wanglab/gogpt-training-data huggingface dataset:
Protein: Kinase suppressor of ras 1 (A0A8I6ADF9)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MHCLWSWVTTKASRDPETPPPTLPREAQGSSRPASDENCEEIPQELTLDALLEMDEAKAKEMLRRWGASAEECSRLQQALTCLRKVTGLGGEHKEDSGWSSAEARESSSGPSVDMLSSLGRAGASTQGPRSISVSALPASDSPVPGLSEGLSDTCIPLHTSGRLTPRALHSFITPPTTPQLRRHAKLKPPRTPPPPSRKVFQLLPSFPTLTRSKSHESQLGNRIDEVAPMRFELPHGSPQLVRRDIGLPVTHRFSTKSWLSQVCNVCQKSMMFGVKCKHCRLKCHNKCTKEAPACRISFLPLARLRRTESVPSDINNPVDRAAEPHFGTLPKALTKKEHPPAMNLDSSSNPSSTTSSTPSSPAPFLTSSNPSSATTPPNPSPGQRDSRFNFPDISACPQAAPLSSTADSTRLDDQPKTDVLGVPEAEAEEPEAGKSEAEDDEDEIDDLPSSRRHWRGPISRKASQTSVYLQEWDIPFEQVELGEPIGQGRWGRVHRGRWHGEVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVVITDFGLFGISGVVREERRENQLKLSHDWLCYLAPEIVREMIPGRDEDQLPFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGSGEGVKRVLASVSLGKEVGEILSACWAFDLQERPSFSLLMDMLEKLPKLNRRLSHPGHFWKSADRWRSRYYGKGRYGHPDFKSSCPLLEEYANSSKVMPRFERFGLGTLESSNPKM
Protein: Pimeloyl-[acyl-carrier protein] methyl ester esterase (EC 3.1.1.85) (Biotin synthesis protein BioH) (Carboxylesterase BioH) (Q8GHL1)
Organism: Serratia marcescens
Function: The physiological role of BioH is to remove the methyl group introduced by BioC when the pimeloyl moiety is complete. It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway through the hydrolysis of the ester bonds of pimeloyl-ACP esters. Also displays a weak thioesterase activity. Can form a complex with CoA, and may be involved in the condensation of CoA and pimelic acid into pimeloyl-CoA, a precursor in biotin biosynthesis.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01260, ECO:0000269|PubMed:12527210}.
Interaction partners:
- 8-amino-7-oxononanoate synthase
- Malonyl-[acyl-carrier protein] O-methyltransferase
- Putative aminotransferase.
- Putative dethiobiotin synthetase
- ATP-dependent dethiobiotin synthetase BioD
- Thioesterase-3
- Biotin synthase
Sequence:
MTALYWQTIGEGERDLVLLHGWGLNAEVWSCIQALTPHFRLHLVDLPGYGRSQGFGALSLAQMTEIVLAAAPPQAWWLGWSLGGLVASQAALMQPQRVSGLITVASSPCFAARDEWPGIRPDVLSGFQHQLSLDFQRTVERFLALQTLGTESARQDARQLKAVVLNQPTPSVEVLNGGLEILRTADLRAPLAELNLPLLRIYGYLDGLVPRKVAELLDAAWPNSTSQIVAKAAHAPFISHPDEFVTMIEAFIAAH
Protein: succinate dehydrogenase (EC 1.3.5.1) (Q726C8)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Interaction partners:
- Succinate--CoA ligase subunit alpha
- Fumarate reductase, cytochrome b subunit
- succinate dehydrogenase
- Tartrate dehydratase alpha subunit, putative
- Tartrate dehydratase beta subunit, putative
- Fumarate hydratase class II
- Pyruvate:ferredoxin oxidoreductase
- L-aspartate oxidase, putative
- Adenylyl-sulphate reductase, alpha subunit
- Fumarate reductase iron-sulfur subunit
Sequence:
MGRTLVFNIFRHDPQDAVSTPRMDTFRLQETDRMTLFIALHRLREEQDPSLKFDFCCRAGVCGSCAMVINGRPGLACHTKTRDLPDTITLLPLPVFKLVGDLAVDTGTWFRAMYQRTESWVHTSVPFDEHAAEARMENETANAIYELDRCIECGCCVAACGTANMRPDFLAPAGFLRVARFLADPRDERDLNAYYELIGTEDGIFGCMGLLACEDVCPKHLPLQNQLGYLRRKLGITAIRRLLPFAK
Protein: tRNA-dihydrouridine(47) synthase [NAD(P)(+)]-like (EC 1.3.1.89) (Zinc finger CCCH domain-containing protein 50) (AtC3H50) (mRNA-dihydrouridine synthase DUS3 homolog) (EC 1.3.1.-) (tRNA-dihydrouridine synthase 3-like) (Q9T0J6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs. Specifically modifies U47 in cytoplasmic tRNAs (By similarity). Catalyzes the synthesis of dihydrouridine in some mRNAs, thereby affecting their translation (By similarity).
