wanglab/gogpt-training-data huggingface dataset:
Protein: Precorrin-2 dehydrogenase (Mba_PC2_DH) (EC 1.3.1.76) (Q46CH4)
Organism: Methanosarcina barkeri (strain Fusaro / DSM 804)
Function: Involved in the archaeal biosynthesis of heme. Catalyzes the oxiation of precorrin-2 into sirohydroclorin.
Interaction partners:
- S-adenosyl-L-methionine-dependent uroporphyrinogen III methyltransferase
- Siroheme decarboxylase beta subunit
- Siroheme decarboxylase alpha subunit
- Sirohydrochlorin cobaltochelatase
- Sirohydrochlorin cobaltochelatase
- Cobalt-factor II C20-methyltransferase
- Glutamate-1-semialdehyde 2,1-aminomutase
- Uroporphyrinogen-III synthase
- Probable porphobilinogen deaminase
- Adenosylcobinamide-GDP ribazoletransferase
Sequence:
MTKTNNFLPLMLDLSGRKIVIFGGGSVGERKAKLFSGCADTLVASLEFSQALQELGTSGQVRLVQLDLLTASDSELRGLISGAFLVIPATSNFELNQKITAIARENDILINQVDTLGSVVIPSVIKRGDLVIGISTLGHSPAVSKYTRKQIEGLVTPEYSDMIRLQDELRSYLKQHVAEQRERKEILWKVLESETVWNGFSESYEKAAERAYAIISSYLVNSNR
Protein: C4b-binding protein beta chain (P20851)
Organism: Homo sapiens (Human)
Function: Controls the classical pathway of complement activation. It binds as a cofactor to C3b/C4b inactivator (C3bINA), which then hydrolyzes the complement fragment C4b. It also accelerates the degradation of the C4bC2a complex (C3 convertase) by dissociating the complement fragment C2a. It also interacts with anticoagulant protein S and with serum amyloid P component. The beta chain binds protein S.
Subcellular location: Secreted.
Interaction partners:
- Complement C4-A
- Complement C4-B
- C4b-binding protein alpha chain
- Vitamin K-dependent protein S
- Complement factor I
- Complement factor H-related protein 4
- Complement component C8 alpha chain
- Complement factor H-related protein 2
- Complement factor H-related protein 3
- Complement factor H-related protein 1
Sequence:
MFFWCACCLMVAWRVSASDAEHCPELPPVDNSIFVAKEVEGQILGTYVCIKGYHLVGKKTLFCNASKEWDNTTTECRLGHCPDPVLVNGEFSSSGPVNVSDKITFMCNDHYILKGSNRSQCLEDHTWAPPFPICKSRDCDPPGNPVHGYFEGNNFTLGSTISYYCEDRYYLVGVQEQQCVDGEWSSALPVCKLIQEAPKPECEKALLAFQESKNLCEAMENFMQQLKESGMTMEELKYSLELKKAELKAKLL
Protein: Tetratricopeptide repeat protein 23 (TPR repeat protein 23) (Q8CHY7)
Organism: Mus musculus (Mouse)
Function: Participates positively in the ciliary Hedgehog (Hh) signaling.
Subcellular location: Cell projection, cilium {ECO:0000269|PubMed:29459677}. Note=Colocalizes with EVC and IQCE at the EvC zone of primary cilia. {ECO:0000269|PubMed:29459677}.
Interaction partners:
- IQ domain-containing protein E
Sequence:
MQESQDTHMSSHLDEVVAAVSVTSKNRIPNKLLQTALFQPPREKLHLCEERAKSYSSSREYKQAIQELVRCVALTRICYGDWHWKLAEAYVNLAQGYLQLKGLSLQAKQHAEKAKEILANSIESPCHNKTDIFKCSLELFYTLGRALLSLQKFKDASENLIKAERLSKEMLQCGNIVKEEWIEIQSRIKLSFAQLYQGQKRSKEAFPFYQKALEYTEITKDEKSLECVQVLRELAGVEQALGLYAAAISHFSRDRLPTPQPCPLGHKCCCPSPFLSPVLNVTWRPFYSSQVDEEEAHLIILSKDPSPEEAADSAHFIARAAAASGMHDHRDVAEKYFQESMTSIKDSEGAERAKFLSIQDEFCSFLQTTGQKERAAMILRESLEAKVGAFGDFSPEVAETYRALGRADLAQGNNSGAYAKLKKCVQIETFLYGSQDKKTLATQHTIDTLSKISEAAGKSRQSVKAKVAFCTSAPQYGMPGKGRHSVAD
Protein: Ig-like domain-containing protein (Q21465)
Organism: Caenorhabditis elegans
Interaction partners:
- Protein unc-87
- Troponin I 2
- Troponin T
- Myosin regulatory light chain 1
- Paramyosin
- Troponin T
Sequence:
MAPPSIYGEPKIRSENGSVFLEVIVTGADVSKIQWFFGPDELEENEFLKFSNSDEGGNRTKFVAEIKDFDKPLAGEYKAVFANADGENSSNFTVAAGNAPDFHDKPHIVQRDNGNVIVIKVRAKSHLEMKAEWFKDEKPVKFTDRVKAVVKKDDKDKDGFQFLLEITGPQKDDEAKYKCVVKNSEGQNQQALNLVFD
Protein: Hypocretin neuropeptide precursor (Hypocretin) (Orexin precursor) (Prepro-orexin) (Preprohypocretin) (Q8AV17)
Organism: Gallus gallus (Chicken)
Subcellular location: Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00004541}. Rough endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004427}. Synapse {ECO:0000256|ARBA:ARBA00034103}.
