Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q62868

- ROCK2_RAT

UniProt

Q62868 - ROCK2_RAT

Protein

Rho-associated protein kinase 2

Gene

Rock2

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 2 (21 Sep 2011)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Protein kinase which is a key regulator of actin cytoskeleton and cell polarity. Involved in regulation of smooth muscle contraction, actin cytoskeleton organization, stress fiber and focal adhesion formation, neurite retraction, cell adhesion and motility via phosphorylation of ADD1, BRCA2, CNN1, EZR, DPYSL2, EP300, MSN, MYL9/MLC2, NPM1, RDX, PPP1R12A and VIM. Phosphorylates SORL1 and IRF4. Acts as a negative regulator of VEGF-induced angiogenic endothelial cell activation. Positively regulates the activation of p42/MAPK1-p44/MAPK3 and of p90RSK/RPS6KA1 during myogenic differentiation. Plays an important role in the timely initiation of centrosome duplication. Inhibits keratinocyte terminal differentiation. May regulate closure of the eyelids and ventral body wall through organization of actomyosin bundles. Plays a critical role in the regulation of spine and synaptic properties in the hippocampus. Plays a role in placental homeostasis during the perinatal period. Plays an important role in generating the circadian rhythm of the aortic myofilament Ca2+ sensitivity and vascular contractility by modulating the myosin light chain phosphorylation.5 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Magnesium.By similarity

    Enzyme regulationi

    Activated by RHOA binding. Inhibited by Y-27632.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei121 – 1211ATPPROSITE-ProRule annotation
    Active sitei214 – 2141Proton acceptorPROSITE-ProRule annotation
    Sitei1131 – 11322Cleavage; by granzyme B

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi98 – 1069ATPPROSITE-ProRule annotation
    Zinc fingeri1260 – 131556Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. kinase activity Source: RGD
    3. metal ion binding Source: UniProtKB-KW
    4. protein binding Source: IntAct
    5. protein serine/threonine kinase activity Source: UniProtKB-KW

    GO - Biological processi

    1. chromosome condensation Source: RGD
    2. regulation of circadian rhythm Source: UniProtKB
    3. Rho protein signal transduction Source: MGI
    4. rhythmic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Biological rhythms

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Rho-associated protein kinase 2 (EC:2.7.11.1)
    Alternative name(s):
    Rho-associated, coiled-coil-containing protein kinase 2
    Rho-associated, coiled-coil-containing protein kinase II
    Short name:
    ROCK-II
    RhoA-binding kinase 2
    p150 ROK-alpha
    Short name:
    ROKalpha
    p164 ROCK-2
    Gene namesi
    Name:Rock2
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi3590. Rock2.

    Subcellular locationi

    Cytoplasm. Cell membrane; Peripheral membrane protein. Nucleus By similarity. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity
    Note: Cytoplasmic, and associated with actin microfilaments and the plasma membrane.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. microtubule organizing center Source: UniProtKB-SubCell
    3. nucleus Source: UniProtKB-SubCell
    4. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    May play a role in hypertension. ROCK-inhibitors lower the blood pressure in spontaneous hypertensive, renal hypertensive and deoxycorticosterone acetate-induced hypertensive rats, but not in normal rats.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi48 – 481D → A: Loss of kinase activity; autophosphorylation and dimerization. 1 Publication
    Mutagenesisi121 – 1211K → A: Loss of kinase activity. 2 Publications
    Mutagenesisi121 – 1211K → M: Loss of autophosphorylation. 2 Publications
    Mutagenesisi414 – 4141T → A: Loss of kinase activity; autophosphorylation and dimerization. 1 Publication
    Mutagenesisi1170 – 11701W → A: Increased activity and autophosphorylation. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 13881388Rho-associated protein kinase 2PRO_0000086627Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei414 – 4141Phosphothreonine; by ROCK21 Publication
    Modified residuei722 – 7221Phosphotyrosine; by SRCBy similarity
    Modified residuei1137 – 11371PhosphoserineBy similarity

    Post-translational modificationi

    Autophosphorylated. Phosphorylation at Tyr-722 reduces its binding to RHOA and is crucial for focal adhesion dynamics. Dephosphorylation by PTPN11 stimulates its RHOA binding activity By similarity.By similarity
    Cleaved by granzyme B during apoptosis. This leads to constitutive activation of the kinase and membrane blebbing.

