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O14974

- MYPT1_HUMAN

UniProt

O14974 - MYPT1_HUMAN

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Protein
Protein phosphatase 1 regulatory subunit 12A
Gene
PPP1R12A, MBS, MYPT1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.3 Publications

GO - Molecular functioni

  1. 14-3-3 protein binding Source: UniProtKB
  2. enzyme inhibitor activity Source: UniProtKB
  3. phosphatase regulator activity Source: UniProtKB
  4. protein binding Source: UniProtKB
  5. protein kinase binding Source: UniProtKB
  6. signal transducer activity Source: ProtInc

GO - Biological processi

  1. G2/M transition of mitotic cell cycle Source: Reactome
  2. centrosome organization Source: UniProtKB
  3. mitotic cell cycle Source: Reactome
  4. mitotic nuclear division Source: UniProtKB
  5. negative regulation of catalytic activity Source: UniProtKB
  6. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  7. protein dephosphorylation Source: UniProtKB
  8. regulation of cell adhesion Source: UniProtKB
  9. regulation of myosin-light-chain-phosphatase activity Source: UniProtKB
  10. regulation of nucleocytoplasmic transport Source: Ensembl
  11. signal transduction Source: GOC
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_160315. Regulation of PLK1 Activity at G2/M Transition.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein phosphatase 1 regulatory subunit 12A
Alternative name(s):
Myosin phosphatase-targeting subunit 1
Short name:
Myosin phosphatase target subunit 1
Protein phosphatase myosin-binding subunit
Gene namesi
Synonyms:MBS, MYPT1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:7618. PPP1R12A.

Subcellular locationi

Cytoplasm
Note: Along actomyosin filaments and stress fibers.2 Publications

GO - Cellular componenti

  1. PTW/PP1 phosphatase complex Source: UniProtKB
  2. actin cytoskeleton Source: HPA
  3. centrosome Source: UniProtKB
  4. contractile fiber Source: UniProtKB
  5. cytoplasm Source: HPA
  6. kinetochore Source: UniProtKB
  7. nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi445 – 4451S → A: Abolishes phosphorylation by NUAK1 and interaction with 14-3-3; when associated with A-472 and A-910.
Mutagenesisi472 – 4721S → A: Abolishes phosphorylation by NUAK1 and interaction with 14-3-3; when associated with A-445 and A-910.
Mutagenesisi473 – 4731S → A: Abolishes binding to the POLO box domains of PLK1. 1 Publication
Mutagenesisi910 – 9101S → A: Abolishes phosphorylation by NUAK1 and interaction with 14-3-3; when associated with A-445 and A-472.
Mutagenesisi1007 – 10071L → A: Loss of binding to PRKG1; when associated with A-1014. 1 Publication
Mutagenesisi1014 – 10141L → A: Loss of binding to PRKG1; when associated with A-1007. 1 Publication
Mutagenesisi1021 – 10211L → A: Loss of binding to PRKG1; when associated with A-1028. 1 Publication
Mutagenesisi1028 – 10281L → A: Loss of binding to PRKG1; when associated with A-1021. 1 Publication

Organism-specific databases

PharmGKBiPA33617.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10301030Protein phosphatase 1 regulatory subunit 12A
PRO_0000067025Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei67 – 671(3S)-3-hydroxyasparagine; by HIF1AN; partial1 Publication
Modified residuei100 – 1001(3S)-3-hydroxyasparagine; by HIF1AN; partial1 Publication
Modified residuei226 – 2261(3S)-3-hydroxyasparagine; by HIF1AN; partial1 Publication
Modified residuei299 – 2991Phosphoserine3 Publications
Modified residuei422 – 4221Phosphoserine3 Publications
Modified residuei432 – 4321Phosphoserine1 Publication
Modified residuei443 – 4431Phosphothreonine By similarity
Modified residuei445 – 4451Phosphoserine; by NUAK13 Publications
Modified residuei472 – 4721Phosphoserine; by NUAK11 Publication
Modified residuei473 – 4731Phosphoserine; by CDK11 Publication
Modified residuei477 – 4771Phosphoserine1 Publication
Modified residuei507 – 5071Phosphoserine2 Publications
Modified residuei601 – 6011Phosphoserine1 Publication
Modified residuei668 – 6681Phosphoserine By similarity
Modified residuei692 – 6921Phosphoserine; by PKA and PKG; in vitro
Modified residuei695 – 6951Phosphoserine; by PKA and PKG; in vitro
Modified residuei696 – 6961Phosphothreonine; by ROCK1, ROCK2, CDC42BP, ZIPK/DAPK3 and RAF15 Publications
Modified residuei852 – 8521Phosphoserine; by ROCK21 Publication
Modified residuei862 – 8621Phosphoserine1 Publication
Modified residuei871 – 8711Phosphoserine3 Publications
Modified residuei910 – 9101Phosphoserine; by NUAK11 Publication
Modified residuei995 – 9951Phosphoserine By similarity