Interaction partners:
- Zinc finger CCCH domain-containing protein 43
- Zinc finger CCCH domain-containing protein 68
- Ribosome biogenesis protein BOP1 homolog
- Zinc finger CCCH domain-containing protein 13
- Zinc finger CCCH domain-containing protein 45
- E3 ubiquitin-protein ligase makorin
- Zinc finger CCCH domain-containing protein 5
- Zinc finger CCCH domain-containing protein 18
- Nucleolar-like protein
- Zinc finger CCCH domain-containing protein 2
Sequence:
MSDVIAEHAVDTSVEGDAKAALPVQSTKQFSVYEATSEELIERSMAPIKKEFLCPPPPSRSVKQNDAADVRAPQSGLVQEKKSKRQLKRERREQSTINLCPQVARTEDVDSCQYKDKCRFNHDIEAFKAQKADDIEGQCPFVASGMKCAYGLSCRFLGSHRDITGNSDDKEKSEMNFFNKETQRLLWKNKMTFTNADAKLKSLGLLGHAKKSNAAEEITAEKTQNGMNGTQATEVAVDSAVSSEHTSEMIQDVDIPGPLETEEVRPMKKAKSEDQKNSKTGDVGGVYDGVKLEEETKKNGYPTSKANVEDEDSIKIVETDSSLKLHPREKKKLIDFRDKLYLAPLTTVGNLPFRRLCKVLGADVTCGEMAMCTNLLQGQASEWALLRRHSSEDLFGVQICGSYPDTVSRVVELIDRECTVDFIDINMGCPIDMVVNKSAGSALLNKPLRMKNIVEVSSSIVETPITIKVRTAFFEGKNRIDSLIADIGNWGATAVTIHGRSRQQRYSKSADWDYIYQCTKNATTNLQVIGNGDVYSYLDWNKHKSDCPELSSCMIARGALIKPWIFTEIKEQRHWDITSGERLNIMKDFVRFGLQHWGSDTKGVETTRHFLLEWLSYTFRYIPVGLLDVIPQQINWRPPSYFGRDDLETLMMSESAGDWVRISEMLLGKVPEGFTFAPKHKSNAYDRAENG
Protein: Threonine--tRNA ligase 2, cytoplasmic (EC 6.1.1.3) (Threonyl-tRNA synthetase) (ThrRS) (Threonyl-tRNA synthetase protein 3) (Q8BLY2)
Organism: Mus musculus (Mouse)
Function: Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged tRNA(Thr) via its editing domain, at the post-transfer stage.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:29579307}. Nucleus {ECO:0000269|PubMed:29579307}. Note=Primarily cytoplasmic. Also detected at lower levels in the nucleus. {ECO:0000269|PubMed:29579307}.
Interaction partners:
- Bifunctional glutamate/proline--tRNA ligase
- Threonine--tRNA ligase 1, cytoplasmic
- Leucine--tRNA ligase, cytoplasmic
- Threonine--tRNA ligase, mitochondrial
- Probable leucine--tRNA ligase, mitochondrial
- Tyrosine--tRNA ligase, cytoplasmic
- Alanine--tRNA ligase, cytoplasmic
- Valine--tRNA ligase
- Lysine--tRNA ligase
- Isoleucine--tRNA ligase, cytoplasmic
Sequence:
MAAQALAAQAVASRLQRQEEDIRWLCAEVQRLRDEQLRGPERGQAEGPRLTREVAQLQAENRDLHQRLCGLRLRLAEQRRTEAGRAAAHEPPTQNQEKDTKKKRLKQSEPGREVKQPNFIKERLQLFETLKTDHQLLPATQEKKNTNNVISVRVAGGKTVQGERWKTTPYQVAAGISKELAEHTVIAKVNGVLWDLDRPLEGDSTVELLMFDNEEAQAVYWHSSAHILGEAMELYYGGHLCYGPPIENGFYYDMFIEDRVVSSTELSALENICKTIIKEKQPFERLEVSKDTLLEMFKYNKFKCRILKEKVDTPTTTVYRCGPLIDLCKGPHVRHTGKIKAIKIFKNSSTYWEGNPEMETLQRIYGISFPDSKMMKDWEKFQEEAKSRDHRKIGKEQELFFFHDLSPGSCFFLPRGAFIYNALMDFIREEYHKRNFTEVLSPNMYNSKLWETSGHWQHYSNNMFTFDVEKDTFALKPMNCPGHCLMFAHRPRSWREMPVRFADFGVLHRNELSGTLSGLTRVRRFQQDDAHIFCMVEQIEEEIKGCLHFLQSVYSTFGFSFQLNLSTRPEHFLGEIEIWDEAERQLQNSLVEFGKPWKINPGDGAFYGPKIDIKIKDAIGRYHQCATIQLDFQLPIRFNLTYVSKDGDDKNRPVIIHRAILGSVERMIAILSENYGGKWPLWLSPRQVMVIPVGPACENYALQVSKECFEEGFMADVDLDDSCTLNKKIRNAQLAQYNFILVVGEKEKINNAVNVRTRDNKIHGEISIASVIEKLKNLKKSRTLNAEEDF
Protein: Alpha-D-glucose 1-phosphate phosphatase YihX (Alpha-D-glucose-1-P phosphatase) (EC 3.1.3.10) (Alpha-D-glucose-1-phosphatase) (Haloacid dehalogenase-like phosphatase 4) (HAD4) (P0A8Y3)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the dephosphorylation of alpha-D-glucose 1-phosphate (Glc1P) and, to a lesser extent, of other sugar phosphates. Has no activity with the beta form of Glc1P. In addition, YihX has significant phosphatase activity against pyridoxal phosphate (PLP) and low beta-phosphoglucomutase activity.
