wanglab/gogpt-training-data huggingface dataset:
Protein: Trafficking kinesin-binding protein 1 (Protein Milton) (Q6PD31)
Organism: Mus musculus (Mouse)
Function: Involved in the regulation of endosome-to-lysosome trafficking, including endocytic trafficking of EGF-EGFR complexes and GABA-A receptors (By similarity). Involved in mitochondrial motility. When O-glycosylated, abolishes mitochondrial motility. Crucial for recruiting OGT to the mitochondrial surface of neuronal processes (By similarity). TRAK1 and RHOT form an essential protein complex that links KIF5 to mitochondria for light chain-independent, anterograde transport of mitochondria (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:24995978}. Nucleus {ECO:0000250|UniProtKB:Q9UPV9}. Mitochondrion {ECO:0000250|UniProtKB:Q9UPV9}. Early endosome {ECO:0000250|UniProtKB:Q9UPV9}. Endosome {ECO:0000250|UniProtKB:Q9UPV9}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q9UPV9}. Cytoplasm, cell cortex {ECO:0000269|PubMed:24995978}. Note=Predominantly associated with early endosome. The localization to early endosomes depends on its interaction with HGS/HRS. Colocalizes with MGARP at the mitochondria. {ECO:0000250|UniProtKB:Q9UPV9}.
Interaction partners:
- Mitochondrial Rho GTPase 1
- Mitochondrial Rho GTPase 2
- Kinesin heavy chain isoform 5A
- Kinesin-1 heavy chain
- Mitofusin-2
- Nuclear distribution protein nudE homolog 1
- Trafficking protein, kinesin binding 2
- Kinesin heavy chain isoform 5C
- Unconventional myosin-XIX
- Disrupted in schizophrenia 1 homolog
Sequence:
MALAIQLRQPSRAQPLPGLSHTLAGTDSCDVCNSTNLPEVEIISLLEEQLPHYKLRADTIYGYDHDDWLHTPLISPDANIDLTTEQIEETLKYFLLCAERVGQMTKTYNDIDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPESVCSTPLKRNESSSSVQNYFHLDSLQKKLKDLEEENVVLRSEACQLKTETITYEEKEQQLVNDCVKELRDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKSCAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNLRNKTMPTSRRYHSLGLFPMDSLAAEIEGTMRKELQLEELESPDITHQKRVFETVRNVNQVVKQRSLTPSPMNIPGSNQSSAMNSLLSSCVSTPRSSFYGSDVSNVVLDNKTNSILLETEAADLGNEDHNKKPGTPGTPGSHDLETALRRLSLRRENYLSERRFFEEEQERKLRELAEKGELHSGSLTPTESIMSLGTHSRFSEFTGFSGMSFSSRSYLPEKLQIVKPLEGSATLHHWQQLAQPHLGGILDPRPGVVTKGFRTLDVDLDEVYCLNDFEEDDTGDHISLAGLATSTPIQHPETSAHHPGKCMSQTNSTFTFTTCRILHPSDELTRVTPSLNSAPAPACSSTSHLKSTPVATPCTPRRLSLAESFTNVRESTTTMSTSLGLVWLLKERGISAAVYDPQSWDRAGRGSLLHSYTPRMAVIPSTPPNSPMQTPSASPPSFEFKCTSPPYNNFLASKPASSILREVREKRPVRSSESQTDVSVSNLNLVDKVRRFGVARVVNSGRARIPTLTEEQGPLLCGPTGPAQALVPGGLVPEGLPLGCPSGIRRNRSFPTMVGSSVQMRAPVILTSGILMGAKLPKQTSLR
Protein: Late secretory pathway protein AVL9 homolog (Q8NBF6)
Organism: Homo sapiens (Human)
Function: Functions in cell migration.
