Protein phosphatase 1 regulatory subunit 12A

Preferred order of sections

Names and origin

Protein names

Recommended name:
Protein phosphatase 1 regulatory subunit 12A

Alternative name(s):
MBSP
Myosin phosphatase-targeting subunit 1
Short name=Myosin phosphatase target subunit 1
Protein phosphatase myosin-binding subunit
Protein phosphatase subunit 1M
Short name=PP-1M
Serine/threonine protein phosphatase PP1 smooth muscle regulatory subunit M110

Gene names

Name:	Ppp1r12a
Synonyms:	Mbs, Mypt1

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	1032 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Key regulator of protein phosphatase 1C (PPP1C). Mediates binding to myosin. As part of the PPP1C complex, involved in dephosphorylation of PLK1. Capable of inhibiting HIF1AN-dependent suppression of HIF1A activity By similarity. Ref.2
Subunit structure	PP1 comprises a catalytic subunit, PPP1CA, PPP1CB or PPP1CC, and one or several targeting or regulatory subunits. PPP1R12A mediates binding to myosin. Binds PPP1R12B, ROCK1 and IL16. Interacts with PPP1CB; the interaction is direct. Interacts (when phosphorylated at Ser-445, Ser-472 and Ser-912) with 14-3-3 By similarity. Interacts with ARHA and CIT. Interacts directly with PRKG1. Non-covalent dimer of 2 dimers; PRKG1-PRKG1 and PPP1R12A-PPP1R12A By similarity. Interacts with SMTNL1 By similarity. Interacts with ROCK1 and ROCK2. Interacts with ZIPK/DAPK3 By similarity. Interacts with RAF1 By similarity. Interacts with HIF1AN By similarity. Ref.4 Ref.5 Ref.9
Subcellular location	Cytoplasm By similarity. Note: Along actomyosin filaments and stress fibers By similarity.
Tissue specificity	Smooth muscle. Detected in aorta, portal vein, stomach, intestine, bladder and lung. Ref.3
Domain	Heterotetramerization is mediated by the interaction between a coiled-coil of PRKG1 and the leucine/isoleucine zipper of PPP1R12A/MBS, the myosin-binding subunit of the myosin phosphatase By similarity. The KVKF motif mediates interaction with PPP1CB By similarity.
Post-translational modification	Phosphorylated on upon DNA damage, probably by ATM or ATR By similarity. Phosphorylated by CIT (Rho-associated kinase). Phosphorylated cooperatively by ROCK1 and CDC42BP on Thr-697. In vitro, phosphorylation of Ser-696 by PKA and PKG appears to prevent phosphorylation of the inhibitory site Thr-697, probably mediated by PRKG1 By similarity. Phosphorylated on upon DNA damage, probably by ATM or ATR By similarity. Phosphorylated by CIT (Rho-associated kinase). Phosphorylated cooperatively by ROCK1 and CDC42BP on Thr-697. May be phosphorylated at Thr-697 by DMPK; may inhibit the myosin phosphatase activity. Phosphorylated at Ser-473 by CDK1 during mitosis, creating docking sites for the POLO box domains of PLK1. Subsequently, PLK1 binds and phosphorylates PPP1R12A By similarity. Ref.4 Ref.5 Ref.6 Ref.9
Sequence similarities	Contains 6 ANK repeats.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing
Domain	ANK repeat Repeat
PTM	Hydroxylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	centrosome organization Inferred from sequence or structural similarity. Source: UniProtKB mitosis Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of transcription from RNA polymerase II promoter Inferred from sequence or structural similarity. Source: UniProtKB protein dephosphorylation Inferred from sequence or structural similarity. Source: UniProtKB regulation of cell adhesion Inferred from sequence or structural similarity. Source: UniProtKB regulation of myosin-light-chain-phosphatase activity Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	PTW/PP1 phosphatase complex Inferred from sequence or structural similarity. Source: UniProtKB centrosome Inferred from sequence or structural similarity. Source: UniProtKB cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell kinetochore Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	14-3-3 protein binding Inferred from sequence or structural similarity. Source: UniProtKB enzyme inhibitor activity Inferred from sequence or structural similarity. Source: UniProtKB phosphatase regulator activity Inferred from sequence or structural similarity. Source: UniProtKB phosphoprotein phosphatase activity Inferred from direct assay Ref.2. Source: RGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NF2	P35240	2	EBI-918263,EBI-1014472	From a different organism.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select] Note: Additional isoforms seem to exist.