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ62868.
    PRIDEiQ62868.

    PTM databases

    PhosphoSiteiQ62868.

    Expressioni

    Tissue specificityi

    Highly expressed in brain, lung, liver, skeletal muscle, kidney and testis.1 Publication

    Gene expression databases

    GenevestigatoriQ62868.

    Interactioni

    Subunit structurei

    Homodimer By similarity. Interacts with CHORDC1, PPP1R12A, SORL1, EP300 and BRCA2 By similarity. Interacts with NPM1 and this interaction enhances its activity By similarity. Interacts with RHOA (activated by GTP), RHOB, RHOC and IRS1. Interacts with RAF1.By similarity5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MYL12AP191052EBI-1569209,EBI-354418From a different organism.

    Protein-protein interaction databases

    BioGridi247569. 1 interaction.
    IntActiQ62868. 5 interactions.
    MINTiMINT-4598028.
    STRINGi10116.ENSRNOP00000063773.

    Structurei

    Secondary structure

    1
    1388
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi1153 – 11586
    Beta strandi1163 – 11664
    Beta strandi1172 – 11787
    Beta strandi1181 – 11866
    Helixi1188 – 11925
    Beta strandi1197 – 12004
    Helixi1202 – 12043
    Beta strandi1205 – 12106
    Turni1213 – 12153
    Beta strandi1217 – 12193
    Turni1221 – 12233
    Helixi1224 – 12263
    Beta strandi1227 – 12326
    Beta strandi1234 – 12363
    Beta strandi1256 – 12583
    Beta strandi1261 – 12666
    Beta strandi1275 – 12817
    Beta strandi1284 – 12863
    Beta strandi1290 – 12967
    Beta strandi1299 – 13013
    Helixi1302 – 13076
    Turni1317 – 13193
    Beta strandi1325 – 13306
    Helixi1334 – 134714

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2ROVNMR-A1151-1351[»]
    2ROWNMR-A1237-1320[»]
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ62868.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini92 – 354263Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini357 – 42569AGC-kinase C-terminalAdd
    BLAST
    Repeati475 – 55985REMAdd
    BLAST
    Domaini1150 – 1349200PHPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni363 – 784422Interaction with PPP1R12AAdd
    BLAST
    Regioni373 – 42048Interaction with NPM1By similarityAdd
    BLAST
    Regioni979 – 104769RHOA bindingBy similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili439 – 1024586Sequence AnalysisAdd
    BLAST
    Coiled coili1052 – 113180Sequence AnalysisAdd
    BLAST

    Domaini

    An interaction between Thr-414 and Asp-48 is essential for kinase activity and dimerization.1 Publication

    Sequence similaritiesi

    Contains 1 AGC-kinase C-terminal domain.Curated
    Contains 1 PH domain.PROSITE-ProRule annotation
    Contains 1 phorbol-ester/DAG-type zinc finger.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation
    Contains 1 REM (Hr1) repeat.Curated

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1260 – 131556Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Coiled coil, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000017259.
    HOVERGENiHBG053111.
    InParanoidiQ62868.
    KOiK17388.

    Family and domain databases

    Gene3Di2.30.29.30. 2 hits.
    InterProiIPR000961. AGC-kinase_C.
    IPR011072. HR1_rho-bd.
    IPR011009. Kinase-like_dom.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR020684. Rho-assoc_coiled-coil_kin.
    IPR015008. Rho-bd_dom.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF02185. HR1. 1 hit.
    PF00169. PH. 1 hit.
    PF00069. Pkinase. 1 hit.
    PF08912. Rho_Binding. 1 hit.
    [Graphical view]
    PIRSFiPIRSF037568. Rho_kinase. 1 hit.
    SMARTiSM00109. C1. 1 hit.
    SM00233. PH. 1 hit.
    SM00133. S_TK_X. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
    PS50003. PH_DOMAIN. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    PS50081. ZF_DAG_PE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q62868-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSRPPPTGKM PGAPEAAAGD GAGAGRQRKL EALIRDPRSP INVESLLDGL     50
    NSLVLDLDFP ALRKNKNIDN FLNRYEKIVK KIRGLQMKAE DYDVVKVIGR 100
    GAFGEVQLVR HKASQKVYAM KLLSKFEMIK RSDSAFFWEE RDIMAFANSP 150
    WVVQLFCAFQ DDRYLYMVME YMPGGDLVNL MSNYDVPEKW AKFYTAEVVL 200
    ALDAIHSMGL IHRDVKPDNM LLDKHGHLKL ADFGTCMKMD ETGMVHCDTA 250
    VGTPDYISPE VLKSQGGDGY YGRECDWWSV GVFLFEMLVG DTPFYADSLV 300
    GTYSKIMDHK NSLCFPEDTE ISKHAKNLIC AFLTDREVRL GRNGVEEIKS 350
    ASFFKNDQWN WDNIRETAAP VVPELSSDID SSNFDDIEDD KGDVETFPIP 400
    KAFVGNQLPF IGFTYFRENL LLSDSPPCRE NDAIQTRKSE ESQEIQKKLY 450
    ALEEHLSSEV QAKEELEQKC KSINTRLEKT AKELEEEITF RKNVESTLRQ 500
    LEREKALLQH KNAEYQRKAD HEADKKRNLE NDVNSLKDQL EDLKKRNQSS 550
    QISTEKVNQL QKQLDEANAL LRTESDTAAR LRKTQAESSK QIQQLESNNR 600
    DLQDKNCLLE TAKLKLEKEF INLQSALESE RRDRTHGSEI INDLQGRISG 650
    LEEDLKTGKT LLAKVELEKR QLQEKLTDLE KEKSNMEIDM TYQLKVIQQS 700
    LEQEEAEHKT TKARLADKNK IYESIEEAKS EAMKEMEKKL LEERSLKQKV 750
    ENLLLEAEKR CSILDCDLKQ SQQKLNELLK QKDVLNEDVR NLTLKIEQET 800
    QKRCLMQNDL KMQTQQVNTL KMSEKQIKQE NNHLMEMKMN LEKQNAELRK 850
    ERQDADGQMK ELQDQLEAEQ YFSTLYKTQV RELKEENEEK TKLCKELQQK 900
    KQDLQDERDS LAAQLEITLT KADSEQLARS IAEEQYSDLE KEKIMKELEI 950
    KEMMARHKQE LTEKDATIAS LEETNRTLTS DVANLANEKE ELNNKLKDTQ 1000
    EQLSKLKDEE ISAAAIKAQF EKQLLTERTL KTQAVNKLAE IMNRKEPVKR 1050
    GSDTDVRRKE KENRKLHMEL KSEREKLTQQ MIKYQKELNE MQAQIAEESQ 1100
    IRIELQMTLD SKDSDIEQLR SQLQALHIGM DSSSIGSGPG DAEPDDGFPE 1150
    SRLEGWLSLP VRNNTKKFGW VKKYVIVSSK KILFYDSEQD KEQSNPYMVL 1200
    DIDKLFHVRP VTQTDVYRAD AKEIPRIFQI LYANEGESKK EPEFPVEPVG 1250
    EKSNYICHKG HEFIPTLYHF PTNCEACMKP LWHMFKPPPA LECSRCHIKC 1300
    HKDHMDKKEE IIAPCKVYYD ISSAKNLLLL ANSTEEQQKW VSRLVKKIPK 1350
    KPPAPDPFAR SSPRTSMKIQ QNQSIRRPSR QLAPNKPS 1388
    Length:1,388
    Mass (Da):160,387
    Last modified:September 21, 2011 - v2
    Checksum:iB23672CA8645067C
    GO

    Sequence cautioni

    The sequence AAB37540.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U38481 mRNA. Translation: AAB37540.1. Different initiation.
    RefSeqiNP_037154.2. NM_013022.2.
    UniGeneiRn.88642.

    Genome annotation databases

    GeneIDi25537.
    KEGGirno:25537.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U38481 mRNA. Translation: AAB37540.1 . Different initiation.
    RefSeqi NP_037154.2. NM_013022.2.
    UniGenei Rn.88642.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2ROV NMR - A 1151-1351 [» ]
    2ROW NMR - A 1237-1320 [» ]
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 247569. 1 interaction.
    IntActi Q62868. 5 interactions.
    MINTi MINT-4598028.
    STRINGi 10116.ENSRNOP00000063773.

    Chemistry

    BindingDBi Q62868.
    ChEMBLi CHEMBL5490.

    PTM databases

    PhosphoSitei Q62868.

    Proteomic databases

    PaxDbi Q62868.
    PRIDEi Q62868.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 25537.
    KEGGi rno:25537.

    Organism-specific databases

    CTDi 9475.
    RGDi 3590. Rock2.

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000017259.
    HOVERGENi HBG053111.
    InParanoidi Q62868.
    KOi K17388.

    Miscellaneous databases

    EvolutionaryTracei Q62868.
    NextBioi 607045.
    PROi Q62868.

    Gene expression databases

    Genevestigatori Q62868.

    Family and domain databases

    Gene3Di 2.30.29.30. 2 hits.
    InterProi IPR000961. AGC-kinase_C.
    IPR011072. HR1_rho-bd.
    IPR011009. Kinase-like_dom.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR020684. Rho-assoc_coiled-coil_kin.
    IPR015008. Rho-bd_dom.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF02185. HR1. 1 hit.
    PF00169. PH. 1 hit.
    PF00069. Pkinase. 1 hit.
    PF08912. Rho_Binding. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF037568. Rho_kinase. 1 hit.
    SMARTi SM00109. C1. 1 hit.
    SM00233. PH. 1 hit.
    SM00133. S_TK_X. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS51285. AGC_KINASE_CTER. 1 hit.
    PS50003. PH_DOMAIN. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    PS50081. ZF_DAG_PE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A novel serine/threonine kinase binding the Ras-related RhoA GTPase which translocates the kinase to peripheral membranes."
      Leung T., Manser E., Tan L., Lim L.
      J. Biol. Chem. 270:29051-29054(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AUTOPHOSPHORYLATION, INTERACTION WITH RHOA, SUBCELLULAR LOCATION.
      Tissue: Brain.
    2. "The p160 RhoA-binding kinase ROK alpha is a member of a kinase family and is involved in the reorganization of the cytoskeleton."
      Leung T., Chen X.-Q., Manser E., Lim L.
      Mol. Cell. Biol. 16:5313-5327(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, AUTOPHOSPHORYLATION, INTERACTION WITH RHOA; RHOB AND RHOC, MUTAGENESIS OF LYS-121, TISSUE SPECIFICITY.
    3. "Calcium sensitization of smooth muscle mediated by a Rho-associated protein kinase in hypertension."
      Uehata M., Ishizaki T., Satoh H., Ono T., Kawahara T., Morishita T., Tamakawa H., Yamagami K., Inui J., Maekawa M., Narumiya S.
      Nature 389:990-994(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ROLE IN HYPERTENSION, INHIBITION BY Y-27632.
    4. "Active Rho kinase (ROK-alpha) associates with insulin receptor substrate-1 and inhibits insulin signaling in vascular smooth muscle cells."
      Begum N., Sandu O.A., Ito M., Lohmann S.M., Smolenski A.
      J. Biol. Chem. 277:6214-6222(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IRS1.
    5. Cited for: INTERACTION WITH RAF1.
    6. "Direct cleavage of ROCK II by granzyme B induces target cell membrane blebbing in a caspase-independent manner."
      Sebbagh M., Hamelin J., Bertoglio J., Solary E., Breard J.
      J. Exp. Med. 201:465-471(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: CLEAVAGE BY GRANZYME B.
    7. "The hydrophobic motif of ROCK2 requires association with the N-terminal extension for kinase activity."
      Couzens A.L., Saridakis V., Scheid M.P.
      Biochem. J. 419:141-148(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAIN, PHOSPHORYLATION AT THR-414, MUTAGENESIS OF ASP-48; LYS-121; THR-414 AND TRP-1170.
    8. "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: FUNCTION, INTERACTION WITH PPP1R12A, SUBCELLULAR LOCATION.
    9. "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: FUNCTION IN PHOSPHORYLATION OF MYL9/MLC2 AND PPP1R12A.

    Entry informationi

    Entry nameiROCK2_RAT
    AccessioniPrimary (citable) accession number: Q62868
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 24, 2004
    Last sequence update: September 21, 2011
    Last modified: October 1, 2014
    This is version 136 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3