Subcellular location: Recycling endosome {ECO:0000269|PubMed:22595670}. Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- DENN domain-containing protein 10
- DENN domain-containing protein 11
- Protein DENND6A
- Dynamin-1-like protein
Sequence:
MEKARRGGDGVPRGPVLHIVVVGFHHKKGCQVEFSYPPLIPGDGHDSHTLPEEWKYLPFLALPDGAHNYQEDTVFFHLPPRNGNGATVFGISCYRQIEAKALKVRQADITRETVQKSVCVLSKLPLYGLLQAKLQLITHAYFEEKDFSQISILKELYEHMNSSLGGASLEGSQVYLGLSPRDLVLHFRHKVLILFKLILLEKKVLFYISPVNKLVGALMTVLSLFPGMIEHGLSDCSQYRPRKSMSEDGGLQESNPCADDFVSASTADVSHTNLGTIRKVMAGNHGEDAAMKTEEPLFQVEDSSKGQEPNDTNQYLKPPSRPSPDSSESDWETLDPSVLEDPNLKEREQLGSDQTNLFPKDSVPSESLPITVQPQANTGQVVLIPGLISGLEEDQYGMPLAIFTKGYLCLPYMALQQHHLLSDVTVRGFVAGATNILFRQQKHLSDAIVEVEEALIQIHDPELRKLLNPTTADLRFADYLVRHVTENRDDVFLDGTGWEGGDEWIRAQFAVYIHALLAATLQLDNEKILSDYGTTFVTAWKNTHNYRVWNSNKHPALAEINPNHPFQGQYSVSDMKLRFSHSVQNSERGKKIGNVMVTTSRNVVQTGKAVGQSVGGAFSSAKTAMSSWLSTFTTSTSQSLTEPPDEKP
Protein: Zinc fingers and homeoboxes protein 3 (Triple homeobox protein 1) (Zinc finger and homeodomain protein 3) (Q9H4I2)
Organism: Homo sapiens (Human)
Function: Acts as a transcriptional repressor. Involved in the early stages of mesenchymal stem cell (MSC) osteogenic differentiation. Is a regulator of podocyte gene expression during primary glomerula disease. Binds to promoter DNA.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000269|PubMed:12659632}.
Interaction partners:
- Nuclear transcription factor Y subunit alpha
Sequence:
MASKRKSTTPCMIPVKTVVLQDASMEAQPAETLPEGPQQDLPPEASAASSEAAQNPSSTDGSTLANGHRSTLDGYLYSCKYCDFRSHDMTQFVGHMNSEHTDFNKDPTFVCSGCSFLAKTPEGLSLHNATCHSGEASFVWNVAKPDNHVVVEQSIPESTSTPDLAGEPSAEGADGQAEIIITKTPIMKIMKGKAEAKKIHTLKENVPSQPVGEALPKLSTGEMEVREGDHSFINGAVPVSQASASSAKNPHAANGPLIGTVPVLPAGIAQFLSLQQQPPVHAQHHVHQPLPTAKALPKVMIPLSSIPTYNAAMDSNSFLKNSFHKFPYPTKAELCYLTVVTKYPEEQLKIWFTAQRLKQGISWSPEEIEDARKKMFNTVIQSVPQPTITVLNTPLVASAGNVQHLIQAALPGHVVGQPEGTGGGLLVTQPLMANGLQATSSPLPLTVTSVPKQPGVAPINTVCSNTTSAVKVVNAAQSLLTACPSITSQAFLDASIYKNKKSHEQLSALKGSFCRNQFPGQSEVEHLTKVTGLSTREVRKWFSDRRYHCRNLKGSRAMIPGDHSSIIIDSVPEVSFSPSSKVPEVTCIPTTATLATHPSAKRQSWHQTPDFTPTKYKERAPEQLRALESSFAQNPLPLDEELDRLRSETKMTRREIDSWFSERRKKVNAEETKKAEENASQEEEEAAEDEGGEEDLASELRVSGENGSLEMPSSHILAERKVSPIKINLKNLRVTEANGRNEIPGLGACDPEDDESNKLAEQLPGKVSCKKTAQQRHLLRQLFVQTQWPSNQDYDSIMAQTGLPRPEVVRWFGDSRYALKNGQLKWYEDYKRGNFPPGLLVIAPGNRELLQDYYMTHKMLYEEDLQNLCDKTQMSSQQVKQWFAEKMGEETRAVADTGSEDQGPGTGELTAVHKGMGDTYSEVSENSESWEPRVPEASSEPFDTSSPQAGRQLETD
Protein: Alanine--tRNA ligase, mitochondrial (EC 6.1.1.7) (Alanyl-tRNA synthetase) (AlaRS) (Protein lactyltransferase AARS2) (EC 6.-.-.-) (Q5JTZ9)
Organism: Homo sapiens (Human)
Function: Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain.
Subcellular location: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03133, ECO:0000269|PubMed:21549344}.