Isoform 1 (identifier: Q10728-1) 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: Q10728-2) The sequence of this isoform differs from the canonical sequence as follows: 608-667: Missing.

Isoform 3 (identifier: Q10728-3) The sequence of this isoform differs from the canonical sequence as follows: 552-607: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1032

1032

Protein phosphatase 1 regulatory subunit 12A

PRO_0000067027

Regions

Repeat

39 – 68

30

ANK 1

Repeat

72 – 101

30

ANK 2

Repeat

105 – 134

30

ANK 3

Repeat

138 – 164

27

ANK 4

Repeat

198 – 227

30

ANK 5

Repeat

231 – 260

30

ANK 6

Region

683 – 866

184

Interaction with ROCK2

Motif

35 – 38

4

KVKF motif

Amino acid modifications

Modified residue

67

1

(3S)-3-hydroxyasparagine; by HIF1AN By similarity

Modified residue

100

1

(3S)-3-hydroxyasparagine; by HIF1AN By similarity

Modified residue

226

1

(3S)-3-hydroxyasparagine; by HIF1AN By similarity

Modified residue

299

1

Phosphoserine By similarity

Modified residue

422

1

Phosphoserine By similarity

Modified residue

432

1

Phosphoserine By similarity

Modified residue

443

1

Phosphothreonine By similarity

Modified residue

445

1

Phosphoserine; by NUAK1 By similarity

Modified residue

472

1

Phosphoserine; by NUAK1 By similarity

Modified residue

473

1

Phosphoserine; by CDK1 By similarity

Modified residue

477

1

Phosphoserine By similarity

Modified residue

507

1

Phosphoserine Ref.8

Modified residue

508

1

Phosphothreonine Ref.8

Modified residue

509

1

Phosphoserine Ref.8

Modified residue

566

1

Phosphoserine Ref.8

Modified residue

569

1

Phosphoserine Ref.8

Modified residue

601

1

Phosphoserine By similarity

Modified residue

669

1

Phosphoserine By similarity

Modified residue

693

1

Phosphoserine; by PKA and PKG; in vitro By similarity

Modified residue

696

1

Phosphoserine; by PKA and PKG; in vitro By similarity

Modified residue

697

1

Phosphothreonine; by ROCK1; ROCK2; CDC42BP; ZIPK/DAPK3 and RAF1 Ref.5 Ref.6

Modified residue

854

1

Phosphoserine; by ROCK2 Ref.5

Modified residue

864

1

Phosphoserine By similarity

Modified residue

873

1

Phosphoserine By similarity

Modified residue

912

1

Phosphoserine; by NUAK1 Probable

Natural variations

Alternative sequence

552 – 607

56

Missing in isoform 3.

VSP_009255

Alternative sequence

608 – 667

60

Missing in isoform 2.