Post-translational modificationi

Phosphorylated by CIT (Rho-associated kinase) By similarity. Phosphorylated cooperatively by ROCK1 and CDC42BP on Thr-696. Phosphorylated on upon DNA damage, probably by ATM or ATR. In vitro, phosphorylation of Ser-695 by PKA and PKG appears to prevent phosphorylation of the inhibitory site Thr-696, probably mediated by PRKG1. Phosphorylation at Ser-445, Ser-472 and Ser-910 by NUAK1 promotes interaction with 14-3-3, leading to inhibit interaction with myosin light chain MLC2, preventing dephosphorylation of MLC2. May be phosphorylated at Thr-696 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.16 Publications

Keywords - PTMi

Hydroxylation, Phosphoprotein

Proteomic databases

MaxQBiO14974.
PaxDbiO14974.
PRIDEiO14974.

2D gel databases

OGPiO14974.

PTM databases

PhosphoSiteiO14974.

Expressioni

Tissue specificityi

Expressed in striated muscles, specifically in type 2a fibers (at protein level).1 Publication

Developmental stagei

Induced by 2-fold during pregnancy, including in abdominus rectus muscle.1 Publication

Gene expression databases

ArrayExpressiO14974.
BgeeiO14974.
CleanExiHS_PPP1R12A.
GenevestigatoriO14974.

Organism-specific databases

HPAiHPA039443.
HPA041296.

Interactioni

Subunit structurei

PP1 comprises a catalytic subunit, PPP1CA, PPP1CB or PPP1CC, and one or several targeting or regulatory subunits. PPP1R12A mediates binding to myosin. Interacts with ARHA and CIT By similarity. Binds PPP1R12B, ROCK1 and IL16. Interacts directly with PRKG1. Non-covalent dimer of 2 dimers; PRKG1-PRKG1 and PPP1R12A-PPP1R12A. Interacts with SMTNL1 By similarity. Interacts with PPP1CB; the interaction is direct. Interacts (when phosphorylated at Ser-445, Ser-472 and Ser-910) with 14-3-3. Interacts with ROCK1 and ROCK2. Interacts with isoform 1 and isoform 2 of ZIPK/DAPK3. Interacts with RAF1. Interacts with HIF1AN.12 Publications

Protein-protein interaction databases

BioGridi110742. 53 interactions.
DIPiDIP-33186N.
IntActiO14974. 27 interactions.
MINTiMINT-195983.
STRINGi9606.ENSP00000261207.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi659 – 66810
Helixi674 – 69623
Turni699 – 7013
Helixi702 – 7109

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KJYNMR-A658-714[»]
ProteinModelPortaliO14974.
SMRiO14974. Positions 1-291, 658-714.

Miscellaneous databases

EvolutionaryTraceiO14974.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati39 – 6830ANK 1
Add
BLAST
Repeati72 – 10130ANK 2
Add
BLAST
Repeati105 – 13430ANK 3
Add
BLAST
Repeati138 – 16427ANK 4
Add
BLAST
Repeati198 – 22730ANK 5
Add
BLAST
Repeati231 – 26030ANK 6
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni682 – 864183Interaction with ROCK2
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi35 – 384KVKF motif

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi519 – 660142Ser/Thr-rich
Add
BLAST
Compositional biasi721 – 75333Glu/Lys-rich
Add
BLAST
Compositional biasi773 – 79523Ser-rich
Add
BLAST

Domaini

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.1 Publication
The KVKF motif mediates interaction with PPP1CB.1 Publication

Sequence similaritiesi

Contains 6 ANK repeats.

