clin. Endocrinol. Metab. 86:4390-4397(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PMDS2 GLN-406.
+	Additional computationally mapped references.

Web resources

Wikipedia

Anti-Mullerian hormone entry

Cross-references

Sequence databases
EMBL GenBank DDBJ	X89013 Genomic DNA. Translation: CAA61418.1. U29700 Genomic DNA. Translation: AAC50328.1. X91156 , X91157, X91158, X91159, X91160, X91161, X91162, X91163, X91164, X91165, X91166 Genomic DNA. Translation: CAA62593.1. AF172932 mRNA. Translation: AAD48497.1. AY714878 mRNA. Translation: AAU21221.1. AK313593 mRNA. No translation available. AC068889 Genomic DNA. No translation available. BC126316 mRNA. Translation: AAI26317.1. BC136356 mRNA. Translation: AAI36357.1.
IPI	IPI00003446. IPI00470548. IPI00944502.
PIR	JC4335.
RefSeq	NP_001158162.1. NM_001164690.1. NP_001158163.1. NM_001164691.1. NP_065434.1. NM_020547.2.
UniGene	Hs.659889.
3D structure databases
ProteinModelPortal	Q16671.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q16671. 1 interaction.
STRING	9606.ENSP00000257863.
PTM databases
PhosphoSite	Q16671.
Polymorphism databases
DMDM	9087133.
Proteomic databases
PaxDb	Q16671.
PRIDE	Q16671.
Protocols and materials databases
DNASU	269.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000257863; ENSP00000257863; ENSG00000135409. ENST00000379791; ENSP00000369117; ENSG00000135409. ENST00000550311; ENSP00000446661; ENSG00000135409.
GeneID	269.
KEGG	hsa:269.
UCSC	uc001scx.2. human. uc009zmy.2. human. uc021qyg.1. human.
Organism-specific databases
CTD	269.
GeneCards	GC12P053823.
HGNC	HGNC:465. AMHR2.
MIM	261550. phenotype. 600956. gene.
neXtProt	NX_Q16671.
Orphanet	2856. Persistent Mullerian duct syndrome.
PharmGKB	PA24770.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG243040.
HOGENOM	HOG000033920.
HOVERGEN	HBG097461.
InParanoid	Q16671.
KO	K04672.
OMA	LTAECVQ.
OrthoDB	EOG4SQWWM.
PhylomeDB	Q16671.
Enzyme and pathway databases
BRENDA	2.7.10.2. 2681.
SignaLink	Q16671.
Gene expression databases
ArrayExpress	Q16671.
Bgee	Q16671.
CleanEx	HS_AMHR2.
Genevestigator	Q16671.
GermOnline	ENSG00000135409. Homo sapiens.
Family and domain databases
InterPro	IPR000472. Activin_rcpt. IPR015771. Anti-muellerian_hrmn_rcpt_II. IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. [Graphical view]
PANTHER	PTHR23255:SF4. PTHR23255:SF4. 1 hit.
Pfam	PF01064. Activin_recp. 1 hit. PF00069. Pkinase. 1 hit. [Graphical view]
PIRSF	PIRSF037392. AMHRII. 1 hit.
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. False negative. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. False negative. [Graphical view]
ProtoNet	Search...
Other
DrugBank	DB00171. Adenosine triphosphate.
GenomeRNAi	269.
NextBio	1057.
SOURCE	Search...

Entry information

Entry name

AMHR2_HUMAN

Accession

Primary (citable) accession number: Q16671
Secondary accession number(s): A0AVE1 , B9EGB7, E9PGD2, F8W1D2, Q13762, Q647K2

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	November 1, 1996
Last modified:	May 29, 2013
This is version 138 of the entry and version 1 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.