VSP_009254

Experimental info

Sequence conflict

11

1

N → R in AAA92961. Ref.2

Sequence conflict

316

1

T → N in AAA92961. Ref.2

Sequence conflict

424

1

K → E in AAA92961. Ref.2

Sequence conflict

579

1

A → P in AAA92961. Ref.2

Sequence conflict

682

1

Q → H in AAA92961. Ref.2

Sequences

Sequence		Length	Mass (Da)
Isoform 1 [UniParc]. Last modified January 16, 2004. Version 2. Checksum: 43B9FC1569CD5DDB Show »	FASTA	1,032	115,283
10 20 30 40 50 60 MKMADAKQKR NEQLKRWIGS ETDLEPPVVK RQKTKVKFDD GAVFLAACSS GDTDEVLKLL 70 80 90 100 110 120 HRGADINYAN VDGLTALHQA CIDDNVDMVK FLVENGANIN QPDNEGWIPL HAAASCGYLD 130 140 150 160 170 180 IAEFLIGQGA HVGAVNSEGD TPLDIAEEEA MEELLQNEVN RQGVDIEAAR KEEERIMLRD 190 200 210 220 230 240 ARQWLNSGHI SDVRHAKSGG TALHVAAAKG YTEVLKLLIQ AGYDVNIKDY DGWTPLHAAA 250 260 270 280 290 300 HWGKEEACRI LVDNLCDMET VNKVGQTAFD VADEDILGYL EELQKKQNLL HSEKRDKKSP 310 320 330 340 350 360 LIESTANMEN NQPQKTFKNK ETLIIEPEKN ASRIESLEQE KADEEEEGKK DESSCSSEED 370 380 390 400 410 420 EEDDSESEAE TDKTKPMASV TNAHTASTQA APAAVTTPTL SSNQGTPTSP VKKFPTSTTK 430 440 450 460 470 480 ISPKEEERKD ESPASWRLGL RKTGSYGALA EITASKEAQK EKDTAGVIRS ASSPRLSSSL 490 500 510 520 530 540 DNKEKEKDNK GTRLAYVAPT IPRRLGSTSD IEEKENRESS NLRTSSSYTR RKWEDDLKKN 550 560 570 580 590 600 SSINEGSTYH RSCSFGRRQD DLISCSVPST TSTPTVTSAA GLQKSFLSST STTAKTPPGS 610 620 630 640 650 660 SPAGTQSSTS NRLWAEDSTE KEKDSAPTAA TILVAPTVVS AAASSTTALT TTTAGTLSST 670 680 690 700 710 720 SEVRERRRSY LTPVRDEESE SQRKARSRQA RQSRRSTQGV TLTDLQEAEK TIGRSRSTRT 730 740 750 760 770 780 REQENEEKDK EEKEKQDKEK QEEKKESEVS REDEYKQKYS RTYDETYARY RPVSTSSSST 790 800 810 820 830 840 PSSSSLSTLG SSLYASSQLN RPNSLVGITS AYSRGLTKDN EREGEKKEEE KEGEDKSQPK 850 860 870 880 890 900 SIRERRRPRE KRRSTGVSFW TQDSDENEQE RQSDTEDGSS KRDTQTDSVS RYDSSSTSSS 910 920 930 940 950 960 DRYDSLLGRS ASYSYLEERK PYGSRLEKDD STDFKKLYEQ ILAENEKLKA QLHDTNMELT 970 980 990 1000 1010 1020 DLKLQLEKAT QRQERFADRS LLEMEKRERR ALERRISEME EELKMLPDLK ADNQRLKDEN 1030 GALIRVISKL SK « Hide
Isoform 2 [UniParc]. Checksum: C9C80CD420FCE751 Show »	FASTA	972	109,116
10 20 30 40 50 60 MKMADAKQKR NEQLKRWIGS ETDLEPPVVK RQKTKVKFDD GAVFLAACSS GDTDEVLKLL 70 80 90 100 110 120 HRGADINYAN VDGLTALHQA CIDDNVDMVK FLVENGANIN QPDNEGWIPL HAAASCGYLD 130 140 150 160 170 180 IAEFLIGQGA HVGAVNSEGD TPLDIAEEEA MEELLQNEVN RQGVDIEAAR KEEERIMLRD 190 200 210 220 230 240 ARQWLNSGHI SDVRHAKSGG TALHVAAAKG YTEVLKLLIQ AGYDVNIKDY DGWTPLHAAA 250 260 270 280 290 300 HWGKEEACRI LVDNLCDMET VNKVGQTAFD VADEDILGYL EELQKKQNLL HSEKRDKKSP 310 320 330 340 350 360 LIESTANMEN NQPQKTFKNK ETLIIEPEKN ASRIESLEQE KADEEEEGKK DESSCSSEED 370 380 390 400 410 420 EEDDSESEAE TDKTKPMASV TNAHTASTQA APAAVTTPTL SSNQGTPTSP VKKFPTSTTK 430 440 450 460 470 480 ISPKEEERKD ESPASWRLGL RKTGSYGALA EITASKEAQK EKDTAGVIRS ASSPRLSSSL 490 500 510 520 530 540 DNKEKEKDNK GTRLAYVAPT IPRRLGSTSD IEEKENRESS NLRTSSSYTR RKWEDDLKKN 550 560 570 580 590 600 SSINEGSTYH RSCSFGRRQD DLISCSVPST TSTPTVTSAA GLQKSFLSST STTAKTPPGS 610 620 630 640 650 660 SPAGTQSRSY LTPVRDEESE SQRKARSRQA RQSRRSTQGV TLTDLQEAEK TIGRSRSTRT 670 680 690 700 710 720 REQENEEKDK EEKEKQDKEK QEEKKESEVS REDEYKQKYS RTYDETYARY RPVSTSSSST 730 740 750 760 770 780 PSSSSLSTLG SSLYASSQLN RPNSLVGITS AYSRGLTKDN EREGEKKEEE KEGEDKSQPK 790 800 810 820 830 840 SIRERRRPRE KRRSTGVSFW TQDSDENEQE RQSDTEDGSS KRDTQTDSVS RYDSSSTSSS 850 860 870 880 890 900 DRYDSLLGRS ASYSYLEERK PYGSRLEKDD STDFKKLYEQ ILAENEKLKA QLHDTNMELT 910 920 930 940 950 960 DLKLQLEKAT QRQERFADRS LLEMEKRERR ALERRISEME EELKMLPDLK ADNQRLKDEN 970 GALIRVISKL SK « Hide