Interaction partners:
Sequence:
MEVPNAKLQRSACLLLLLLLLCSLAGGRQSLPECCRQKTCSCRIYDLLHGMGNHAAGILTLGKRKSIPPAFQSRLYRLLHGSGNHAAGILTIGKREERPGTACRDALSCAAGTQPTVTPRGTAASPRECQEHAEKDLTKGWAAAKSFY
Protein: Adiponectin receptor protein 1 (Progestin and adipoQ receptor family member 1) (Progestin and adipoQ receptor family member I) (Q96A54)
Organism: Homo sapiens (Human)
Function: Receptor for ADIPOQ, an essential hormone secreted by adipocytes that regulates glucose and lipid metabolism. Required for normal glucose and fat homeostasis and for maintaining a normal body weight. ADIPOQ-binding activates a signaling cascade that leads to increased AMPK activity, and ultimately to increased fatty acid oxidation, increased glucose uptake and decreased gluconeogenesis. Has high affinity for globular adiponectin and low affinity for full-length adiponectin (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:12802337, ECO:0000269|PubMed:25855295}; Multi-pass membrane protein {ECO:0000269|PubMed:12802337, ECO:0000269|PubMed:25855295}. Note=Localized to the cell membrane and intracellular organelles. {ECO:0000269|PubMed:12802337}.
Interaction partners:
- Adiponectin
- DCC-interacting protein 13-alpha
- Adiponectin receptor protein 2
- Leptin
- Cadherin-13
- Insulin-like growth factor 1 receptor
- Peroxisome proliferator-activated receptor alpha
- Proto-oncogene tyrosine-protein kinase Src
- Insulin
- Resistin
Sequence:
MSSHKGSVVAQGNGAPASNREADTVELAELGPLLEEKGKRVIANPPKAEEEQTCPVPQEEEEEVRVLTLPLQAHHAMEKMEEFVYKVWEGRWRVIPYDVLPDWLKDNDYLLHGHRPPMPSFRACFKSIFRIHTETGNIWTHLLGFVLFLFLGILTMLRPNMYFMAPLQEKVVFGMFFLGAVLCLSFSWLFHTVYCHSEKVSRTFSKLDYSGIALLIMGSFVPWLYYSFYCSPQPRLIYLSIVCVLGISAIIVAQWDRFATPKHRQTRAGVFLGLGLSGVVPTMHFTIAEGFVKATTVGQMGWFFLMAVMYITGAGLYAARIPERFFPGKFDIWFQSHQIFHVLVVAAAFVHFYGVSNLQEFRYGLEGGCTDDTLL
Protein: Kinesin-like protein 3 (Kinesin-related protein 1) (Q9US60)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Cytoplasmic motor that could play a role in Golgi membrane recycling.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10641037}.
Interaction partners:
- Tubulin alpha-2 chain
- Myosin-51
- Inner kinetochore subunit mis6
- Myosin-52
- Tubulin beta chain
- Tropomyosin
- Tubulin alpha-1 chain
- Microtubule-associated protein mmb1
- Kinesin-like protein 8
- Dynein heavy chain, cytoplasmic
Sequence:
MTSIKVVCRIRPTNQLEQDLGGNNVIYPLNDSTVHIETSDYSGNFVFDRVFHPSSTQNDIFSYSIESTVDDLFLGYNGTVLAYGQTGSGKTYTMMGIENNFEKEGMTPRMLRRIFDKIRDSPSTTEYEVKVSYMEIYMEKIHDLLSEKNDRLTVHEDKLQGVYVQGLKTIYVSSETEALDILNKGMGSRAVASTSMNAQSSRSHSIFVLEVVQTDTESGETRRGRLFLVDLAGSESVGKSGAVGQTLEEAKKINRSLSTLGMVINSLTDSKLSHVPYRDSKLTRILKESLGGNSRTTLIINCSPDSYNATETLSTLRFGHRAKSIKNKAVVNSELSVDEMKRQLYIYKDALSRCVCGARINNNLDYNNCHSNVWSGEHSLTLSNLAEKSNLKEAEIIQGNRTIQESNNDRDESTVASIHRHNFDSDSINRLYAEAQLELKQRDGVLSSTKQQLSDLMTALGDAQERYVELVKNHRVNSNLTANNSLNDKPGFTIEQKDKNFSINNERNNFLQKLSTLDSSLAALVNVQRKLIKALISKERPQNGTVIKKIQGGT
Protein: Collagenase ColG (EC 3.4.24.3) (Class I collagenase) (Gelatinase ColG) (Microbial collagenase) (Q9X721)
Organism: Hathewaya histolytica (Clostridium histolyticum)
Function: Clostridial collagenases are among the most efficient degraders of eukaryotic collagen known; saprophytes use collagen as a carbon source while pathogens additionally digest collagen to aid in host colonization. Has both tripeptidylcarboxypeptidase on Gly-X-Y and endopeptidase activities; the endopeptidase cuts within the triple helix region of collagen while tripeptidylcarboxypeptidase successively digests the exposed ends, thus clostridial collagenases can digest large sections of collagen. Active on soluble type I collagen, insoluble collagen, azocoll, soluble PZ-peptide (all collagenase substrates) and gelatin. The full-length protein has collagenase activity, while the in vivo derived C-terminally truncated shorter versions only act on gelatin. In vitro digestion of soluble calf skin collagen fibrils requires both ColG and ColH; ColG forms missing the second collagen-binding domain are also synergistic with ColH, although their overall efficiency is decreased. The activator domain (residues 119-388) and catalytic subdomain (389-670) open and close around substrate using a Gly-rich hinge (387-397), allowing digestion when the protein is closed. Binding of collagen requires Ca(2+) and is inhibited by EGTA; the collagen-binding domain (CBD, S3a plus S3b) specifically recognizes the triple-helical conformation made by 3 collagen protein chains in the triple-helical region. Isolated CBD (S3a plus S3b) binds collagen fibrils and sheets of many tissues.
Subcellular location: Secreted {ECO:0000269|PubMed:18374061, ECO:0000269|PubMed:22099748, ECO:0000269|PubMed:9922257}.
Interaction partners:
Sequence:
MKKNILKILMDSYSKESKIQTVRRVTSVSLLAVYLTMNTSSLVLAKPIENTNDTSIKNVEKLRNAPNEENSKKVEDSKNDKVEHVKNIEEAKVEQVAPEVKSKSTLRSASIANTNSEKYDFEYLNGLSYTELTNLIKNIKWNQINGLFNYSTGSQKFFGDKNRVQAIINALQESGRTYTANDMKGIETFTEVLRAGFYLGYYNDGLSYLNDRNFQDKCIPAMIAIQKNPNFKLGTAVQDEVITSLGKLIGNASANAEVVNNCVPVLKQFRENLNQYAPDYVKGTAVNELIKGIEFDFSGAAYEKDVKTMPWYGKIDPFINELKALGLYGNITSATEWASDVGIYYLSKFGLYSTNRNDIVQSLEKAVDMYKYGKIAFVAMERITWDYDGIGSNGKKVDHDKFLDDAEKHYLPKTYTFDNGTFIIRAGDKVSEEKIKRLYWASREVKSQFHRVVGNDKALEVGNADDVLTMKIFNSPEEYKFNTNINGVSTDNGGLYIEPRGTFYTYERTPQQSIFSLEELFRHEYTHYLQARYLVDGLWGQGPFYEKNRLTWFDEGTAEFFAGSTRTSGVLPRKSILGYLAKDKVDHRYSLKKTLNSGYDDSDWMFYNYGFAVAHYLYEKDMPTFIKMNKAILNTDVKSYDEIIKKLSDDANKNTEYQNHIQELADKYQGAGIPLVSDDYLKDHGYKKASEVYSEISKAASLTNTSVTAEKSQYFNTFTLRGTYTGETSKGEFKDWDEMSKKLDGTLESLAKNSWSGYKTLTAYFTNYRVTSDNKVQYDVVFHGVLTDNADISNNKAPIAKVTGPSTGAVGRNIEFSGKDSKDEDGKIVSYDWDFGDGATSRGKNSVHAYKKAGTYNVTLKVTDDKGATATESFTIEIKNEDTTTPITKEMEPNDDIKEANGPIVEGVTVKGDLNGSDDADTFYFDVKEDGDVTIELPYSGSSNFTWLVYKEGDDQNHIASGIDKNNSKVGTFKSTKGRHYVFIYKHDSASNISYSLNIKGLGNEKLKEKENNDSSDKATVIPNFNTTMQGSLLGDDSRDYYSFEVKEEGEVNIELDKKDEFGVTWTLHPESNINDRITYGQVDGNKVSNKVKLRPGKYYLLVYKYSGSGNYELRVNK
Protein: Mitochondrial pyruvate carrier (F1Q6Z3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004448, ECO:0000256|RuleBase:RU363100}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004448, ECO:0000256|RuleBase:RU363100}.
Interaction partners:
- Mitochondrial pyruvate carrier
- Mitochondrial pyruvate carrier
- Small nuclear ribonucleoprotein polypeptide F.
Sequence:
MAATLARKAVDHLRSKEFRDYLMSTHFWGPVANWGLPIAAISDMKKSPEIISGRMTFALTCYSLLFMRFAYKVQPRNWLLFACHFTNEGAQLIQGSRLIKYNMEKKMAK
Protein: Translocating chain-associated membrane protein (Q9U3P5)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MVKPQGGSKASKKPQPPILSHEFIIQNHGDIMSCVVMVFIVGLMFPLTHSLSSLFIAPQYNGTYTVAVEQGQEREVHGYLSGILDLPAIFFYSVCWIVVHAVVQEYGLDKISKKTHLSKVSTFKFGESFHQMFFTVYSIAHAFYIVSERLEDFSEVKSVWLGYPTEHRVMSAAYKLYFIFQISYWIHQFPEFYLQKLKRDEIRQKSVQAILHIAFISIAYFFNFTRVGLALITLEYITQLIFHIARFAHFVGRKGLSDPAFKLFNGSFVLVRLGSIIIAVMTFWYGLRQAESPFVDISAGNFNTAVIRLNVLLAVVLLQLFLLYSFVVFHMGRFRESNAKKEKKKSAAAAAAVPKKEKKRQDSESDSKKKN
Protein: Calcineurin subunit B type 1 (Protein phosphatase 2B regulatory subunit 1) (Protein phosphatase 3 regulatory subunit B alpha isoform 1) (P63100)
Organism: Rattus norvegicus (Rat)
Function: Regulatory subunit of calcineurin, a calcium-dependent, calmodulin stimulated protein phosphatase. Confers calcium sensitivity.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q63810}. Cell membrane {ECO:0000250|UniProtKB:Q63810}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:Q63810}. Cell membrane {ECO:0000250|UniProtKB:P63098}; Lipid-anchor {ECO:0000250|UniProtKB:P63098}. Note=Translocates from the cytosol to the sarcolemma in a CIB1-dependent manner during cardiomyocyte hypertrophy. {ECO:0000250|UniProtKB:Q63810}.
Interaction partners:
- Protein phosphatase 3 catalytic subunit alpha
- Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform
- Calmodulin-like protein 4
- Serine/threonine-protein phosphatase
- Nuclear factor of activated T-cells 1
- Calmodulin-like protein 3
- Calmodulin-1
- Nuclear factor of activated T-cells, cytoplasmic 3
- Nuclear factor of activated T-cells, cytoplasmic 4
- Nuclear factor of activated T-cells 2
Sequence:
MGNEASYPLEMCSHFDADEIKRLGKRFKKLDLDNSGSLSVEEFMSLPELQQNPLVQRVIDIFDTDGNGEVDFKEFIEGVSQFSVKGDKEQKLRFAFRIYDMDKDGYISNGELFQVLKMMVGNNLKDTQLQQIVDKTIINADKDGDGRISFEEFCAVVGGLDIHKKMVVDV
Protein: RAS guanyl-releasing protein 1 (H0YKM0)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004202}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}. Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}. Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004406}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004406}. Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004395}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004395}.
Interaction partners:
Sequence:
MKVVPTSPTPTDARRPRLGQIWITPVERTSTQAALVQGAGRRAQGTCLRPSPADGYLETPGHRKPSHGCRAASKARLEAKPANSPFPSHPSLAHITQFRMMVSLGHLAKGASLDDLIDSCIQSFDADGNLCRSNQLLQVMLTMHRIVISSAELLQKVITLYKDALAKNSPGLCLKICYFVRYWITEFWVMFKMDASLTDTMEEFQELVKAKGEELHCRLIDTTQINARDWSRKLTQRIKSNTSKKRKVSLLFDHLEPEELSEHLTYLEFKSFRRISFSDYQNYLVNSCVKENPTMERSIALCNGISQWVQLMVLSRPTPQLRAEVFIKFIQVAQKLHQLQNFNTLMAVIGGLCHSSISRLKETSSHVPHEINKVLGEMTELLSSSRNYDNYRRAYGECTDFKIPILGVHLKDLISLYEAMPDYLEDGKVNVHKLLALYNHISELVQLQEVAPPLEANKDLVHLLTLSLDLYYTEDEIYELSYAREPRNHRAPPLTPSKPPVVVDWASGVSPKPDPKTISKHVQRMVDSVFKNYDHDQDGYISQEEFEKIAASFPFSFCVMDKDREGLISRDEITAYFMRASSIYSKLGLGFPHNFQETTYLKPTFCDNCAGFLWGVIKQGYRCKDCGMNCHKQCKDLVVFECKKRAKNPVAPTENNTSVGPVSNLCSLGAKDLLHAPEEGPFTFPNGEAVEHGEESKDRTIMLMGVSSQKISLRLKRAVAHKATQTESQPWIGSEGPSGPFVLSSPRKTAQDTLYVLPSPTSPCPSPVLVRKRAFVKWENKDSLIKSKEELRHLRLPTYQELEQEINTLKADNDALKIQLKYAQKKIESLQLEKSNHVLAQMEQGDCS
Protein: Ubiquitin carboxyl-terminal hydrolase 30 (EC 3.4.19.12) (Deubiquitinating enzyme 30) (Ubiquitin thioesterase 30) (Ubiquitin-specific-processing protease 30) (Ub-specific protease 30) (Q70CQ3)
Organism: Homo sapiens (Human)
Function: Deubiquitinating enzyme tethered to the mitochondrial outer membrane that acts as a key inhibitor of mitophagy by counteracting the action of parkin (PRKN): hydrolyzes ubiquitin attached by parkin on target proteins, such as RHOT1/MIRO1 and TOMM20, thereby blocking parkin's ability to drive mitophagy. Preferentially cleaves 'Lys-6'- and 'Lys-11'-linked polyubiquitin chains, 2 types of linkage that participate in mitophagic signaling. Does not cleave efficiently polyubiquitin phosphorylated at 'Ser-65'. Acts as negative regulator of mitochondrial fusion by mediating deubiquitination of MFN1 and MFN2 (By similarity).
Subcellular location: Mitochondrion outer membrane {ECO:0000269|PubMed:18287522, ECO:0000269|PubMed:24896179}.
Interaction partners:
- Ubiquitin-ribosomal protein eS31 fusion protein
- Polyubiquitin-C
- Ubiquitin-ribosomal protein eL40 fusion protein
- Polyubiquitin-B
- Mitochondrial import receptor subunit TOM20 homolog
- Zinc finger-containing ubiquitin peptidase 1
- Mitochondrial fission 1 protein
- Ubiquitin carboxyl-terminal hydrolase 1
- Mitochondrial ubiquitin ligase activator of NFKB 1
- Serine/threonine-protein kinase PINK1, mitochondrial
Sequence:
MLSSRAEAAMTAADRAIQRFLRTGAAVRYKVMKNWGVIGGIAAALAAGIYVIWGPITERKKRRKGLVPGLVNLGNTCFMNSLLQGLSACPAFIRWLEEFTSQYSRDQKEPPSHQYLSLTLLHLLKALSCQEVTDDEVLDASCLLDVLRMYRWQISSFEEQDAHELFHVITSSLEDERDRQPRVTHLFDVHSLEQQSEITPKQITCRTRGSPHPTSNHWKSQHPFHGRLTSNMVCKHCEHQSPVRFDTFDSLSLSIPAATWGHPLTLDHCLHHFISSESVRDVVCDNCTKIEAKGTLNGEKVEHQRTTFVKQLKLGKLPQCLCIHLQRLSWSSHGTPLKRHEHVQFNEFLMMDIYKYHLLGHKPSQHNPKLNKNPGPTLELQDGPGAPTPVLNQPGAPKTQIFMNGACSPSLLPTLSAPMPFPLPVVPDYSSSTYLFRLMAVVVHHGDMHSGHFVTYRRSPPSARNPLSTSNQWLWVSDDTVRKASLQEVLSSSAYLLFYERVLSRMQHQSQECKSEE
Protein: Hemoglobin subunit beta (Beta-globin) (Hemoglobin beta chain) (P02067)
Organism: Sus scrofa (Pig)
Function: Involved in oxygen transport from the lung to the various peripheral tissues.
Interaction partners:
- Hemoglobin subunit alpha
- Hemoglobin subunit theta-1
- Haptoglobin
- Hemoglobin subunit zeta
- Hemoglobin subunit mu
Sequence:
MVHLSAEEKEAVLGLWGKVNVDEVGGEALGRLLVVYPWTQRFFESFGDLSNADAVMGNPKVKAHGKKVLQSFSDGLKHLDNLKGTFAKLSELHCDQLHVDPENFRLLGNVIVVVLARRLGHDFNPNVQAAFQKVVAGVANALAHKYH
Protein: GPI ethanolamine phosphate transferase 1 (EC 2.-.-.-) (A0A1W2PQA9)
Organism: Homo sapiens (Human)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU367138}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU367138}.
Interaction partners:
Sequence:
MLLFFTLGLLIHFVFFASIFDIYFTSPLVHGMTPQFTPLPPPARRLVLFVADGLRADALYELDENGNSRAPFIRNIIMHEGSWGISHTRVPTESRPGHVALIAGFYEDVSAVAKGWKENPVEFDSLFNESKYTWSWGSPDILPMFAKGASGDHVYTYSYDAKREDFGAQDATKLDTWVFDNVKDFFHHARNNQSLFSKINEEKIVFFLHLLGIDTNGHAHRPSSRDYKHNIKKVDDGVKEIVSMFNHFYGNDGKTTFIFTSDHGMTDWGSHGAGHPSETLTPLVTWGAGIKYPQRVSAQQFDDAFLKEWRLENWKRLDVNQADIAPLMTSLIGVPFPLNSVGILPVDYLNNTDLFKAESMFTNAVQILEQFKVKMTQKKEVTLPFLFTPFKLLSDSKQFNILRKARSYIKHRKFDEVVSLCKELIHLALKGLSYYHTYDRFFLGVNVVIGFVGWISYASLLIIKSHSNLIKGVSKEVKKPSHLLPCSFVAIGILVAFFLLIQACPWTYYVYGLLPLPIWYAVLREFQVIQDLVVSVLTYPLSHFVGYLLAFTLGIEVLVLSFFYRYMLTAGLTAFAAWPFLTRLWTRAKMTSLSWTFFSLLLAVFPLMPVVGRKPDISLVMGAGLLVLLLSLCVVTSLMKRKDSFIKEELLVHLLQVLSTVLSMYVVYSTQSSLLRKQGLPLMNQIISWATLASSLVVPLLSSPVLFQRLFSILLSLMSTYLLLSTGYEALFPLVLSCLMFVWINIEQETLQQSGVCCKQKLTSIQFSYNTDITQFRQLYLDDIRRAFFLVFFLVTAFFGTGNIASINSFDLASVYCFLTVFSPFMMGALMMWKILIPFVLVMCAFEAVQLTTQLSSKSLFLIVLVISDIMALHFFFLVKDYGSWLDIGTRQLLACTAWLFMYISASPNRLWMLSDPGLDLNLLHAIRACISHYVIVMSMTIFLVFLNGLAQLLTTKKLRLCGKPKSHFM
Protein: Canoe, isoform E (Canoe, isoform J) (FI05483p) (Q9VN82)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Polychaetoid, isoform O
- Ras-related protein Rap1
- Echinoid, isoform A
- Vinculin
- DE-cadherin
- Adherens junction protein p120
- Alhambra, isoform P
- LD33695p
- Atypical protein kinase C
- Ras-like protein 1
Sequence:
MSHDKKMLDREAVRSVIQQWNANRLDLFALSEPDENLLFHGVMRFYFQDAGQKVATKCIRVASDATVTDVIDTLIEKFRPDMRMLSVPNYALYEVHANGEERRLNADEKPLLVQLNWHIDDREGRFLLKNIDQKTTPIEQTDLNFKRKLSKREKKEQKKKEKMAKLSSDPPTSNGSHLGLGNGVGASSGSAHMNGNAGGTGGDSSDAVAGKLYTELPETSFTRSISNPEAVMRRRRQQKLEKKLQQFRSRDGGPDTGGTLKIYGESLCQDVPYKTLLLSIRDCAQAVVREMLTKYGLEKADPLHYCLVQVNSDGTEYILDDDECPLSILMNHPTSRGSIMFHVRRRPADSQPRRRKKKPLGAANGANHISGDREGPVLVEVTHSGDGGRRIKLGSDPVEVGSANTNCLQLFGPSIQPRHCLISLLEGVCTVTPLHTDALTFVNGHHISQPTILHNGSVVMFGRVASYRFLDSPTDGRYNLALSQSQLDSACLYESRSPTSPGSWNDEDGALSSTHKSDYDHHQQANHSSAYHNNNNNSSDHPLSSTLRDVVDSKAGQDQGANSGNYDGQSLEGNLENETKSISSLKSGGSNSQDRSPKMTGSGILAGGGSGSGDTQGQEPILPAVLEFPETHQELFLRHIISELDVNVPHFKLAPVYSLYLCARYRASTHYRPELQPTERAHKLTMFLHHVANLVYSVVQEQYTDPRILAFWMANSSEFLHFLKSDRHISAFSVQAQEVLAEAVQTAFRNLVNCFRLELSQTLNQFLSENIDHDSAAGLVLTVLGSAMALLRRCRVNAALTIQLFSQLFHYINVICFNTIVANSQMCTGDWGKVMTERLQLLELWAERQGLELAADCHLAKINQCAQFLQAPKSSVEEIQQLACSCFRLNSLQMAALLQQEKLPRNLVDTAIRMAESVADELTRADGREVRLEESPELHLALLLPDDGFSCDVVRGIPTGLVDFLNPLQQQGMCRLAAQPTSIGLWTVYMHQFNARSSSAMSNKLPQPELQLIKLHKNSNGMGLSIVAAKGAGQEKLGIYIKSVVPGGAADADGRLQAGDQLLRVDGQSLIGITQERAADYLVRTGPVVSLEVAKQGAIYHGLATLLQQPSPVIQRGNRRMSERDLTRMGGAESTKSLGPLIANNHPNHSLSLSQHLNNSHNNTLGNSNNSSIINPLAAHLPNSKSVPALHHHTGSGTISLANSKSRSTHSLHNNTSGMGGIGGAAAGGMLGQPNGSQNNANGNGNGNEQGFYQNLSVYRAQNQSQPILNERPPIAAHAAMNAYNGSSPLAPQQQPQQQQQSPYQQQQQQQHMQANANLPPTRPVSAYYHSQQSAQQQLQQQQQQQQQHSLQQQQFALSSGNLNGQQQQQQQHQHQHQLTLNNRTKSQQNFQHTLRMQQMMAPSMPNISNMYHHQQQQQQQLPLQQQQQQQQQPLMSSSQSMQNVNDFAGGYQNGSLEYRRSQLHDPSTLYEIQQQQLQQQQQQQQQQQQQQQASPNFIALPPKPLGSLQSPNKPNVPPSTAPKPQQDKPPLPPTATHPLFKATQQIAPGMNYVASTLDPPKGSYVASNQGNNRPLHSGSNPWEREEREKDLEMRREHIRQWREQQISELSQIVSRSPMQEEQLKTLILERDFERRAQELQEQEEQDQEQQYDKENVQELFRLAGGGQVSAIQTPITSYRQTEIKLAEMPDSNSLVDSVPPQPPAPTAQPLSSNTQQPKSILKHNRYSEGGVGPSGAPSSPSKSQKSASFADERHLHTEHPISNLAKELNQLTMLDKDNNNETLDAVVPPPPPPERNSSYLIMSQQKLRGSTGNATSSMGLLKTATSNQAAAAVEIKKASLLNTQTNNNNNLSGSLNNNTMHGSPLSAMELNAAYVSATGTGIIGGLGTPPPPPPLMQRDNKRVSFHDEENNFVSGNSQQQQLQQQYIMDNYGMEHQDLDTIREDTSYLQHNLDASMLPSMPATPDAALWNTSVQSTPGVIGAQEVYRDPRTRRLAEKQQQQQQQRAGDAVPEKLSFKEKMKMFALESGEDKTPKDKLKISRAQRDIDAVH
Protein: Protein CHROMATIN REMODELING 25 (AtCHR25) (EC 3.6.4.-) (DNA repair and recombination protein RAD54) (AtRAD54) (Q0PCS3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Dissociates RAD51 from nucleoprotein filaments formed on dsDNA. Could be involved in the turnover of RAD51 protein-dsDNA filaments. Addition of RAD54 overcomes inhibition of DNA strand exchange by RAD51 bound to substrate dsDNA. Species preference in the RAD51 dissociation and DNA strand exchange assays underlines the importance of specific RAD54-RAD51 interactions. RAD51 is unable to release dsDNA upon ATP hydrolysis, leaving it stuck on the heteroduplex DNA product after DNA strand exchange (By similarity). Involved in DNA repair and mitotic recombination. Functions in the homologous recombinational DNA repair (RAD52) pathway. Required for synthesis-dependent strand annealing (SDSA) during double-strand break repair.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P32863}.
Interaction partners:
- DNA repair protein RAD51 homolog 1
- Crossover junction endonuclease MUS81
- DNA ligase 4
- ATP-dependent DNA helicase 2 subunit KU70
- Exonuclease 1
- DNA repair protein RAD51 homolog 3
- Protein VAC14 homolog
- ATP-dependent DNA helicase 2 subunit KU80
- ATP-dependent DNA helicase Q-like 4A
- DNA repair protein XRCC3 homolog
Sequence:
MEEEDEEILSSSDCDDSSDSYKDDSQDSEGENDNPECEDLAVVSLSSDADRKSKNVKDLLRGNLVVQRQPLLPRVLSVSDGAAVCRKPFKPPCSHGYDSTGQLSRRLSARKRFVPWGSSTPVVVALPTKLEASTNIERDEEEEVVCLPPDIEPLVLWQSEEDGMSNVTTIMVHSVLVKFLRPHQREGVQFMFDCVSGLHGSANINGCILADDMGLGKTLQSITLLYTLLCQGFDGTPMVKKAIIVTPTSLVSNWEAEIKKWVGDRIQLIALCESTRDDVLSGIDSFTRPRSALQVLIISYETFRMHSSKFCQSESCDLLICDEAHRLKNDQTLTNRALASLTCKRRVLLSGTPMQNDLEEFFAMVNFTNPGSLGDAAHFRHYYEAPIICGREPTATEEEKNLAADRSAELSSKVNQFILRRTNALLSNHLPPKIIEVVCCKMTTLQSTLYNHFISSKNLKRALADNAKQTKVLAYITALKKLCNHPKLIYDTIKSGNPGTVGFENCLEFFPAEMFSGRSGAWTGGDGAWVELSGKMHVLSRLLANLRRKTDDRIVLVSNYTQTLDLFAQLCRERRYPFLRLDGSTTISKRQKLVNRLNDPTKDEFAFLLSSKAGGCGLNLIGANRLVLFDPDWNPANDKQAAARVWRDGQKKRVYVYRFLSTGTIEEKVYQRQMSKEGLQKVIQHEQTDNSTRQGNLLSTEDLRDLFSFHGDVRSEIHEKMSCSRCQNDASGTENIEEGNENNVDDNACQIDQEDIGGFAKDAGCFNLLKNSERQVGTPLEEDLGSWGHHFTSKSVPDAILQASAGDEVTFVFTNQVDGKLVPIESNVSPKTVESEEHNRNQPVNKRAFNKPQQRPREPLQPLSLNETTKRVKLSTYKRLHGNSNIDDAQIKMSLQRPNLVSVNHDDDFV
Protein: Inositol polyphosphate-5-phosphatase D (H0Y5Q9)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
KREGFCQLLQQMKNKHSEQPEPDMITIFIGTWNMGNAPPPKKITSWFLSKGQGKTRDDSADYIPHDIYVIGTQEDPLSEKEWLEILKHSLQEITSVTFKTVAIHTLWNIRIVVLAKPEHENRISHICTDNVKTGIANTLGNKGAVGVSFMFNGTSLGFVNSHLTSGSEKKLRRNQNYMNILRFLALGDKKLSPFNITHRFTHLFWFGDLNYRVDLPTWEAETIIQKIKQQQYADLLSHDQLLTERREQKVFLHFEEEEITFAPTYRFERLTRDKYAYTKQKATGMKYNLPSWCDRVLWKSYPLVHVVCQSYGSTSDIMTSDHSPVFATFEAGVTSQFVSKNGPGTVDSQGQIEFLRCYATLKTKSQTKFYLEFHSSCLESFVKSQEGENEEGSEGELVVKFGETLPKLKPIISDPEYLLDQHILISIKSSDSDESYGEGCIALRLEATETQLPIYTPLTHHGELTGHFQGEIKLQTSQGKTREKLYDFVKTERDESSGPKTLKSLTSHDPMKQWEVTSRAPPCSGSSITEIINPNYMGVGPFGPPMPLHVKQTLSPDQQPTAWSYDQPPKDSPLGPCRGESPPTPPGQPPISPKKFLPSTANRGLPPRTQESRPSDLGKNAGDTLPQEDLPLTKPEMFENPLYGSLSSFPKPAPRKDQESPKMPRKEPPPCPEPGILSPSIVLTKAQEADRGEGPGKQVPAPRLRSFTCSSSAEGRAAGGDKSQGKPKTPVSSQAPVPAKRPIKPSRSEINQQTPPTPTPRPPLPVKSPAVLHLQHSKGRDYRDNTELPHHGKHRPEEGPPGPLGRTAMQ
Protein: Fasciclin-like arabinogalactan protein 9 (Q9ZWA8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be a cell surface adhesion protein.
Subcellular location: Cell membrane; Lipid-anchor, GPI-anchor.
Interaction partners:
- Fasciclin-like arabinogalactan protein 18
- Fasciclin-like arabinogalactan protein 3
- Fasciclin-like arabinogalactan protein 14
- Fasciclin-like arabinogalactan protein 15
- Fasciclin-like arabinogalactan protein 16
- Fasciclin-like arabinogalactan protein 17
- Fasciclin-like arabinogalactan protein 21
- Putative fasciclin-like arabinogalactan protein 20
- Fasciclin-like arabinogalactan protein 19
- Fasciclin-like arabinogalactan protein 5
Sequence:
MATTRLTLAPLLLIAAVLLATKATAQPAAPAPEPAGPINLTAILEKGGQFTTFIHLLNITQVGSQVNIQVNSSSEGMTVFAPTDNAFQNLKPGTLNQLSPDDQVKLILYHVSPKYYSMDDLLSVSNPVRTQASGRDNGVYGLNFTGQTNQINVSTGYVETRISNSLRQQRPLAVYVVDMVLLPGEMFGEHKLSPIAPAPKSKSGGVTDDSGSTKKAASPSDKSGSGEKKVGLGFGLGLIVLCLKFLF