Interaction partners:
- Aspartate--tRNA ligase, mitochondrial
- Valine--tRNA ligase, mitochondrial
- Tyrosine--tRNA ligase, cytoplasmic
- Nondiscriminating glutamyl-tRNA synthetase EARS2, mitochondrial
- Leucine--tRNA ligase, mitochondrial
- Isoleucine--tRNA ligase, mitochondrial
- Valine--tRNA ligase
- Threonine--tRNA ligase, mitochondrial
- Alanine--tRNA ligase, cytoplasmic
- Probable arginine--tRNA ligase, mitochondrial
Sequence:
MAASVAAAARRLRRAIRRSPAWRGLSHRPLSSEPPAAKASAVRAAFLNFFRDRHGHRLVPSASVRPRGDPSLLFVNAGMNQFKPIFLGTVDPRSEMAGFRRVANSQKCVRAGGHHNDLEDVGRDLSHHTFFEMLGNWAFGGEYFKEEACNMAWELLTQVYGIPEERLWISYFDGDPKAGLDPDLETRDIWLSLGVPASRVLSFGPQENFWEMGDTGPCGPCTEIHYDLAGGVGAPQLVELWNLVFMQHNREADGSLQPLPQRHVDTGMGLERLVAVLQGKHSTYDTDLFSPLLNAIQQGCRAPPYLGRVGVADEGRTDTAYRVVADHIRTLSVCISDGIFPGMSGPPLVLRRILRRAVRFSMEILKAPPGFLGSLVPVVVETLGDAYPELQRNSAQIANLVSEDEAAFLASLERGRRIIDRTLRTLGPSDMFPAEVAWSLSLCGDLGLPLDMVELMLEEKGVQLDSAGLERLAQEEAQHRARQAEPVQKQGLWLDVHALGELQRQGVPPTDDSPKYNYSLRPSGSYEFGTCEAQVLQLYTEDGTAVASVGKGQRCGLLLDRTNFYAEQGGQASDRGYLVRAGQEDVLFPVARAQVCGGFILHEAVAPECLRLGDQVQLHVDEAWRLGCMAKHTATHLLNWALRQTLGPGTEQQGSHLNPEQLRLDVTTQTPLTPEQLRAVENTVQEAVGQDEAVYMEEVPLALTAQVPGLRSLDEVYPDPVRVVSVGVPVAHALDPASQAALQTSVELCCGTHLLRTGAVGDLVIIGDRQLSKGTTRLLAVTGEQAQQARELGQSLAQEVKAATERLSLGSRDVAEALRLSKDIGRLIEAVETAVMPQWQRRELLATVKMLQRRANTAIRKLQMGQAAKKTQELLERHSKGPLIVDTVSAESLSVLVKVVRQLCEQAPSTSVLLLSPQPMGKVLCACQVAQGAMPTFTAEAWALAVCSHMGGKAWGSRVVAQGTGSTTDLEAALSIAQTYALSQL
Protein: Uncharacterized protein (Q586U2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MQRDADRMKRKKEEHRDEEEFGAFRFADGSMYEGKFCRRESNADGTAKSQFPSAHPPTTRNAQQQELPPPIPFHHGKGVFKDAGGLVYDGCWVEGDMTGEGLLRFPSGATYEGSMYANSFWGTGTYTWPDGSRYEGQWENNKMHGKGTYIDAKGKRWAGKFHHGQGVGLLAEVSL
Protein: Low-density lipoprotein receptor-related protein-2 (G0W2S9)
Organism: Gallus gallus (Chicken)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MGTRQQTGGKAATACGVLLLLAACILRGSCQGCGGGQFRCGNGRCIPADWRCDGARDCSDDTDEAGCPRPTCEGNQFQCQTDGECIPHSWVCDDEEDCEDGSDEHQQCPGRTCSSQQFTCSNGQCIPSAYRCDRVKDCTDGTDERDCRYPRCEQLSCANGACFNASQRCDGKVDCRDTSDEANCTRGCASTQFQCANGECIPQAFMCDHDDDCGDRSDENSCTYATCRGNFFTCPSGRCIHQSWICDGDDDCEDNEDERGCESSYHECYPGEWACPESGHCIPIGKVCDGAADCPAGEDETNITAGRHCNISHCAALSCQYRC
Protein: ABC multidrug transporter A-2 (Q4X006)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Pleiotropic ABC efflux transporter that confers resistance to structurally and functionally unrelated compounds including azoles such as itraconazole, posaconazole, and voriconazole.