Keywords - Domaini

ANK repeat, Repeat

Phylogenomic databases

eggNOGiCOG0666.
HOGENOMiHOG000290648.
HOVERGENiHBG052561.
InParanoidiO14974.
KOiK06270.
OMAiTDKQTTT.
OrthoDBiEOG7060Q5.
PhylomeDBiO14974.
TreeFamiTF105543.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR017401. Pase-1_reg_su_12A/B/C_euk.
[Graphical view]
PfamiPF00023. Ank. 4 hits.
[Graphical view]
PIRSFiPIRSF038141. PP1_12ABC_vert. 1 hit.
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 6 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 4 hits.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O14974-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MKMADAKQKR NEQLKRWIGS ETDLEPPVVK RQKTKVKFDD GAVFLAACSS     50
GDTDEVLKLL HRGADINYAN VDGLTALHQA CIDDNVDMVK FLVENGANIN 100
QPDNEGWIPL HAAASCGYLD IAEFLIGQGA HVGAVNSEGD TPLDIAEEEA 150
MEELLQNEVN RQGVDIEAAR KEEERIMLRD ARQWLNSGHI NDVRHAKSGG 200
TALHVAAAKG YTEVLKLLIQ AGYDVNIKDY DGWTPLHAAA HWGKEEACRI 250
LVDNLCDMEM VNKVGQTAFD VADEDILGYL EELQKKQNLL HSEKRDKKSP 300
LIESTANMDN NQSQKTFKNK ETLIIEPEKN ASRIESLEQE KVDEEEEGKK 350
DESSCSSEED EEDDSESEAE TDKTKPLASV TNANTSSTQA APVAVTTPTV 400
SSGQATPTSP IKKFPTTATK ISPKEEERKD ESPATWRLGL RKTGSYGALA 450
EITASKEGQK EKDTAGVTRS ASSPRLSSSL DNKEKEKDSK GTRLAYVAPT 500
IPRRLASTSD IEEKENRDSS SLRTSSSYTR RKWEDDLKKN SSVNEGSTYH 550
KSCSFGRRQD DLISSSVPST TSTPTVTSAA GLQKSLLSST STTTKITTGS 600
SSAGTQSSTS NRLWAEDSTE KEKDSVPTAV TIPVAPTVVN AAASTTTLTT 650
TTAGTVSSTT EVRERRRSYL TPVRDEESES QRKARSRQAR QSRRSTQGVT 700
LTDLQEAEKT IGRSRSTRTR EQENEEKEKE EKEKQDKEKQ EEKKESETSR 750
EDEYKQKYSR TYDETYQRYR PVSTSSSTTP SSSLSTMSSS LYASSQLNRP 800
NSLVGITSAY SRGITKENER EGEKREEEKE GEDKSQPKSI RERRRPREKR 850
RSTGVSFWTQ DSDENEQEQQ SDTEEGSNKK ETQTDSISRY ETSSTSAGDR 900
YDSLLGRSGS YSYLEERKPY SSRLEKDDST DFKKLYEQIL AENEKLKAQL 950
HDTNMELTDL KLQLEKATQR QERFADRSLL EMEKRERRAL ERRISEMEEE 1000
LKMLPDLKAD NQRLKDENGA LIRVISKLSK 1030
Length:1,030
Mass (Da):115,281
Last modified:January 1, 1998 - v1
Checksum:iEA43E9BFF5DA08FF
GO
Isoform 2 (identifier: O14974-2) [UniParc]FASTAAdd to Basket

Also known as: Myosin phosphatase target subunit 1 variant

The sequence of this isoform differs from the canonical sequence as follows:
     935-969: Missing.

Note: No experimental confirmation available.

Show »
Length:995
Mass (Da):111,185
Checksum:i67E4FF32DDCCBD78
GO
Isoform 3 (identifier: O14974-3) [UniParc]FASTAAdd to Basket

Also known as: Myosin phosphatase target subunit 1 variant 2

The sequence of this isoform differs from the canonical sequence as follows:
     552-607: Missing.

Show »
Length:974
Mass (Da):109,728
Checksum:iD211212480EF48DE
GO
Isoform 4 (identifier: O14974-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     608-666: Missing.

Note: No experimental confirmation available.