Isoform 3 [UniParc]. Checksum: 9C25C0117ED89661 Show »	FASTA	976	109,720
10 20 30 40 50 60 MKMADAKQKR NEQLKRWIGS ETDLEPPVVK RQKTKVKFDD GAVFLAACSS GDTDEVLKLL 70 80 90 100 110 120 HRGADINYAN VDGLTALHQA CIDDNVDMVK FLVENGANIN QPDNEGWIPL HAAASCGYLD 130 140 150 160 170 180 IAEFLIGQGA HVGAVNSEGD TPLDIAEEEA MEELLQNEVN RQGVDIEAAR KEEERIMLRD 190 200 210 220 230 240 ARQWLNSGHI SDVRHAKSGG TALHVAAAKG YTEVLKLLIQ AGYDVNIKDY DGWTPLHAAA 250 260 270 280 290 300 HWGKEEACRI LVDNLCDMET VNKVGQTAFD VADEDILGYL EELQKKQNLL HSEKRDKKSP 310 320 330 340 350 360 LIESTANMEN NQPQKTFKNK ETLIIEPEKN ASRIESLEQE KADEEEEGKK DESSCSSEED 370 380 390 400 410 420 EEDDSESEAE TDKTKPMASV TNAHTASTQA APAAVTTPTL SSNQGTPTSP VKKFPTSTTK 430 440 450 460 470 480 ISPKEEERKD ESPASWRLGL RKTGSYGALA EITASKEAQK EKDTAGVIRS ASSPRLSSSL 490 500 510 520 530 540 DNKEKEKDNK GTRLAYVAPT IPRRLGSTSD IEEKENRESS NLRTSSSYTR RKWEDDLKKN 550 560 570 580 590 600 SSINEGSTYH RSTSNRLWAE DSTEKEKDSA PTAATILVAP TVVSAAASST TALTTTTAGT 610 620 630 640 650 660 LSSTSEVRER RRSYLTPVRD EESESQRKAR SRQARQSRRS TQGVTLTDLQ EAEKTIGRSR 670 680 690 700 710 720 STRTREQENE EKDKEEKEKQ DKEKQEEKKE SEVSREDEYK QKYSRTYDET YARYRPVSTS 730 740 750 760 770 780 SSSTPSSSSL STLGSSLYAS SQLNRPNSLV GITSAYSRGL TKDNEREGEK KEEEKEGEDK 790 800 810 820 830 840 SQPKSIRERR RPREKRRSTG VSFWTQDSDE NEQERQSDTE DGSSKRDTQT DSVSRYDSSS 850 860 870 880 890 900 TSSSDRYDSL LGRSASYSYL EERKPYGSRL EKDDSTDFKK LYEQILAENE KLKAQLHDTN 910 920 930 940 950 960 MELTDLKLQL EKATQRQERF ADRSLLEMEK RERRALERRI SEMEEELKML PDLKADNQRL 970 KDENGALIRV ISKLSK « Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of cDNA encoding the 110 kDa and 21 kDa regulatory subunits of smooth muscle protein phosphatase 1M." Chen Y.H., Chen M.X., Alessi D.R., Campbell D.G., Shanahan C., Cohen P., Cohen P.T.W. FEBS Lett. 356:51-55(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). Tissue: Aorta.
[2]	"Molecular cloning and functional expression of a recombinant 72.5 kDa fragment of the 110 kDa regulatory subunit of smooth muscle protein phosphatase 1M." Haystead C.M.M., Gailly P., Somlyo A.P., Somlyo A.V., Haystead T.A.J. FEBS Lett. 377:123-127(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 11-728 (ISOFORM 2), FUNCTION. Strain: Wistar. Tissue: Kidney.
[3]	"A myosin phosphatase targeting subunit isoform transition defines a smooth muscle developmental phenotypic switch." Dirksen W.P., Vladic F., Fisher S.A. Am. J. Physiol. 278:C589-C600(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 490-665 (ISOFORM 1), TISSUE SPECIFICITY, ALTERNATIVE SPLICING. Strain: Sprague-Dawley.
[4]	"Regulation of myosin phosphatase by Rho and Rho-associated kinase (Rho-kinase)." Kimura K., Ito M., Amano M., Chihara K., Fukata Y., Nakafuku M., Yamamori B., Feng J., Nakano T., Okawa K., Iwamatsu A., Kaibuchi K. Science 273:245-248(1996) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION, INTERACTION WITH ARHA AND CIT.