Subcellular location: Cell membrane {ECO:0000269|PubMed:24123268}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- ABC multidrug transporter A-1
Sequence:
MAMQPSYPAPFGAAAISSSAGQEVASTIRRQFTDADADRIVETPLGEKADSSDTAGPDSEDGIDQEGHDKITALARSLSQISQKSAGPTNTFLDPSSDPELDPNSDKFSSRKWMKNLLHIKTRDPDRYPRRTAGVSFRNLNAYGYGTAADYQADVANMWLKGFGWLRSILGCRNRVQIDILRNFEGFVRSGEMLVVLGRPGSGCSTFLKTIAGETHGLWLDEGTHIQYEGISWDEMHSRFRGEVIYQAETEIHFPQLTAGETLLFAAQARTPANRFPGVSREQYATHMRDVVMTMLGLSHTVNTRIGNEYIRGVSGGERKRVSIAETILCGCPLQCWDNSTRGLDSSTALEFVKNLRLSTDYTGSTAIVAIYQASQAIYDIFDKVIVLYEGRQIYFGKASDAKRFFIDMGFDCPDRQTTGDFLTSLTSPSERLVRKGYEALVPRTPDEFAARWRESAERQRLLADIEAFENESPLGGSKYKEFTVSRAAEKAKGTRAPSPYTLSYPMQIRLCLRRGFLRLKGDMSMTLATVIGNSIMAFIVSSVFYNLDQTTNSFFSRGALLFFAILLNAFASSLEILTLWQQRPIVEKHDKYALYHPSAEAISSMIVDLPSKFLVSVVFNLILYFMTNLRRTPGHFFVFYLFSVTITLTMSNIFRWIGAISRSMAQAMVPSSIFMMILVIYTGFTIPVRDMHPWFKWLNYLNPIGYAFESLMINEFSDRRFPCAQYVPAGPGYEDVPLSSKICSQKGAVAGQDYVDGDAFINTSYRYFSSHLWRNYGIILGFFFFFLAAYIICSELVRAKPSKGEILVFPRGKIPAFVKKSRRDGDLEGAPTFEKQQLDNAGHDSTAAIVKQTSIFHWQDVCYDIKVKGETRRILDHIDGWVKPGTLTALMGVTGAGKTSLLDVLANRVTMGVITGEMLVDGRMRDDSFQRKTGYVQQQDLHLETSTVREALIFSATLRQPASTPHKEKLAYVEEVIKMLNMEEYAEAVVGVLGEGLNVEQRKRLTIGVELAAKPALLCFFDEPTSGLDSQTAWSICTLMRKLADHGQAILCTIHQPSAILMQQFDRLLFLAKGGKTVYFGELGPNMETLIKYFENKGSSKCPKNANPAEWMLEVIGAAPGSHADQDWPEVWNNSPERAQVRAELARMKEELLQRPPPPRTKEYGEFAMPLWAQFLVCLQRMFQQYWRSPSYIYSKAATSIIPPLFIGFTFWREPTSLQGLQNQMFAIFMLLVIFPNLVQQMMPYFVTQRALYEVRERPSKAYSWKAFMLASILVELPWNILMAVPAYFCWYYPIGLYRNAYPTDSVTERGGTMFLLILIFMMFTSTFSSMIIAGIEQPETGGNIAQLLFSLCLIFNGVLASPSALPGFWIFMYRVSPFTYLVSAVLSVGLAGTSVKCSDIEILHVPPPQGQNCSSFLDAYVQMSHGRLLNPEATSDCQVCPVADTDTFLAQVSISYSDRWRNVGLLFVYIVFNIFAAIFLYWLIRVPKKRSRKIKEE
Protein: Chitinase 2 (EC 3.2.1.14) (P40953)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Chitinase involved in the remodeling of chitin in the fungal cell wall. Plays a role in cell separation.
Subcellular location: Secreted, cell wall. Membrane; Lipid-anchor, GPI-anchor.
Interaction partners:
- Chitinase 4
- Chitinase 3
- chitin deacetylase
- Ngs1p
- Beta-hexosaminidase
- Chitinase 1
- Cell wall protein RHD3
Sequence:
MLSFKSLLAAAVVASSALASASNQVALYWGQNGAGGQERLAQYCQEADVDIILLSFLNLFPDPLNVNFANQCGNTFESGLLHCSQIGADIKTCQSLGKTVLLSLGGGVGDYGFSDVASATKFADTLWNKFGAGEDPERPFDDAVVDGFDFDIEHGGATGYPELATALRGKFAKDTSKNYFLSAAPQCPYPDASLGDLLSKVPLDFAFIQFYNNYCSINGQFNYDTWSKFADSAPNKNIKLFVGVPATSNIAGYVDTSKLSSAIEEIKCDSHFAGVSLWDASGAWLNTDEKGENFVVQVKNVLNQNACVAPSSSATTQSTTTTSSAVTQSTTTTSAAITQSATTTSAAVATKSNQIVTSSSSSSSSIFYGNSTTESSTGIATGTVLPTGSNENAATTGSGSNTKLAISTVTDVQKTVITITSCSEHKCVATPVTTGVVVVTDIDTVYTTYCPLTNSQVYVSVKTVVCTEETCVPSPTSTSQKPKASTTIKGVEKGQTTSYPVVGTTEGVKKIVTTSAQTVGSSTKYVTIELTSTITPVTYPTSVASNGTNTTVPVFTFEGGAAVANSLNSVWFTVPFLLAAFAF
Protein: Arginase (EC 3.5.3.1) (A0A509AF89)
Organism: Plasmodium berghei (strain Anka)
Function: Catalyzes the hydrolysis of L-arginine into urea and L-ornithine, which is a precursor for polyamine biosynthesis. May play a role in parasite intra-hepatic development during the host liver stage.