Show »
Length:971
Mass (Da):109,104
Checksum:i351DE33C5EB3C276
GO
Isoform 5 (identifier: O14974-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-87: Missing.

Note: No experimental confirmation available.

Show »
Length:943
Mass (Da):105,641
Checksum:i0C4751FF983E49F9
GO

Sequence cautioni

The sequence AAH47898.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
The sequence AAH92481.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti116 – 1161C → W.
Corresponds to variant rs12582646 [ dbSNP | Ensembl ].
VAR_038949
Natural varianti305 – 3051T → P.
Corresponds to variant rs2596781 [ dbSNP | Ensembl ].
VAR_038950
Natural varianti734 – 7341K → N.
Corresponds to variant rs12820960 [ dbSNP | Ensembl ].
VAR_038951

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 8787Missing in isoform 5.
VSP_045079Add
BLAST
Alternative sequencei552 – 60756Missing in isoform 3.
VSP_009251Add
BLAST
Alternative sequencei608 – 66659Missing in isoform 4.
VSP_009252Add
BLAST
Alternative sequencei935 – 96935Missing in isoform 2.
VSP_009253Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21K → Q in AAI11753. 1 Publication
Sequence conflicti322 – 3221T → A in AAH92481. 1 Publication
Sequence conflicti350 – 3501K → R in BAG63921. 1 Publication
Sequence conflicti653 – 6531A → V in AAH92481. 1 Publication
Sequence conflicti690 – 6901R → G in AAQ88438. 1 Publication
Sequence conflicti783 – 7831S → P in AAQ88438. 1 Publication
Sequence conflicti930 – 9301T → P in AAQ88438. 1 Publication
Sequence conflicti959 – 9591D → G in AAQ88438. 1 Publication
Sequence conflicti1027 – 10271K → Q in AAQ88438. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D87930 mRNA. Translation: BAA22378.1.
AY380574 mRNA. Translation: AAQ88438.1.
AF458589 mRNA. Translation: AAM49717.1.
AK302692 mRNA. Translation: BAG63921.1.
AC018476 Genomic DNA. No translation available.
AC073569 Genomic DNA. No translation available.
AC074270 Genomic DNA. No translation available.
BC047898 mRNA. Translation: AAH47898.1. Sequence problems.
BC092481 mRNA. Translation: AAH92481.1. Sequence problems.
BC111752 mRNA. Translation: AAI11753.1.
AB042196 Genomic DNA. Translation: BAB39107.1.
CCDSiCCDS44947.1. [O14974-1]
CCDS44948.1. [O14974-5]
CCDS58259.1. [O14974-3]
CCDS58260.1. [O14974-2]
RefSeqiNP_001137357.1. NM_001143885.1. [O14974-1]
NP_001137358.1. NM_001143886.1. [O14974-5]
NP_001231919.1. NM_001244990.1. [O14974-2]
NP_001231921.1. NM_001244992.1. [O14974-3]
NP_002471.1. NM_002480.2. [O14974-1]
UniGeneiHs.49582.

Genome annotation databases

EnsembliENST00000261207; ENSP00000261207; ENSG00000058272. [O14974-1]
ENST00000437004; ENSP00000416769; ENSG00000058272. [O14974-2]
ENST00000450142; ENSP00000389168; ENSG00000058272. [O14974-1]
ENST00000546369; ENSP00000449514; ENSG00000058272. [O14974-5]
ENST00000550107; ENSP00000446855; ENSG00000058272. [O14974-3]
GeneIDi4659.
KEGGihsa:4659.
UCSCiuc001syz.3. human. [O14974-1]
uc001sza.3. human. [O14974-3]
uc001szb.3. human. [O14974-2]
uc001szc.2. human. [O14974-4]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D87930 mRNA. Translation: BAA22378.1 .
AY380574 mRNA. Translation: AAQ88438.1 .
AF458589 mRNA. Translation: AAM49717.1 .
AK302692 mRNA. Translation: BAG63921.1 .
AC018476 Genomic DNA. No translation available.
AC073569 Genomic DNA. No translation available.
AC074270 Genomic DNA. No translation available.
BC047898 mRNA. Translation: AAH47898.1 . Sequence problems.
BC092481 mRNA. Translation: AAH92481.1 . Sequence problems.
BC111752 mRNA. Translation: AAI11753.1 .
AB042196 Genomic DNA. Translation: BAB39107.1 .
CCDSi CCDS44947.1. [O14974-1 ]
CCDS44948.1. [O14974-5 ]
CCDS58259.1. [O14974-3 ]
CCDS58260.1. [O14974-2 ]
RefSeqi NP_001137357.1. NM_001143885.1. [O14974-1 ]
NP_001137358.1. NM_001143886.1. [O14974-5 ]
NP_001231919.1. NM_001244990.1. [O14974-2 ]
NP_001231921.1. NM_001244992.1. [O14974-3 ]
NP_002471.1. NM_002480.2. [O14974-1 ]
UniGenei Hs.49582.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2KJY NMR - A 658-714 [» ]
ProteinModelPortali O14974.
SMRi O14974. Positions 1-291, 658-714.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110742. 53 interactions.
DIPi DIP-33186N.
IntActi O14974. 27 interactions.
MINTi MINT-195983.
STRINGi 9606.ENSP00000261207.