[5]	"Phosphorylation of myosin-binding subunit (MBS) of myosin phosphatase by Rho-kinase in vivo." Kawano Y., Fukata Y., Oshiro N., Amano M., Nakamura T., Ito M., Matsumura F., Inagaki M., Kaibuchi K. J. Cell Biol. 147:1023-1038(1999) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT THR-697 AND SER-854, INTERACTION WITH ROCK1.
[6]	"Zipper-interacting protein kinase induces Ca(2+)-free smooth muscle contraction via myosin light chain phosphorylation." Niiro N., Ikebe M. J. Biol. Chem. 276:29567-29574(2001) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT THR-697 BY ZIPK/DAPK3.
[7]	"Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-MS/MS." Moser K., White F.M. J. Proteome Res. 5:98-104(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-912, MASS SPECTROMETRY. Strain: Fischer. Tissue: Liver.
[8]	"Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites." Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A. Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-507; THR-508; SER-509; SER-566 AND SER-569, MASS SPECTROMETRY. Tissue: Renal collecting duct.
[9]	"ROCK isoform regulation of myosin phosphatase and contractility in vascular smooth muscle cells." Wang Y., Zheng X.R., Riddick N., Bryden M., Baur W., Zhang X., Surks H.K. Circ. Res. 104:531-540(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION, INTERACTION WITH ROCK1 AND ROCK2.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	S74907 mRNA. Translation: AAB32731.1. U50185 mRNA. Translation: AAA92961.1. AF110176 Genomic DNA. Translation: AAD34326.1.
IPI	IPI00211695. IPI00400680. IPI00400681.
PIR	S68418.
RefSeq	NP_446342.1. NM_053890.1.
UniGene	Rn.162937.
3D structure databases
ProteinModelPortal	Q10728.
SMR	Q10728. Positions 1-291.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q10728. 3 interactions.
STRING	10116.ENSRNOP00000062297.
PTM databases
PhosphoSite	Q10728.
Proteomic databases
PaxDb	Q10728.
PRIDE	Q10728.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	116670.
KEGG	rno:116670.
UCSC	RGD:620013. rat.
Organism-specific databases
CTD	4659.
RGD	620013. Ppp1r12a.
Phylogenomic databases
eggNOG	COG0666.
HOGENOM	HOG000290648.
HOVERGEN	HBG052561.
InParanoid	Q10728.
KO	K06270.
OrthoDB	EOG4R7V9D.
Gene expression databases
ArrayExpress	Q10728.
Genevestigator	Q10728.
GermOnline	ENSRNOG00000004925. Rattus norvegicus.
Family and domain databases
Gene3D	1.25.40.20. 1 hit.
InterPro	IPR002110. Ankyrin_rpt. IPR020683. Ankyrin_rpt-contain_dom. IPR017401. Pase-1_reg_su_12A/B/C_euk. [Graphical view]
Pfam	PF12796. Ank_2. 2 hits. [Graphical view]
PIRSF	PIRSF038141. PP1_12ABC_vert. 1 hit.
PRINTS	PR01415. ANKYRIN.
SMART	SM00248. ANK. 6 hits. [Graphical view]
SUPFAM	SSF48403. ANK. 1 hit.
PROSITE	PS50297. ANK_REP_REGION. 1 hit. PS50088. ANK_REPEAT. 4 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	619487.

Entry information

Entry name

MYPT1_RAT

Accession

Primary (citable) accession number: Q10728
Secondary accession number(s): Q62937, Q9WU33

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	January 16, 2004
Last modified:	April 3, 2013
This is version 111 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Alternative products

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents