wanglab/gogpt-training-data huggingface dataset:
Protein: Uncharacterized protein Rv2212 (P9WMU7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Probable cytosol aminopeptidase
- Aminomethyltransferase
- CRP-like cAMP-activated global transcriptional regulator
- Probable cyclase
- Branched-chain-amino-acid aminotransferase
- Adenylate cyclase
- Probable conserved transmembrane protein
Sequence:
MYDSLDFDALEAAGIANPRERAGLLTYLDELGFTVEEMVQAERRGRLFGLAGDVLLWSGPPIYTLATAADELGLSADDVARAWSLLGLTVAGPDVPTLSQADVDALATWVALKALVGEDGAFGLLRVLGTAMARLAEAESTMIRAGSPNIQMTHTHDELATARAYRAAAEFVPRIGALIDTVHRHHLASARTYFEGVIGDTSASVTCGIGFADLSSFTALTQALTPAQLQDLLTEFDAAVTDVVHADGGRLVKFIGDAVMWVSSSPERLVRAAVDLVDHPGARAAELQVRAGLAYGTVLALNGDYFGNPVNLAARLVAAAAPGQILAAAQLRDMLPDWPALAHGPLTLKGFDAPVMAFELHDNPRARDADTPSPAASD
Protein: Cadherin (O15202)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
EIQSYHMEVEASDGGGLSGKCTVAIEVMDINDNAPELTMSLLISDILENSPETVVAVFGISDPDSGNNGKMMCSIQDHLPFLLKPTLENFYTLLTEGALDRESRAEYNITITVTDLGTPRLKTEYKHYLRVSDV
Protein: FH2 domain-containing protein 1 (Inverted formin-1) (Q9C0D6)
Organism: Homo sapiens (Human)
Function: Microtubule-associated formin which regulates both actin and microtubule dynamics. Induces microtubule acetylation and stabilization and actin stress fiber formation. Regulates Golgi ribbon formation. Required for normal cilia assembly. Early in cilia assembly, may assist in the maturation and positioning of the centrosome/basal body, and once cilia assembly has initiated, may also promote cilia elongation by inhibiting disassembly.
Subcellular location: Cell projection, cilium {ECO:0000269|PubMed:29742020}. Golgi apparatus {ECO:0000250|UniProtKB:Q3ULZ2}. Note=Associates with microtubules. {ECO:0000269|PubMed:18815276}.
Interaction partners:
- Profilin-4
- E3 ubiquitin-protein ligase RNF135
- Protein phosphatase Slingshot homolog 2
Sequence:
MHVMNCVSLVSDKENGNIATAPGFMIGQTPPPAPPPPPPPPPPSPPCSCSREECPSSPPPPPPPPLPGEPPIPPPPPGLPPTTHMNGYSHLGKKKRMRSFFWKTIPEEQVRGKTNIWTLAARQEHHYQIDTKTIEELFGQQEDTTKSSLPRRGRTLNSSFREAREEITILDAKRSMNIGIFLKQFKKSPRSIVEDIHQGKSEHYGSETLREFLKFLPESEEVKKLKAFSGDVSKLSLADSFLYGLIQVPNYSLRIEAMVLKKEFLPSCSSLYTDITVLRTAIKELMSCEELHSILHLVLQAGNIMNAGGYAGNAVGFKLSSLLKLADTKANKPGMNLLHFVAQEAQKKDTILLNFSEKLHHVQKTARLSLENTEAELHLLFVRTKSLKENIQRDGELCQQMEDFLQFAIEKLRELECWKQELQDEAYTLIDFFCEDKKTMKLDECFQIFRDFCTKFNKAVKDNHDREAQELRQLQRLKEQEQKQRSWATGELGAFGRSSSENDVELLTKKGAEGLLPFLHPRPISPSSPSYRPPNTRRSRLSLGPSADRELLTFLESSTGSPEEPNKFHSLPRSSPRQARPTIACLEPAEVRHQDSSFAHKPQASGGQEEAPNPPSAQAHQLAAAQPENHASAFPRARRQGVSVLRKRYSEPVSLGSAQSPPLSPLALGIKEHELVTGLAQFNLQGSQGMEETSQLTLSDFSPMELESVGHRGPQSLSASSSSLTPMGRDALGSLSPALEDGKAAPDEPGSAALGSVGSSDPENKDPRPLFCISDTTDCSLTLDCSEGTDSRPRGGDPEEGGEGDGSMSSGVGEMGDSQVSSNPTSSPPGEAPAPVSVDSEPSCKGGLPRDKPTKRKDVVAPKRGSLKEASPGASKPGSARRSQGAVAKSVRTLTASENESMRKVMPITKSSRGAGWRRPELSSRGPSQNPPSSTDTVWSRQNSVRRASTGAEEQRLPRGSSGSSSTRPGRDVPLQPRGSFKKPSAKPLRNLPRQKPEENKTCRAHSEGPESPKEEPKTPSVPSVPHELPRVPSFARNTVASSSRSMRTDLPPVAKAPGITRTVSQRQLRVKGDPEDAAPKDSSTLRRASSARAPKKRPESAEGPSANTEAPLKARGAGERASLRRKDSSRTTLGRILNPLRK
Protein: Matrix metallopeptidase 28 (Epilysin) (Matrix metalloproteinase-28 variant A) (Q8CGV5)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MVAGVSLLLRALPLLLWGCQDAQPTQHGLPELRQEAEAFLEKYGYLSEQGSKAPASAQFRNAIREFQWISQLPLSGVLDQATLRQMTRPRCGVADTDSHATWTERISTLLAGHRAKMRRKKRFAKPGNKWYKQHLSYRLVNWPERLPEPAVRGAVRAAFQLWSNVSALEFWEAPATGPADIRLTFFQGDHNDGLANAFDGPGGALAHAFLPRRGEAHFDGDERWSLSRRRGRNLFVVLAHEIGHTLGLTHSPAPRALMAPYYKKLGRDALLSWDDVLAVQSLYGKPLGRSVATQLPGKVFTDFEAWDPHNSQSRRPETRGPKYCHSSFDAITVGSYFWEVTVDGNVSEPRPLQKRWPGLPPGIEAAAVSLEDGDFYFFKGNRCWRFQGTKSVWGFAQLCRAGGLPRHPDAALFFPPLRRLVLFKGSRYYVLAQGGMQVEPYYPRSLRDWAGVPEEVSGALPRPDGSIIFFRDDHYWHLDQAKLRVTSSGRWATELSWMGCWNANSGGALF
Protein: Uncharacterized membrane protein YohP (C1P609)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane {ECO:0000305|PubMed:19121005, ECO:0000305|PubMed:21778229}; Single-pass membrane protein {ECO:0000269|PubMed:19121005, ECO:0000269|PubMed:21778229}. Note=May be able to insert into the membrane in both orientations. Depletion of SecE or YidC does not affect membrane insertion.
Interaction partners:
- Uncharacterized membrane protein YkgR
- Uncharacterized protein YncL
- Uncharacterized protein IlvX
- Uncharacterized protein YshB
Sequence:
MKIILWAVLIIFLIGLLVVTGVFKMIF
Protein: Homologous-pairing protein 2 homolog (Protein AHP2) (AtAHP2) (Protein ARABIDOPSIS HOMOLOG PAIRING 2) (Protein HOP2) (AtHOP2) (Q9FX64)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in bivalent formation and segregation of homologous chromosomes in meiosis.
Subcellular location: Nucleus {ECO:0000269|PubMed:12974806}.
Interaction partners:
- Meiotic nuclear division protein 1 homolog
- Meiotic recombination protein DMC1 homolog
- Meiotic recombination protein SPO11-1
- Meiotic recombination protein SPO11-2
- DNA repair protein RAD51 homolog 1
- Meiosis-specific protein ASY1
- MND1-interacting protein 1
- DNA topoisomerase 6 subunit A
- DNA repair protein recA homolog 1, chloroplastic
- DNA mismatch repair protein MSH4
Sequence:
MAPKSDNTEAIVLNFVNEQNKPLNTQNAADALQKFNLKKTAVQKALDSLADAGKITFKEYGKQKIYIARQDQFEIPNSEELAQMKEDNAKLQEQLQEKKKTISDVESEIKSLQSNLTLEEIQEKDAKLRKEVKEMEEKLVKLREGITLVRPEDKKAVEDMYADKINQWRKRKRMFRDIWDTVTENSPKDVKELKEELGIEYDEDVGLSFQAYADLIQHGKKRPRGQ
Protein: LIM/homeobox protein Lhx3 (G3V9E7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
- Insulin gene enhancer protein ISL-1
- LIM domain binding 1
- LIM domain binding 2
- Pituitary-specific positive transcription factor 1
- Neurogenin 2
- Insulin gene enhancer protein ISL-2
- Pituitary homeobox 1
- Motor neuron and pancreas homeobox 1
Sequence:
MEARGELDPSRESAGGDLLLALLARRADLRREIPMCAGCDQHILDRFILKALDRHWHSKCLKCSDCHVPLAERCFSRGESVYCKDDFFKRFGTKCAACQLGIPPTQVVRRAQDFVYHLHCFACVVCKRQLATGDEFYLMEDSRLVCKADYETAKQREAEATAKRPRTTITAKQLETLKSAYNTSPKPARHVREQLSSETGLDMRVVQVWFQNRRAKEKRLKKDAGRQRWGQYFRNMKRSRGSSKSDKDSIQEGQDSDAEVSFTDEPSMADMGTANGLYSSLGEPAPALGRPVGGLGSFTLEHGGLAGPEQFRELRPGSPYGIPPSPAAPQSLPGPQPLLSSLVYPDTNLGLVPSGPPGGPPPMRVLAGNGPSSDLSTESSGGYPDFPASPASWLDEVDHAQF
Protein: Far upstream element binding protein 3 (A0A8I6ATS5)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MAELVQGQSAPVGLKAEDFVDALHRVRQIAAKIDSIPHLNNSTPLVDPSVYGYGVQKRPLDDGVGNQLGALVHQRAVITEEFKVPDKMVGFIIGRGGEQISRIQAESGCKIQIASESSGIPERPCVLTGTPESIEQAKRLLGQIVDRCRNGPGFHNDIDGNSTIQELLIPASKVGLVIGKGGETIKQLQERTGVKMVMIQDGPLPTGADKPLRITGDPFKVQQAREMVLEIIREKDQADFRGVRSDFTSRAGGGSIEVSVPRFVVGIVIGRNGEMIKKIQNDAGVRIQFKPDDGISPERAAQVMGPPDRCQHAARIINELILTAQEREILGGLTGTRGRGRGRGDWSVGTPGGIQEITYTVPADKCGLVIGKGGENIKSINQQSGAHVELQRNPPPNTDPNLRIFTIRGAPQQIEVARHLIDEKVGGASLGAPTAFGQSPFSQPPAAPHQNTFPPRAFPNIAAKVNGNPHSTPVSGPPAFLTQGWGSTYQAWQQPTQQVPSQQSQPQNSQPDYSKAWEDYYKKQADDGLHQPNSDAQPLGSCEVKPTLCGSFTL
Protein: Importin beta-1 subunit, putative (Q38BV5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- GTP-binding nuclear protein
- Ribosomal RNA-processing protein 8
- Importin subunit alpha
- Sperm-associated antigen 6
- Nucleoporin
- Delta
- Nuclear cap-binding protein subunit 2
- Nucleoporin NSP1-like C-terminal domain-containing protein
- Nucleoporin
- Importin N-terminal domain-containing protein
Sequence:
MSSLTELLTALGSPDPSVRIPAEEQVNRAKQGGLGGFLCSLLEEFRDESKPLFARNMAGTLLKNAVAPNLRETAARRALEREWKNLPVALRTEVKQCVLSTLGSPKKDIQNVAANIIGNLSRIELPAGEWPDLMDILISATESQSEFHQVAALTAIGYVCEEGHDHEDVEAALINYTGGILNAVVCGMNSGKEEVCYCATNALCNAMEFIHDNMQQQNQRDLLVDTLCRTVASSHNSRTREKAMESLVKVADMYYSTLPNYIDRLHAITTGAIFGEEEGVALQAMLFWISICETELDMKESADPRCLFYAQKGASMLVNICLQTIVRQEEGQEEGDWNIAIAGGKLLQSLAMCIQDPVVDLVMPFVYSNIEGATWREKEAAVLAFGCILNGPNADKIQDTVAQAVPGLLQYIRHDHPLVADTAGWVLATVCELFGDVFLLQPWNLQQLINIVTPMIGEGTEKAIRGCHIVHNLSLTYEEEDCQPTNELSRYFAELLNVLLLAIDKGVDYTVKSVAQEALNALIDAAAVDCLQFLNLLVPELHKRIYNVLGERQQGQVGEMEASSLLGLLCGSLGSTARKLMLAFNEHLQPSMEIVLKILENPQGTVLEEVLTMLGSFAHAVKQGMAPYLDRITGHVVKALQCVDEPDLVTVAVGTVGDLSLGVQKDLAPYVEGILGALYGNLQNPEVDRCVKCIFLNCIGDIVLNVGEANFAQYVNIFMPFVHSMFEQSCGVNVTDDPDNEEYVMSLWESISTLYTSVCQSFKGNEIPLAPYLQNMLQFVLYTAPLAKSHGYVEVFIAIITVIGDMASVLKSVSLKELRQQAQSALLSSEVVAIVKVAAELNDGRDGFREQVRWVESQLQQLSKVV
Protein: Probable calcium-binding protein CML14 (Calmodulin-like protein 14) (Q8VZ50)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Potential calcium sensor.
Interaction partners:
- Probable calcium-binding protein CML36
- Probable calcium-binding protein CML43
- Probable calcium-binding protein CML34
- Probable calcium-binding protein CML32
- Calcium-binding protein CML42
- Probable calcium-binding protein CML35
- Calcium-binding protein CML39
- Probable calcium-binding protein CML31
- Probable calcium-binding protein CML21
- Probable calcium-binding protein CML44
Sequence:
MSKDGLSNDQVSSMKEAFMLFDTDGDGKIAPSELGILMRSLGGNPTESQLKSIITTENLSSPFDFNRFLDLMAKHLKTEPFDRQLRDAFKVLDKEGTGFVAVADLRHILTSIGEKLQPSEFDEWIKEVDVGSDGKIRYEDFIARMVAK
Protein: Coiled-coil domain-containing glutamate-rich protein 1 (Q8TC90)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000269|PubMed:38081819}. Note=Forms condensates in the nucleus through liquid-liquid phase separation. {ECO:0000269|PubMed:38081819}.
Interaction partners:
Sequence:
MTQTLDTREDPLNLGGGGGGGCGCGWAHSASLSSWSSCHRRRPGAPAYNRPHRYSPKTEYGPPRKQPKQQHGPGFWFQPPVCSNWGCWGGPWRPPPPGFWKFPCPVQVFRVYGLHPLCFCCCSCWSGSWNPGWVKPPGRKKRWGRRGRGLRHHPRHSYPRSPPADVSTLPRPVKLYEWREPGMRAPPNTTQFIMNQIYEDMRQQEKVERQQEALRAQKATVSGEASPARSSGNDAPPGGSKETWGLQETLYGFVQNPSLAFSPNPEENQSLAPLLVEEEEEKKNDDEEEYDQEVCDAKEASEEEEEVEDEEEEVEDEEEEEVEEAEYVEEGEEELEEEELEEEEEVLEENEQRGEEFHLPLEMPLSIFVEAEEKRENFISCTFLNPEQIIPKVPQESLFMAQDFNC
Protein: Uncharacterized protein (Q4GZ58)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MQRDVYASLIKKRHKQMVPLLIHQVSGDITRENIFDEVFHGYKLRRIVLMTHMAATPATLPRLPRDIIVSDFDKLKAIHQPHFHYKLLPLLCTDFEAFSALQGICASANSPFTIEDRKDPQGLTHRLSNGCSERQALCEFFDPHIAPAEKLVPVFSRKLPISAVVFDGLLLKQNYPKVAALLTVHEAASEKSIIERAIMRDFFVSPLYTKVSGNSDVAQSLRLVHHCTHFMALKRAVGSDAPSRQSLMRLAAEKKLFMYEKIGDEYQFVH
Protein: Nipped-B protein (Q1XG44)
Organism: Xenopus laevis (African clawed frog)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU364107}.
Interaction partners:
Sequence:
MNGDMPHVPITTLAGIASLTDLLNQLPLPSPLPATTTKSLLFNGRIAEEVNCLLTCRDEPLVSQLIHSLNQVSTDHIELKDNLGSDDPEGDIPVLLQATLARNPNVFREKSLQNRYGVQSGLMIPPYKLPQNSMHGSPASSNYQQTTISHSPSSRFVPPQSSSTNRFIGQQNSPVPSPYAPQSPAGYMPYSHPGGYPQHQGLQQASVSSPIVAGGLRNLHENKVSGQLSGSSANHHADNSRHGTTEDYLQMVHRLGGEDSDSSIRNAASFSLRSPQSVCSPAGSEGTPKGSRPLILQTQPPPYSSPRDAPPDILLDSPDRKQRRPKKLKLSKDDKEQTEKSAMYDIISSPSKDSTKLTLRLTRVRSSEMDQQGDMLSNMENSNLSEGDAAFNAQFPGNASKTPVTPQDLSRPLNAAACFQEQSEFLQVQQVPVLQPNTSAAAKPPQPLVAQSQPQQTGNITPYDEVELDALAEIERIERESAIERERFSKEVQDKDKPLKKRKQDSYPLEAGGATGGNRPASQETGSAGNGSRPALMVSIDLQHAGRGDSQATVTQDSDCARKADNIKNCNDGYISGPQEDTVFKHNPENHPLRKSESDMECPDKSIKSTTANLSTERGLEKSLNETKLCDIKSEPVECSEEAKVSSDCPTEAKSESCEVDYDDSMMDFKNSEGSNEDIKTEALLNETSNDVKSFDLQDESKENGNQSKSSKIDNRLEIRQKQKQNDGQPETPRQKFEGKSEALQQKVEVKSEASKQKAEGKPETIRQKSEVKSDTLKQKTEGHPETPKQKNENKPETPKQRSDSKPETQKQKNDSKPDTPKQKSEGRPETPKQKSESRPNTPKQKSEGRQDTSRQKNEGRQEINRQKSEEHKSDGRPETPKHKHDMKKDSNRLSTEKKPDLSKHKTDSKSDSPRVKPEGRTDGVKQRIDGRPSHESSKRDCDNPKQKHDDKGESEKHKGEMSRLRRPESLRSFSKNDQETRPGSKPDTPKMDKAEKKHRRDSDDSREKHSSGEQKQRPGSPRIKQDSKSDPNKSDSSKLKSDKPALKSPTGKEEKRTDGNKSKVEGNKGHSDNKTGFPSYLLGGNQGTLKNFVIPKLKRDKDGNITQESKRSESKGEQMDKPEKMGFVEDLNKGAKPVVVLQKLSLDEVQKLIKERDDKSKGSLKSNKNRPSKSSKGGIDQSVLKELPPELVAEIESSMPLCERVKMNTRKRGAVKEKPKYTEISSGEDEEREETFEPSRKRPKKGKSDADWQYDGERERRSSGDHRRSGNDSRRGSRYRERSAEDSEMEDSPPPPRLSEVARRLKKERQKKRKAYEPKLTPEEMMDSSTFKRFSSAVENILENLEDMDFSAFGDDDEIPQEMLLGKHQLSELGSESAKIKSMGIMNKISSEKMVKLLGILEKNIQDGSKLSTMLNHNDTEDEEKLWRDLIMERVTKSADACLTAINIMTSQSMPKAVYIEDVIEHVIQYTKYHLQNTLYPQYDPVYRVDPHGGGLMSSKAKRAKCSTHKQRVIVMLYNKICDIVASLSELLEIQLLTDTTILQVSSMGITPFFVENVSELQLCAIKLVTAVFSRYEKHRQLILEELFTSLARLPTSKRSLRNFRLNSSDDAGESMYIQMVTALVLQLIQCVVHLPSDKDNAEEESNKKIDQDVFITNSYETAMRTAQNFLSIFLKKCGSKQGEEDYRPLFENFVQDLLSTVNKPEWPAAELLLSLLGRLLVHQFSNKSTEMALRVASLDYLGTVAARLRKDAVTSKMDQGSINRILKQASEGDEIQQLQKALLDYLEENTETDPSLVFSRKFYIAQWFRDTTMETEKAMKSQKDDDEGTLHAKEVESTGDIMRQAEKRKKFLRNIIRTAPSQFSTLKSNSDTVDYDDACLIVRYLASMRPFAQSFDIYLTQILRVLGENAIAVRTKAMKCLSEVVAVDPSILARLDMQRGVHGRLMDNSTSVREAAVELLGRFVLCRPQLAEQYYEMLIERILDTGISVRKRVIKILRDICLEQPTFPKITEMCVKMIRRVNDEEGIKKLVNETFQKLWFTPTPQNDKEAMTRKILNITDVVAACRDTGFDWFEQLLQNLLKSEEDASYKPVKKACTQLVDNLVEHILKYEESLADSDSKGVNSGRLVACITTLFLFSKIRPQLMVKHAMTMQPYLTTKCSTQNDFMVICNVAKILELVVPLMEHPSETFLATIEEDLMKLIIKYGMTVVQHCVSCLGAVVNKVTQNYKFVWACFNRYYGALLKLKSQHQEDPNNTILTTNKPALLRSLFTVGALCRHFDFDQEEFKGSSKVNISVNIKDKVLELLLYFTKHSDEEVQTKAIIGLGFSFIQHPVLMFEVEVKNLYNSILSDKNCSVNLKIQVLKNLQTYLQEEDTRMQQADRDWKKMSKQEDLKEMGDISSGMSSSIMQLYLKQVLESFFSTQSSVRHFALNVIALTLNQGLIHPVQCVPYLIAMGTDPEPSMRNKSDQQLVEIDKKYTGFIHMKAVAGIKMSYQVQQAIISNANQIVRGFRKDETNSALCSHLYSMIRGNRQHRRAFLISLLNLFDDAAKTEVNMLLYIADNLACFPYQTQEEPLFIMHHIDITLSVSGSNLLQSFKESMVKGKQKVKAASSNEENSSESDEEVIRPKKTRRRGNDESDSDGEDDVEHVLRCLPNNASPLIEFANASQGILLLLMLKQHIKNLCGFSDSKIQKYSPSESAKVYDKTINRKHAVLFRPKQTLEYLKRNMTCAKINDEVKRSIAKQYLDFKMLMEHLDPDEEEEEGEVSASTDARNKAITNLLGGNSPKNNVAETEEEESDGEEKAGGTSGLRKSKRLSDSSDAAVQMNETVDVQDVIAICCPKYKDRPQIAKVVQKTSHGFSVQWMAGSYSGPWAEAKRRDGRKLVPWVDTIKESDIIYKKIALTSANKLTNKVAQTLRSLYAAKDGTSS
Protein: Ankyrin repeat domain-containing protein 9 (Q96BM1)
Organism: Homo sapiens (Human)
Function: Substrate receptor subunit of a cullin-RING superfamily E3 ligase complex (CUL5-based E3 ubiquitin ligase complex) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Depending of the metabolic state of the cell, promotes the proteasomal degradation of IMPDH2, the rate-limiting enzyme in GTP biosynthesis or protects IMPDH2 by stabilizing IMPDH2 filaments assembly. Implicated in different cellular processes, like copper homeostasis and cell proliferation.
Subcellular location: Cytoplasmic vesicle {ECO:0000269|PubMed:31337707}. Cytoplasm, cytosol {ECO:0000269|PubMed:30293565, ECO:0000269|PubMed:31337707}. Note=Detected in long filamentous cytosolic structures where it colocalizes with IMPDH2 (PubMed:31337707). Under basal conditions ANKRD9 is mainly in vesicle-like structures, upon nutrient limitation (guanine nucleotides deficiency) ANKRD9 loses its vesicular pattern and assembles with IMPDH2 into rodlike filaments (PubMed:31337707). {ECO:0000269|PubMed:31337707}.
Interaction partners:
- Elongin-C
- Elongin-B
- Cullin-5
- Inosine-5'-monophosphate dehydrogenase 2
- RING-box protein 2
- E3 ubiquitin-protein ligase RBX1
- Kelch domain-containing protein 1
- Ankyrin repeat and SOCS box protein 4
Sequence:
MPWDARRPGGGADGGPEASGAARSRAQKQCRKSSFAFYQAVRDLLPVWLLEDMRASEAFHWDERGRAAAYSPSEALLYALVHDHQAYAHYLLATFPRRALAPPSAGFRCCAAPGPHVALAVRYNRVGILRRILRTLRDFPAEERARVLDRRGCSRVEGGGTSLHVACELARPECLFLLLGHGASPGLRDGGGLTPLELLLRQLGRDAGATPSAAGAPASAPGEPRQRRLLLLDLLALYTPVGAAGSARQELLGDRPRWQRLLGEDKFQWLAGLAPPSLFARAMQVLVTAISPGRFPEALDELPLPPFLQPLDLTGKG
Protein: Large ribosomal subunit protein mL64 (39S ribosomal protein L59, mitochondrial) (Growth arrest and DNA damage-inducible proteins-interacting protein 1) (Q9VP13)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Large ribosomal subunit protein uL11m
- Large ribosomal subunit protein mL40
- Large ribosomal subunit protein mL62
- Large ribosomal subunit protein mL49
- Large ribosomal subunit protein bL28m
- Large ribosomal subunit protein mL41
- Ribosomal protein
- Large ribosomal subunit protein uL4m
- Large ribosomal subunit protein uL22m
- Large ribosomal subunit protein uL30m
Sequence:
MNVGKISVVTRLPALRSCAQYSSAAKAELPASLVGDVDVEPTYPQTVDRSGLQPQHKNVLLNKLPYQEPHSWIHLTEKYQRQAFGRYGAQSNVNPKICFDSHGEKDSRQVMQLETLLKMLEKNRAQKAEELARINAREEDIAKKMEKLTQWKADLHAKIAKREADAAAAIQRKERLVEEVRRHFGFKVDTRDERFKEMLEQKEKEDKKKQKEAKRKAKEEKMMAKLVEKASV
Protein: Taste receptor type 2 member 16 (T2R16) (T2R18) (T2R3) (Taste receptor type 2 member 118) (Q9JKU0)
Organism: Rattus norvegicus (Rat)
Function: Gustducin-coupled receptor implicated in the perception of bitter compounds in the oral cavity and the gastrointestinal tract. Signals through PLCB2 and the calcium-regulated cation channel TRPM5.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9NYV7}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Taste receptor type 2 member 38
- Taste receptor type 2 member 106
- Taste receptor type 2 member 107
Sequence:
MVPTQVTIFSIIMYVLESLVIIVQSCTTVAVLFREWMHFQRLSPVEIILISLGISHFCLQWTSMLYNFGTYSRPVLLFWKVSVVWEFMNVLTFWLTSLLAVLYCVKVSSFSHPVFLWLRLKILKLVLWLLLGALIASCLSIIPSVVKYHIQMELLTLDHLPKNSSLILRLQMFEWYFSNPFKMIGFGVPFLVFLISIILLTVSLVQHWGQMKHYSSSSSSLRAQCTVLKSLATFFIFFTSYFLTIVVSFIGTVFDKKSWFWVCEAVIYGLVCIHFTSLMMSNPTLKKALRLQFWSPESS
Protein: Mitosis inducer protein blt1 (O74338)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: At the onset of mitosis, forms a medial ring structure before the arrangement of the medial actin ring. Essential for the central positioning of the division septum before the cell divides.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:14655046, ECO:0000269|PubMed:19474789}.
Interaction partners:
- Kinesin-like protein 8
- Rho guanine nucleotide exchange factor gef2
- Mitosis inducer protein kinase cdr2
- Anillin-related medial ring protein mid1
- Cell division control protein 15
- Mitosis inducer protein kinase cdr1
- Uncharacterized protein C12B10.10
- Ras GTPase-activating-like protein rng2
- Myosin type-2 heavy chain 1
- Cell division control protein 12
Sequence:
MSKSAFTSKSQLKGIDGSFNDPFRQPSMNLPTPPHDDGLPSIPRSTALPNLSNRLSPYSHRNYLPIPEADSRNLEVLNSISLTTGSVVNQINKLYQRSCDNANYLQDLRSLILQTPTAEANATQVTESLNQIQKILQEASSKDREQIVQVIKELNKGNSLEVRRELGNCLAHLKKGTLNIDNALQASLQKYWKELQYFNVSKDKLLSLEESIKLLSARLEETDTPSSTHWIEINAGFKEVGDELSENFQRKQEILSGLQNNVILRTNNRKPVGSDGSNSNFNGGEEQMDSKDQEEIQDYLNSLLSVHEKDGVLLQKFHNSYVQYQKLAVALSKYENFDADKLFQQMNLAKQSNETLLQTLTEQTDQLLSFKETMDSFKFILGPSMENQALQQGILAEQQDLVAQLRDIVLRSETLAENPSNMPGSCLPGASSNTADEFTEQLNLLKNEVARLSAICPSPNSGINASVLTNADNLEKENLLLVNNNAFKVDDRSVSSVALDDHNRQLQMNVEELEGKKADLTSKINRLDKDFVKLNTTYSLLTDQVKTKQLALQEIESRVIRLEERLNMLQKLSMQPAISSSSEFVPIESHPSSSAVVPIEEPKNSIIEKKRVPHNAARNSVNLEVTLPNSKKRFSSFSGSSSKLPVRPSTALTDKRKPSWSRRLAAAIGFSSGSPEKKHVITSSDAGHQRSKSRSFSSKM
Protein: ATP synthase F(1) complex subunit gamma, mitochondrial (ATP synthase F1 subunit gamma) (F-ATPase gamma subunit) (P36542)
Organism: Homo sapiens (Human)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and the central stalk which is part of the complex rotary element. The gamma subunit protrudes into the catalytic domain formed of alpha(3)beta(3). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P05631}; Peripheral membrane protein {ECO:0000250|UniProtKB:P05631}; Matrix side {ECO:0000250|UniProtKB:P05631}.
Interaction partners:
- ATP synthase F
- ATP synthase peripheral stalk subunit OSCP, mitochondrial
- ATP synthase F
- ATP synthase peripheral stalk subunit b, mitochondrial
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase peripheral stalk subunit d, mitochondrial
- ATP synthase F
Sequence:
MFSRAGVAGLSAWTLQPQWIQVRNMATLKDITRRLKSIKNIQKITKSMKMVAAAKYARAERELKPARIYGLGSLALYEKADIKGPEDKKKHLLIGVSSDRGLCGAIHSSIAKQMKSEVATLTAAGKEVMLVGIGDKIRGILYRTHSDQFLVAFKEVGRKPPTFGDASVIALELLNSGYEFDEGSIIFNKFRSVISYKTEEKPIFSLNTVASADSMSIYDDIDADVLQNYQEYNLANIIYYSLKESTTSEQSARMTAMDNASKNASEMIDKLTLTFNRTRQAVITKELIEIISGAAALD
Protein: C-hairy1A (Hes family bHLH transcription factor 4) (Q6XLQ0)
Organism: Gallus gallus (Chicken)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MPADTGMEKPTASPIAGAPASASHTPDKPRSASEHRKSSKPIMEKRRRARINESLGQLKMLILDALKKDSSRHSKLEKADILEMTVKHLRNLQRAQMAAALSADPSVLGKYRAGFNECMNEVTRFLSTCEGVNADVRARLLGHLSACLGQIVAMNYLPPPPAGQPAHLAQPLHVQLPPTTTGAVPVPCKLEPTEALSPKVYGGFQLVPATDGQFAFLIPNPAFPPGSGPVIPLYANANVPVSTSGGSGNASTTPSASPVQGLTSFGHSVVPASQAGSPIAERRESVWRPW
Protein: Rho GTPase-activating protein conundrum (Q8T0G4)
Organism: Drosophila melanogaster (Fruit fly)
Function: GTPase-activating protein (GAP) for Rho1; functions with the ERM protein Moe to regulate Rho1 and control proliferation in the developing epithelium. Recruited by Moe to the cell cortex where it negatively regulates Rho1 activity. Can also promote cell proliferation independently of its GAP activity, perhaps by acting with Arf51F (Arf6) to positively regulate Rac1.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23468526}. Cell membrane {ECO:0000269|PubMed:23468526}; Peripheral membrane protein {ECO:0000269|PubMed:23468526}. Cytoplasm, cell cortex {ECO:0000269|PubMed:23468526}. Cell junction {ECO:0000269|PubMed:23468526}. Note=Recruited by Moe to the cell cortex. In the epithelium, predominately expressed at the apical cortex. {ECO:0000269|PubMed:23468526}.
Interaction partners:
- RE33981p
Sequence:
MNSNTDLHHSDDQDFSEFLNEYYLQSNSQSIEPEASYEDGEMEAEWLVSAGYPELTKPFEQGLEVSKKDLEPILTTLSKPHAEAIVQLVRTLNKTVRVRTKSRPKRKPDIRDVFREFDEQGTVTRSRSATPDSLDSLQIDEAWTNNSLPTFVNVYEKNTETAIQCVEQSNEIYLKQNLRRTPSAPPKSGTYADIFRGSQVRCDIPLYSADGVELLGYSRIGTIQFPRNRSVSDPFCSIGRSKESRSENDARSQKKKSSEVLSASENECGRLLPMPYNVLSFESICRDSSSLDSCEVLDTCDIPSTLFTDVVLISETDMKRLQTILWLELATIFDRNKVSLDKRKPFKRRRKEEGNLFGVSINALIRRDQQVTGTDSSLVPLFLEKLIGELLRRGSREEGLLRIGGHKQKTELLYNELESTFYQNPDNLDNLFRTATVHELSSLLKRWLRELPQPLLTNELIQLFYQCHTLPSIDQMNALSILCHLLPPENRNTLRSLLSFFNIIINLKDINKMNVHNVATIMAPSMFPPRYIHPSDNNSIAEQVRMAAQCCRLTNILILRGEKLFQVPNNLIVESQKTMMGKKGWHRHRNSNEITAKPSGKASNVGVGHDSTVINKYSTNLKHLHPFVI
Protein: D-2-hydroxyacid dehydrogenase (D2-HDH) (EC 1.1.1.-) (D-specific 2-hydroxyacid dehydrogenase) (Q2VEQ7)
Organism: Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4) (Halobacterium mediterranei)
Function: Catalyzes the stereospecific NAD(P)H-dependent reduction of 2-ketocarboxylic acids into the corresponding D-2-hydroxycarboxylic acids. Can use both NADPH or NADH as reductant, displaying a marked preference for NADPH over NADH. Shows a broad substrate specificity, although it displays a marked preference for the 2-ketocarboxylic acids having an unbranched chain of 4-5 carbon atoms.
Interaction partners:
Sequence:
MHIERLAVDESVGRAMPPQRFIEALSDLGVPVEFAGEDEQFGPGDAVASFGHRDAFLDADWVHCIRAGYDEFPVGVYEEAGTYLTNSTGIHGTTVGETVAGYMLTFARRLHAYRDAQHDHAWDLPRYEEPFTLAGERVCVVGLGTLGRGVVDRAAALGMEVVGVRRSGDPVDNVSTVYTPDRLHEAIADARFVVLATPLTDETEGMVAAPEFETMREDASLVNVARGPVVVESDLVAALDSGDIAGAALDVFSEEPLPEDSPLWDFEDVLITPHVSAATSKYHEDVAALIRENIEKIATGDELTNRVV
Protein: Insulin-like growth factor-binding protein 2-B (IGF-binding protein 2-B) (IGFBP-2-B) (IGFBP-2b) (B3F211)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Si:dkey-58f6.2.
- GAS2-like protein 3
Sequence:
MSLALLCSLLLVHGSLGEIVFRCPSCTAERQAACPKLTTSCEIVREPGCGCCPVCARQKGELCGVYTTRCGSGLRCYPSANSELPLEQLIQGLGRCENKVDLEPTMTNQESAAHSGEVNGTRSPPMKKPGKDYQYIKEIAVNKHHNNKRTRMYNTQDDPKTPHPKQSQCQQELDKVLENISRMAFHDNKGPLENLYDLKFPNCDKTGQYNLKQCHMSTHGQRGECWCVNPYTGVQIPSSDKVRGDPNCSQYYGGPELEPPTAQQK