Interaction partners:
- UPF0761 membrane protein YihY
- Aldose 1-epimerase
- Phosphoglucomutase
- Uncharacterized protein YihR
- Glucose-1-phosphatase
- Glucokinase
- Probable acyltransferase FabY
- D-aminoacyl-tRNA deacylase
- UTP--glucose-1-phosphate uridylyltransferase
- Glycogen phosphorylase
Sequence:
MLYIFDLGNVIVDIDFNRVLGAWSDLTRIPLASLKKSFHMGEAFHQHERGEISDEAFAEALCHEMALPLSYEQFSHGWQAVFVALRPEVIAIMHKLREQGHRVVVLSNTNRLHTTFWPEEYPEIRDAADHIYLSQDLGMRKPEARIYQHVLQAEGFSPSDTVFFDDNADNIEGANQLGITSILVKDKTTIPDYFAKVLC
Protein: SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 4 (A0A2R8Y4P4)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSTPDPPLGGTPRPGPSPGPGPSPGAMLGPSPGPSPGSAHSMMGPSPGPPSAGHPIPTQGPGGYPQDNMHQMHKPMESMHEKGMSDDPRYNQMKGMGMRSGGHAGMGPPPSPMDQHSQGYPSPLGGSEHASSPVPASGPSSGPQMSSGPGGAPLDGADPQALGQQNRGPTPFNQNQLHQLRAQIMAYKMLARGQPLPDHLQMAVQGKRPMPGMQQQMPTLPPPSVSATGPGPGPGPGPGPGPGPAPPNYSRPHGMGGPNMPPPGPSGVPPGMPGQPPGGPPKPWPEGPMANAAAPTSTPQKLIPPQPTGRPSPAPPAVPPAASPVMPPQTQSPGQPAQPAPMVPLHQKQSRITPIQKPRGLDPVEILQEREYRLQARIAHRIQELENLPGSLAGDLRTKATIELKALRLLNFQRQLRQEVVVCMRRDTALETALNAKAYKRSKRQSLREARITEKLEKQQKIEQERKRRQKHQEYLNSILQHAKDFKEYHRSVTGKIQKLTKAVATYHANTEREQKKENERIEKERMRRLMAEDEEGYRKLIDQKKDKRLAYLLQQTDEYVANLTELVRQHKAAQVAKEKKKKKKKKKAENAEGQTPAIGPDGEPLDETSQMSDLPVKVIHVESGKILTGTDAPKAGQLEAWLEMNPGYEVAPRSDSEESGSEEEEEEEEEEQPQAAQPPTLPVEEKKKIPDPDSDDVSEVDARHIIENAKQDVDDEYGVSQALARGLQSYYAVAHAVTERVDKQSALMVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWAYEFDKWAPSVVKVSYKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKVDLNEEETILIIRRLHKVLRPFLLRRLKKEVEAQLPEKVEYVIKCDMSALQRVLYRHMQAKGVLLTDGSEKDKKGKGGTKTLMNTIMQLRKICNHPYMFQHIEESFSEHLGFTGGIVQGLDLYRASGKFELLDRILPKLRATNHKVLLFCQMTSLMTIMEDYFAYRGFKYLRLDGTTKAEDRGMLLKTFNEPGSEYFIFLLSTRAGGLGLNLQSADTVIIFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLCTVNSVEEKILAAAKYKLNVDQKVIQAGMFDQKSSSHERRAFLQAILEHEEQDEEEDEVPDDETVNQMIARHEEEFDLFMRMDLDRRREEARNPKRKPRLMEEDELPSWIIKDDAEVERLTCEEEEEKMFGRGSRHRKEVDYSDSLTEKQWLKKITGKDIHDTASSVARGLQFQRGLQFCTRASKTLKAIEEGTLEEIEEEVRQKKSSRKRKRDSDAGSSTPTTSTRSRDKDDESKKQKKRGRPPAEKLSPNPPNLTKKMKKIVDAVIKYKDSSSGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVFTSVRQKIEKEDDSEGEESEEEEEGEEEGSESESRSVKVKIKLGRKEKAQDRLKGGRRRPSRGSRAKPVVSDDDSEEEQEEDRSGSGSEED
Protein: Protoporphyrinogen oxidase (PPO) (EC 1.3.3.4) (Q10062)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX.
Subcellular location: Mitochondrion {ECO:0000250}.
Interaction partners:
- Ferrochelatase, mitochondrial
- Uroporphyrinogen decarboxylase
- Probable oxygen-dependent coproporphyrinogen-III oxidase
- Delta-aminolevulinic acid dehydratase
- Porphobilinogen deaminase
- 5-aminolevulinate synthase, mitochondrial
- Uroporphyrinogen-III synthase
Sequence:
MSIAICGGGIAGLSTAFYLARLIPKCTIDLYEKGPRLGGWLQSVKIPCADSPTGTVLFEQGPRTLRPAGVAGLANLDLISKLGIEDKLLRISSNSPSAKNRYIYYPDRLNEIPSSILGSIKSIMQPALRPMPLAMMLEPFRKSKRDSTDESVGSFMRRRFGKNVTDRVMSAMINGIYAGDLNDLSMHSSMFGFLAKIEKKYGNITLGLIRALLAREILSPAEKALKAALLAEPKTAELSNSMKSTSMFAFKEGIETITLSIADELKKMPNVKIHLNKPAKTLVPHKTQSLVDVNGQAYEYVVFANSSRNLENLISCPKMETPTSSVYVVNVYYKDPNVLPIRGFGLLIPSCTPNNPNHVLGIVFDSEQNNPENGSKVTVMMGGSAYTKNTSLIPTNPEEAVNNALKALQHTLKISSKPTLTNATLQQNCIPQYRVGHQDNLNSLKSWIEKNMGGRILLTGSWYNGVSIGDCIMNGHSTARKLASLMNSSS
Protein: Slit homolog 1 protein (Slit-1) (Q80TR4)
Organism: Mus musculus (Mouse)
Function: Thought to act as molecular guidance cue in cellular migration, and function appears to be mediated by interaction with roundabout homolog receptors. During neural development involved in axonal navigation at the ventral midline of the neural tube and projection of axons to different regions (By similarity). SLIT1 and SLIT2 together seem to be essential for midline guidance in the forebrain by acting as repulsive signal preventing inappropriate midline crossing by axons projecting from the olfactory bulb.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Roundabout homolog 2
- Roundabout homolog 1
- Roundabout homolog 4
- Roundabout homolog 3
- Netrin-1
Sequence:
MALTPQRGSSSGLSRPELWLLLWAAAWRLGATACPALCTCTGTTVDCHGTGLQAIPKNIPRNTERLELNGNNITRIHKNDFAGLKQLRVLQLMENQIGAVERGAFDDMKELERLRLNRNQLQVLPELLFQNNQALSRLDLSENFLQAVPRKAFRGATDLKNLQLDKNRISCIEEGAFRALRGLEVLTLNNNNITTIPVSSFNHMPKLRTFRLHSNHLFCDCHLAWLSQWLRQRPTIGLFTQCSGPASLRGLNVAEVQKGEFSCSGQGEAAGAPACTLSSGSCPAMCSCSSGIVDCRGKGLTAIPANLPETMTEIRLELNGIKSIPPGAFSPYRKLRRIDLSNNQIAEIAPDAFQGLRSLNSLVLYGNKITDLPRGVFGGLYTLQLLLLNANKINCIRPDAFQDLQNLSLLSLYDNKIQSLAKGTFTSLRAIQTLHLAQNPFICDCNLKWLADFLRTNPIETTGARCASPRRLANKRIGQIKSKKFRCSAKEQYFIPGTEDYHLNSECTSDVACPHKCRCEASVVECSSLKLSKIPERIPQSTTELRLNNNEISILEATGLFKKLSHLKKINLSNNKVSEIEDGTFEGAASVSELHLTANQLESIRSGMFRGLDGLRTLMLRNNRISCIHNDSFTGLRNVRLLSLYDNHITTISPGAFDTLQALSTLNLLANPFNCNCHLSWLGDWLRKRKIVTGNPRCQNPDFLRQIPLQDVAFPDFRCEEGQEEVGCLPRPQCPQECACLDTVVRCSNKHLQALPKGIPKNVTELYLDGNQFTLVPGQLSTFKYLQLVDLSNNKISSLSNSSFTNMSQLTTLILSYNALQCIPPLAFQGLRSLRLLSLHGNDVSTLQEGIFADVTSLSHLAIGANPLYCDCRLRWLSSWVKTGYKEPGIARCAGPPEMEGKLLLTTPAKKFECQGPPSLAVQAKCDPCLSSPCQNQGTCHNDPLEVYRCTCPSGYKGRHCEVSLDGCSSNPCGNGGTCHAQEGEDAGFTCSCPSGFEGPTCGVDTDDCVKHACVNGGVCVDGVGNYTCQCPLQYTGRACEQLVDFCSPDMNPCQHEAQCVGTPDGPRCECMLGYTGDNCSENQDDCKDHKCQNGAQCVDEVNSYACLCVEGYSGQLCEIPPAPRSSCEGTECQNGANCVDQGSRPVCQCLPGFGGPECEKLLSVNFVDRDTYLQFTDLQNWPRANITLQVSTAEDNGILLYNGDNDHIAVELYQGHVRVSYDPGSYPSSAIYSAETINDGQFHTVELVTFDQMVNLSIDGGSPMTMDNFGKHYTLNSEAPLYVGGMPVDVNSAAFRLWQILNGTSFHGCIRNLYINNELQDFTKTQMKPGVVPGCEPCRKLYCLHGICQPNATPGPVCHCEAGWGGLHCDQPVDGPCHGHKCVHGKCVPLDALAYSCQCQDGYSGALCNQVGAVAEPCGGLQCLHGHCQASATKGAHCVCSPGFSGELCEQESECRGDPVRDFHRVQRGYAICQTTRPLSWVECRGACPGQGCCQGLRLKRRKLTFECSDGTSFAEEVEKPTKCGCAQCA
Protein: Mitochondrial translation factor 2 (Protein NAM1) (P10849)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for the processing and/or for the stability of the CYTB and COX1 intron-containing pre-mRNAs and of the ATP6 transcript. Could be a stem-loop RNA-binding protein that plays a role in determining RNA stability.
Subcellular location: Mitochondrion matrix.
Interaction partners:
- DNA-directed RNA polymerase, mitochondrial
- General control transcription factor GCN4
- Mitochondrial COX1 translation regulator PET309
- Protein PET111
- Cytochrome c oxidase subunit 1
- Sigma-like sequence protein 1, mitochondrial
- Mitochondrial transcription factor 1
- Cytochrome b
- COX3 mRNA-specific translational activator PET494
- Leucine--tRNA ligase, mitochondrial
Sequence:
MIRTSSILKNCNYRYIHCIHRCLLNEANLKDRKTHNVERVSNEKTFEQALEEERKVFGELFEAGARVENMRHTNASKIIDKYYNGLQDNSEGTSVKKEKIVFNHSQRAQRKLPNKDHEFLKETAGNDYVYERAEPSAISTKTISEQTRTLLEKIFDEDNSINKSNRELLNLNLRKGSGMEALRQPVAHSNVKFSEEVMQEIGNKIRYQTTLDQVLEPHIDYLREAVKSDYDLLRYLKQSLDIYKKRNKDLELKMNAESSNIFEDIRSACINKPAELPKPLAMTLPYIIVKSLRLGDFDFPADRKYTLISYVYNECKNNMDASLYLTICNVDFYNLLVQLLWENFQEIRYLRRVVTEMSVNGVIGNIETVDILDKIVKEMRSLNEDVFLEAGEQLSADEEVSSSANKIVNVGVLWNKDTNNDLLIVENYLKSLKKNLTRDR
Protein: Nucleoredoxin (EC 1.8.1.8) (Protein Red-1) (P97346)
Organism: Mus musculus (Mouse)
Function: Functions as a redox-dependent negative regulator of the Wnt signaling pathway, possibly by preventing ubiquitination of DVL3 by the BCR(KLHL12) complex. May also function as a transcriptional regulator act as a regulator of protein phosphatase 2A (PP2A).
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:16604061}. Nucleus {ECO:0000269|PubMed:10903915, ECO:0000269|PubMed:9119370}.
Interaction partners:
- Segment polarity protein dishevelled homolog DVL-1
Sequence:
MSGFLEELLGDKLVTGGGEEVDVHSLGARGIALLGLYFGCSLSAPCAQLSASLAAFYGRLRGDAAAGPGAGAGAGAAAEPEPRHRLEIVFVSSDQDQRQWQDFVRDMPWLALPYKEKHRKLKLWNKYRVSNIPSLIFLDATTGKVVCRNGLLVIRDDPEGLEFPWGPKPFREVIAGPLLRNNGQSLESSSLEGSHVGVYFSAHWCPPCRSLTRVLVESYRKIKEAGQEFEIIFVSADRSEESFKQYFSEMPWLAVPYTDEARRSRLNRLYGIQGIPTLIVLDPQGEVITRQGRVEVLNDEDCREFPWHPKPVLELSDSNAVQLNEGPCLVLFVDSEDDGESEAAKQLIQPIAEKIIAKYKAKEEEAPLLFFVAGEDDMTDSLRDYTNLPEAAPLLTILDMSARAKYVMDVEEITPAIVETFVNDFLAEKLKPEPI
Protein: Rho-related protein racJ (Q9GPQ9)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- Rac guanine nucleotide exchange factor B
- Uncharacterized protein
- Ras guanine nucleotide exchange factor S
- GTPase activating protein homolog 1
- Mss4-like family protein
- Cofilin-1A
Sequence:
MERNFNNFLVKIFCLGDDGVGKSCVMNSYSSGGPLTSLFQGSELTWTDYTVSVTHNQKPLKLRLVIGDQNELRRIKQIEFNDVFLICFSVDSKASYDNIEKWNTEIRKILPTPNIILVGTKIDLRKEGGELKKSIVTQEMGIEKAKEINAIKYMECSTATYEGVKEVFDESINIYMTKKLYIQDLRKKSFLIPKKNTNKKSCKTQ
Protein: Transcriptional regulator ATRX (EC 3.6.4.12) (ATP-dependent helicase ATRX) (X-linked nuclear protein) (F1MQ85)
Organism: Bos taurus (Bovine)
Subcellular location: Chromosome, telomere {ECO:0000256|ARBA:ARBA00004574}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Death domain-associated protein 6
- Methyl-CpG-binding protein 2
- HSR domain-containing protein.
- DNA repair protein RAD51 homolog 1
- PH-interacting protein
- Cohesin subunit SA
- Structural maintenance of chromosomes 5.
- Serine-protein kinase ATM
- Nipped-B protein
- Histone H3.3
Sequence:
MTAEPMSESKLNTLVQKLHDFLAHSSEESEETSSPPRLVMNQSTDKASGSGNNSDMMENSREEGASSAEKSKSSGSSRSKRKPSIVTKYVESDDEKTLDETVNEDASNENSENDITMQSLPKGTVIVQPEPVLNEDKDDFKGPEFRSRSKMKTENLKKRGDGLHGIVSCTACGQQVNHFQKDSIYRHPSLQVLICKNCFKYYMSDDISRDSDGMDEQCRWCAEGGNLICCDFCHNAFCKKCILRNLGRKELSTIMDENNQWYCYICHPEPLLDLVTACNSVFENLEQLLQQNKKKIKVDNEKTSKVYEHAPRFSPKKNSSNCNGEEKKLDDSYSGSVTYSYSALIVPKDMIKKAKKLIETTANMNSSYVKFLKQATDNSEINSATKLRQLKAFKSVLADIKKAHLALEEDLNSEIQALDAVNKEKNTKEHKVIDAKSETKVRKGEKPCVLERKDISKSEGKLSRKQVDSEHIGQSVAVEEQRAHKNDSTEHKKSDKKEPQYEPSNTAEDLDMDIVSVPSSVPEDIFENLETAMEVQSSAEYQGDGNSGTEQELETSVKLNITSKDNRGGIKSKTTAKVTKELYVKLTPVSLSISPIKGADCQEVPQDKDSYKSSCLNPKPENCELGQEKNDNEHLAKSEVPLLSEESDLRRSPRVKTTPLRRQTETNRTTSNSDEENNETVKEQQKLSVPMRKKDKRNSSDSAIDNPKPNKLPKSKQSEIVDHISDSDEMLTILKDMPSMSHSSSDTDINEPHTNNKKTFYSEIQRGKDDKRKRKRKSSTSGSDFDIKKGKSVKKAIISKKKRQNQSESSNYDSELEKEIKRMSKIGTARTTKKRVPNKEYYDSSEDEKHSKQGMDNQGHKSLRTAQEGSSDDVERKQERENFSSAEGTVDKDKTIMELRDRLSKKQQPNVSSESADKLCSGKEESFNSPEDKKVAESKGKSKHQRTRMCQKILGGLCDVAEKFSEKEQSDESSEDDNEQSKKEIEEKEKKTADLNKKVMEQEYESSSDTTEKLPEGEEICDFPKSIKQNKSSADGEKKCKKIKDKASKKKGELSDNSEKLPGKRESCDSSEDKRSKNGTSSREKKRFNLPEKSSRKRQDCSSSDTEKYSMKEDDCDFSDKRPKGIELRERRNLNSNRNSKEVQSGSSSDVEESSEDNKNLKKQRALAKKKAGSIKEKMRNSLRTSTKRKQADITSSSSDIGDDDQKSVGEGSSDEQKIKPVTENLVLSSHTGFCQSSGDEALSKSVPVTVDDDDDDNDPENRIAKKMLLEEIKANLSSDEDGSSDESEEGKKRTGKHNEENPGDEEIKNQAISESDSDSEESKKPRYRHRLLRHKLTLSDGESGEEKKMKPKEHKEAKSRNRRKVSSEDSEDSDFQESGVSEEVSESEDEQRPRTRSAKKAELEENQRSYKQKKKRRRIKVQEDSSSENKSNSEEDKEEDEEEDEEEDENDDSKSPGKGRKKIRKILKDDKLRTETQNALKEEEERRKRIAEREREREKLREVIEIEDASPTKCPITTKLVLDEDEETKEPLVQVHRNMVIKLKPHQVDGVQFMWDCCCESVKKTKKSPGSGCILAHCMGLGKTLQVVSFLHTVLLCDKLDFSTALVVCPLNTALNWMNEFEKWQEGLKDDEKLEVSELATVKRPQERSYMLQRWQEDGGVMIIGYEMYRNLAQGRNVKSRKLKEIFNKALVDPGPDFVVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNGQCADSTMVDVRVMKKRAHILYEMLAGCVQRKDYTALTKFLPPKHEYVLAVRMTPIQCKLYQYYLDHLTGVGNSSEGGRGKAGAKLFQDFQMLSRIWTHPWCLQLDYISKENKGYFDEDSMDEFIASDSDETSMSLSSDDYTKKKKAKGKKGKKDSSSSGSGSDNDVEVIKVWNSRSRGGGEGNVDETGNNPSVSLKLEESKATSSSNPSSPAPDWYKDFVTDADAEVLEHSGKMVLLFEILRMAEEIGDKVLVFSQSLISLDLIEDFLELASREKTEDKDKPLIYKGEGKWLRNIDYYRLDGSTTAQSRKKWAEEFNDETNVRGRLFIISTKAGSLGINLVAANRVIIFDASWNPSYDIQSIFRVYRFGQTKPVYVYRFLAQGTMEDKIYDRQVTKQSLSFRVVDQQQVERHFTMNELTELYTFEPDLLDDPNSEKKKKRDTPMLPKDTILAELLQIHKEHIVGYHEHDSLLDHKEEEELTEEERKAAWAEYEAEKKGLTMRFNIPTGTNLPPVSFNSQTPYIPFNLGALSAMSNQQLEDLINQGREKVVEATNSVTAVRIQPLEDIISAVWKENMNLSEAQVQALALSRQASQELDVKRREAIYNDVLTKQQMLISCVQRILMNRRLQQQYNQQQQQQMTYQQATLGHLMMPKPPNLIMNPSNYQQIDMRGMYQSVAGGMQPPPLQRAPPPMRSKNPGPSPGKSM
Protein: Adhesion G protein-coupled receptor L4 (EGF, latrophilin and seven transmembrane domain-containing protein 1) (EGF-TM7-latrophilin-related protein) (ETL protein) (Q9HBW9)
Organism: Homo sapiens (Human)
Function: Endothelial orphan receptor that acts as a key regulator of angiogenesis.
Subcellular location: Cell membrane {ECO:0000269|PubMed:23871637}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Endomucin
Sequence:
MKRLPLLVVFSTLLNCSYTQNCTKTPCLPNAKCEIRNGIEACYCNMGFSGNGVTICEDDNECGNLTQSCGENANCTNTEGSYYCMCVPGFRSSSNQDRFITNDGTVCIENVNANCHLDNVCIAANINKTLTKIRSIKEPVALLQEVYRNSVTDLSPTDIITYIEILAESSSLLGYKNNTISAKDTLSNSTLTEFVKTVNNFVQRDTFVVWDKLSVNHRRTHLTKLMHTVEQATLRISQSFQKTTEFDTNSTDIALKVFFFDSYNMKHIHPHMNMDGDYINIFPKRKAAYDSNGNVAVAFVYYKSIGPLLSSSDNFLLKPQNYDNSEEEERVISSVISVSMSSNPPTLYELEKITFTLSHRKVTDRYRSLCAFWNYSPDTMNGSWSSEGCELTYSNETHTSCRCNHLTHFAILMSSGPSIGIKDYNILTRITQLGIIISLICLAICIFTFWFFSEIQSTRTTIHKNLCCSLFLAELVFLVGINTNTNKLFCSIIAGLLHYFFLAAFAWMCIEGIHLYLIVVGVIYNKGFLHKNFYIFGYLSPAVVVGFSAALGYRYYGTTKVCWLSTENNFIWSFIGPACLIILVNLLAFGVIIYKVFRHTAGLKPEVSCFENIRSCARGALALLFLLGTTWIFGVLHVVHASVVTAYLFTVSNAFQGMFIFLFLCVLSRKIQEEYYRLFKNVPCCFGCLR
Protein: Auxin response factor 8 (Protein FRUIT WITHOUT FERTILIZATION) (Q9FGV1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Auxin response factors (ARFs) are transcriptional factors that bind specifically to the DNA sequence 5'-TGTCTC-3' found in the auxin-responsive promoter elements (AuxREs). Seems to act as transcriptional activator. Formation of heterodimers with Aux/IAA proteins may alter their ability to modulate early auxin response genes expression. Regulates both stamen and gynoecium maturation. Promotes jasmonic acid production. Partially redundant with ARF6. Involved in fruit initiation. Acts as an inhibitor to stop further carpel development in the absence of fertilization and the generation of signals required to initiate fruit and seed development.
Subcellular location: Nucleus.
Interaction partners:
- Transcription factor BPE
- Auxin-responsive protein IAA9
- Auxin-responsive protein IAA19
- Auxin-responsive protein IAA6
- Transcription factor PIF4
- Auxin-responsive protein IAA17
- Auxin transporter protein 1
- Auxin-responsive protein IAA1
- Protein TRANSPORT INHIBITOR RESPONSE 1
- Auxin-responsive protein IAA8
Sequence:
MKLSTSGLGQQGHEGEKCLNSELWHACAGPLVSLPSSGSRVVYFPQGHSEQVAATTNKEVDGHIPNYPSLPPQLICQLHNVTMHADVETDEVYAQMTLQPLTPEEQKETFVPIELGIPSKQPSNYFCKTLTASDTSTHGGFSVPRRAAEKVFPPLDYTLQPPAQELIARDLHDVEWKFRHIFRGQPKRHLLTTGWSVFVSAKRLVAGDSVIFIRNEKNQLFLGIRHATRPQTIVPSSVLSSDSMHIGLLAAAAHASATNSCFTVFFHPRASQSEFVIQLSKYIKAVFHTRISVGMRFRMLFETEESSVRRYMGTITGISDLDSVRWPNSHWRSVKVGWDESTAGERQPRVSLWEIEPLTTFPMYPSLFPLRLKRPWHAGTSSLPDGRGDLGSGLTWLRGGGGEQQGLLPLNYPSVGLFPWMQQRLDLSQMGTDNNQQYQAMLAAGLQNIGGGDPLRQQFVQLQEPHHQYLQQSASHNSDLMLQQQQQQQASRHLMHAQTQIMSENLPQQNMRQEVSNQPAGQQQQLQQPDQNAYLNAFKMQNGHLQQWQQQSEMPSPSFMKSDFTDSSNKFATTASPASGDGNLLNFSITGQSVLPEQLTTEGWSPKASNTFSEPLSLPQAYPGKSLALEPGNPQNPSLFGVDPDSGLFLPSTVPRFASSSGDAEASPMSLTDSGFQNSLYSCMQDTTHELLHGAGQINSSNQTKNFVKVYKSGSVGRSLDISRFSSYHELREELGKMFAIEGLLEDPLRSGWQLVFVDKENDILLLGDDPWESFVNNVWYIKILSPEDVHQMGDHGEGSGGLFPQNPTHL
Protein: PDZ and LIM domain protein 3 (Actinin-associated LIM protein) (Alpha-actinin-2-associated LIM protein) (SK-2) (Q66HS7)
Organism: Rattus norvegicus (Rat)
Function: May play a role in the organization of actin filament arrays within muscle cells.
Subcellular location: Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:9334352}. Note=Localizes to myofiber Z-lines.
Interaction partners:
- F-actin cross-linking protein
Sequence:
MPQNVVLPGPAPWGFRLSGGIDFNQPLVITRITPGSKAEAANLCPGDVILAIDGFGTESMTHADAQDRIKAASYQLCLKIDRAETRLCPAVSEDGKAHPFKINLEAEPQDVNYFEHKHNIRPKPFIIPGRTSGCSTPSGIDCGSGRSTPSSVSTVSTICPGDLKVAAKMAPNIPLEMELPGVKIVHAQFNTPMQLYSDDNIMETLQGQVSTALGETPSMSEPTASVPPQSDVYRMLHDNRDEPAAPRQSGSFRVLQELVNDGSDDRPAGTRSVRPVTKVHGGAGGAQRMPLCDKCGSGIVGAVVKARDKYRHPECFVCADCNLNLKQKGYFFVEGELYCEMHARARTRPPEGYDTVTLYPKA
Protein: 4-hydroxy-2-oxovalerate aldolase (HOA) (EC 4.1.3.39) (4-hydroxy-2-keto-pentanoic acid aldolase) (4-hydroxy-2-oxopentanoate aldolase) (P51016)
Organism: Pseudomonas sp. (strain CF600)
Function: Catalyzes the retro-aldol cleavage of 4-hydroxy-2-oxopentanoate to pyruvate and acetaldehyde. Is involved in the meta-cleavage pathway for the degradation of aromatic compounds such as phenols, cresols and catechols.
Interaction partners:
Sequence:
MTFNPSKKLYISDVTLRDGSHAIRHQYTLDDVRAIARALDKAKVDSIEVAHGDGLQGSSFNYGFGRHTDLEYIEAVAGEISHAQIATLLLPGIGSVHDLKNAYQAGARVVRVATHCTEADVSKQHIEYARNLGMDTVGFLMMSHMIPAEKLAEQGKLMESYGATCIYMADSGGAMSMNDIRDRMRAFKAVLKPETQVGMHAHHNLSLGVANSIVAVEEGCDRVDASLAGMGAGAGNAPLEVFIAVAERLGWNHGTDLYTLMDAADDIVRPLQDRPVRVDRETLGLGYAGVYSSFLRHAEIAAAKYNLKTLDILVELGHRRMVGGQEDMIVDVALDLLAAHKENRA