PTM databases

PhosphoSitei O14974.

2D gel databases

OGPi O14974.

Proteomic databases

MaxQBi O14974.
PaxDbi O14974.
PRIDEi O14974.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000261207 ; ENSP00000261207 ; ENSG00000058272 . [O14974-1 ]
ENST00000437004 ; ENSP00000416769 ; ENSG00000058272 . [O14974-2 ]
ENST00000450142 ; ENSP00000389168 ; ENSG00000058272 . [O14974-1 ]
ENST00000546369 ; ENSP00000449514 ; ENSG00000058272 . [O14974-5 ]
ENST00000550107 ; ENSP00000446855 ; ENSG00000058272 . [O14974-3 ]
GeneIDi 4659.
KEGGi hsa:4659.
UCSCi uc001syz.3. human. [O14974-1 ]
uc001sza.3. human. [O14974-3 ]
uc001szb.3. human. [O14974-2 ]
uc001szc.2. human. [O14974-4 ]

Organism-specific databases

CTDi 4659.
GeneCardsi GC12M080142.
H-InvDB HIX0010848.
HGNCi HGNC:7618. PPP1R12A.
HPAi HPA039443.
HPA041296.
MIMi 602021. gene.
neXtProti NX_O14974.
PharmGKBi PA33617.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0666.
HOGENOMi HOG000290648.
HOVERGENi HBG052561.
InParanoidi O14974.
KOi K06270.
OMAi TDKQTTT.
OrthoDBi EOG7060Q5.
PhylomeDBi O14974.
TreeFami TF105543.

Enzyme and pathway databases

Reactomei REACT_160315. Regulation of PLK1 Activity at G2/M Transition.

Miscellaneous databases

ChiTaRSi PPP1R12A. human.
EvolutionaryTracei O14974.
GeneWikii PPP1R12A.
GenomeRNAii 4659.
NextBioi 17954.
PROi O14974.
SOURCEi Search...

Gene expression databases

ArrayExpressi O14974.
Bgeei O14974.
CleanExi HS_PPP1R12A.
Genevestigatori O14974.

Family and domain databases

Gene3Di 1.25.40.20. 1 hit.
InterProi IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR017401. Pase-1_reg_su_12A/B/C_euk.
[Graphical view ]
Pfami PF00023. Ank. 4 hits.
[Graphical view ]
PIRSFi PIRSF038141. PP1_12ABC_vert. 1 hit.
PRINTSi PR01415. ANKYRIN.
SMARTi SM00248. ANK. 6 hits.
[Graphical view ]
SUPFAMi SSF48403. SSF48403. 1 hit.
PROSITEi PS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 4 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Localization of the gene coding for myosin phosphatase, target subunit 1 (MYPT1) to human chromosome 12q15-q21."
    Takahashi N., Ito M., Tanaka J., Nakano T., Kaibuchi K., Odai H., Takemura K.
    Genomics 44:150-152(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Brain and Liver.
  2. Guo J.H., Chen X.Y., Yu L.
    Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Liver.
  3. "Molecular cloning and functional analysis of a new isoform of human MYPT1."
    Xia D., Kamm K., Stull J.T.
    Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
  4. "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 5).
    Tissue: Testis.
  5. "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].
  6. "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), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-722 (ISOFORM 4).
    Tissue: Blood and Brain.
  7. "Molecular cloning and analysis of the 5'-flanking region of human MYPT1 gene."
    Machida H., Ito M., Okamoto R., Shiraki K., Isaka N., Hartshorne D.J., Nakano T.
    Biochim. Biophys. Acta 1517:424-429(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-79.
  8. "MYPT1, the targeting subunit of smooth-muscle myosin phosphatase, is a substrate for the asparaginyl hydroxylase factor inhibiting hypoxia-inducible factor (FIH)."
    Webb J.D., Muranyi A., Pugh C.W., Ratcliffe P.J., Coleman M.L.
    Biochem. J. 420:327-333(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 63-76; 95-105 AND 217-228, FUNCTION, HYDROXYLATION AT ASN-67; ASN-100 AND ASN-226 BY HIF1AN.
  9. "Regulation of myosin phosphatase by a specific interaction with cGMP-dependent protein kinase Ialpha."
    Surks H.K., Mochizuki N., Kasai Y., Georgescu S.P., Tang K.M., Ito M., Lincoln T.M., Mendelsohn M.E.
    Science 286:1583-1587(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PRKG1, PHOSPHORYLATION BY PRKG1, SUBUNIT.
  10. "Myotonic dystrophy protein kinase phosphorylates the myosin phosphatase targeting subunit and inhibits myosin phosphatase activity."
    Muranyi A., Zhang R., Liu F., Hirano K., Ito M., Epstein H.F., Hartshorne D.J.
    FEBS Lett. 493:80-84(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY DMPK.
  11. "Identification, characterization, and functional analysis of heart-specific myosin light chain phosphatase small subunit."
    Arimura T., Suematsu N., Zhou Y.-B., Nishimura J., Satoh S., Takeshita A., Kanaide H., Kimura A.
    J. Biol. Chem. 276:6073-6082(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PPP1R12B.
  12. "Rho-kinase--mediated contraction of isolated stress fibers."
    Katoh K., Kano Y., Amano M., Onishi H., Kaibuchi K., Fujiwara K.
    J. Cell Biol. 153:569-584(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-852.
  13. "Caspase-3-mediated cleavage of ROCK I induces MLC phosphorylation and apoptotic membrane blebbing."
    Sebbagh M., Renvoize C., Hamelin J., Riche N., Bertoglio J., Breard J.
    Nat. Cell Biol. 3:346-352(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ROCK1, PHOSPHORYLATION.
  14. "Phosphorylation of the myosin-binding subunit of myosin phosphatase by Raf-1 and inhibition of phosphatase activity."
    Broustas C.G., Grammatikakis N., Eto M., Dent P., Brautigan D.L., Kasid U.
    J. Biol. Chem. 277:3053-3059(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-696 BY RAF1, INTERACTION WITH RAF1.
  15. "Dimerization of cGMP-dependent protein kinase 1alpha and the myosin-binding subunit of myosin phosphatase: role of leucine zipper domains."
    Surks H.K., Mendelsohn M.E.
    Cell. Signal. 15:937-944(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, MUTAGENESIS OF LEU-1007; LEU-1014; LEU-1021 AND LEU-1028, INTERACTION WITH PRKG1.
  16. "PDZ domain-mediated interaction of interleukin-16 precursor proteins with myosin phosphatase targeting subunits."
    Bannert N., Vollhardt K., Asomuddinov B., Haag M., Koenig H., Norley S., Kurth R.
    J. Biol. Chem. 278:42190-42199(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IL16, SUBCELLULAR LOCATION.
  17. "RhoE binds to ROCK I and inhibits downstream signaling."
    Riento K., Guasch R.M., Garg R., Jin B., Ridley A.J.
    Mol. Cell. Biol. 23:4219-4229(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ROCK1, PHOSPHORYLATION.
  18. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
    Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
    Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  19. "Smooth muscle phosphatase is regulated in vivo by exclusion of phosphorylation of threonine 696 of MYPT1 by phosphorylation of Serine 695 in response to cyclic nucleotides."
    Wooldridge A.A., MacDonald J.A., Erdodi F., Ma C., Borman M.A., Hartshorne D.J., Haystead T.A.J.
    J. Biol. Chem. 279:34496-34504(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY PRKG1 ON SER-692; SER-695; THR-696 AND SER-852.
  20. "Cdc42-MRCK and Rho-ROCK signalling cooperate in myosin phosphorylation and cell invasion."
    Wilkinson S., Paterson H.F., Marshall C.J.
    Nat. Cell Biol. 7:255-261(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-696.
    Tissue: Colon.
  21. Cited for: PHOSPHORYLATION BY ZIPK/DAPK3, INTERACTION WITH ZIPK/DAPK3.
  22. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  23. "Interactions between the leucine-zipper motif of cGMP-dependent protein kinase and the C-terminal region of the targeting subunit of myosin light chain phosphatase."
    Lee E., Hayes D.B., Langsetmo K., Sundberg E.J., Tao T.C.
    J. Mol. Biol. 373:1198-1212(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PRKG1.
  24. "Myosin phosphatase-targeting subunit 1 regulates mitosis by antagonizing polo-like kinase 1."
    Yamashiro S., Yamakita Y., Totsukawa G., Goto H., Kaibuchi K., Ito M., Hartshorne D.J., Matsumura F.
    Dev. Cell 14:787-797(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-432; SER-473 AND SER-601, PHOSPHORYLATION BY PLK1, MUTAGENESIS OF SER-473.
  25. "Probing the interaction between the coiled coil leucine zipper of cGMP-dependent protein kinase Ialpha and the C terminus of the myosin binding subunit of the myosin light chain phosphatase."
    Sharma A.K., Zhou G.-P., Kupferman J., Surks H.K., Christensen E.N., Chou J.J., Mendelsohn M.E., Rigby A.C.
    J. Biol. Chem. 283:32860-32869(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PRKG1, SUBUNIT.
  26. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
    Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
    J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: T-cell.
  27. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  28. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299; SER-422; SER-445; SER-477; SER-507; THR-696; SER-862 AND SER-871, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  29. Carrascal M., Abian J.
    Submitted (JAN-2008) to UniProtKB
    Cited for: PHOSPHORYLATION AT SER-445, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: T-cell.
  30. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  31. "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.
  32. "Distinct roles for ROCK1 and ROCK2 in the regulation of keratinocyte differentiation."
    Lock F.E., Hotchin N.A.
    PLoS ONE 4:E8190-E8190(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-696.
  33. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-871, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  34. "New roles for the LKB1-NUAK pathway in controlling myosin phosphatase complexes and cell adhesion."
    Zagorska A., Deak M., Campbell D.G., Banerjee S., Hirano M., Aizawa S., Prescott A.R., Alessi D.R.
    Sci. Signal. 3:RA25-RA25(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PPP1CB AND 14-3-3, DOMAIN KVKF MOTIF, PHOSPHORYLATION AT SER-445; SER-472 AND SER-910.
  35. "Smoothelin-like 1 protein regulates myosin phosphatase-targeting subunit 1 expression during sexual development and pregnancy."
    Lontay B., Bodoor K., Weitzel D.H., Loiselle D., Fortner C., Lengyel S., Zheng D., Devente J., Hickner R., Haystead T.A.
    J. Biol. Chem. 285:29357-29366(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  36. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299; SER-422 AND SER-871, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  37. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  38. "Chelerythrine perturbs lamellar actomyosin filaments by selective inhibition of myotonic dystrophy kinase-related Cdc42-binding kinase."
    Tan I., Lai J., Yong J., Li S.F., Leung T.
    FEBS Lett. 585:1260-1268(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY CDC42BP AND DMPK.
  39. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299; SER-422 AND SER-507, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  40. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  41. "Solution structure of the inhibitory phosphorylation domain of myosin phosphatase targeting subunit 1."
    Mori S., Iwaoka R., Eto M., Ohki S.-Y.
    Proteins 77:732-735(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 658-714, PHOSPHORYLATION AT THR-696.

Entry informationi

Entry nameiMYPT1_HUMAN
AccessioniPrimary (citable) accession number: O14974
Secondary accession number(s): B4DZ09
, F8VWB4, Q2NKL4, Q569H0, Q86WU3, Q8NFR6, Q9BYH0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: January 1, 1998
Last modified: September 3, 2014
This is version 138 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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