Interaction partners:
- Ornithine aminotransferase
- Spermidine synthase, putative
- Eukaryotic translation initiation factor 5A
- S-adenosylmethionine decarboxylase/ornithine decarboxylase, putative
- S-adenosylmethionine synthase
- Pyrroline-5-carboxylate reductase
- proton-translocating NAD
Sequence:
MYECIQDYLTNHKDEKNIYVNKCISIVGSPLSAGQSLSGVNKACDNLRKFGLHDVIKAVGWGYEDIGNIGEKIPINGFLKQENIEKENDQINNNNPSYYNNIKNAEVIGKFSEKLFQTMSSELKKKNFILNIGGDHGVAFSSILSMLQTYNNLKVIWIDAHGDINIPETSPSGNYHGMSLAHALGLFKKKVPYFEWSEKLLHLKPENVAIIGIRDIDKYEKIILKKCNINYYTMFDIDKKGIYNIICEALNKIDPNKNSPIHISLDIDSVDSIYAPGTGTIAKGGLNYREIHLLIKSISDTKRVVSMDIVEYNPLLDESDKAVHGDSLPIDPNATKTGKLCLELIARVLGNDIV
Protein: Uncharacterized protein C3H7.13 (O74388)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Nucleus.
Interaction partners:
- Factor arrest protein 11
- Uncharacterized WD repeat-containing protein C1773.01
- Uncharacterized protein C2C4.10c
- Putative serine/threonine-protein phosphatase C22H10.04
- Protein phosphatase PP2A regulatory subunit A
- 2-oxoglutarate dehydrogenase, mitochondrial
Sequence:
MSAVITLTPLNESFQTKKLVISPSTIYKIGRHTNKSTSPSPSNLFFNSKVLSRQHAELWLDKDTLSVYIRDVKSSNGTFVNETRLSPENKPSAPCKLNSGDIVDFGVDIYNEDEIVHQKVSAQVRIVVRGATFATTPARSLDSEVMLDSIMRQMVFQYQRCVELNENLESLENGVEEVSKSLSWLETGKTRDNRNNHHYSRKSSPHISSLAVPSTKHLDGERDRNLKRSTSPLSSSPFVTEAALNEAELAKTNLEAWKARAFTAEARLSSKNKSWQEKKYLVLSPFFIAVAGIIVYMGYWR
Protein: Uncharacterized protein (Q3UM69)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
EAPAAPDHPCAARVRGAGPARAGVPGEVRGAAIPGGPGPRRSYLCLEDQLSPRPLPFPPLWPHSTPPTSPSFPPHRSLPPSHPPTHRLPQAPPPPLSQAQALNSLSMVLPPRKREKGPGPELHSGCLDGLRSLFEGPPCPYPGAVIPFQAPGPSHPSPTTPSGDESMEEHLAVMHERLRQELPTLFLRSHDYTIYSMDVEFINEILNIRTKGRTFYVMSLTLCRFLVWNYFAQFRLEILQLTRHPENWTLQARWRLIGLPIHMLFLRFYRRDKEDLYRTFDAFSTFYLNSSGLICRHHLDKLMPSHSPSTPVKKLLVGALVALGLSEPEPSLHLCSKA
Protein: Mediator of RNA polymerase II transcription subunit 10 (Mediator complex subunit 10) (P87310)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}. Nucleus envelope {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 6
- Mediator of RNA polymerase II transcription subunit 4
- Mediator of RNA polymerase II transcription subunit 22
- Mediator of RNA polymerase II transcription subunit 18
- Mediator of RNA polymerase II transcription subunit 31
- Mediator of RNA polymerase II transcription subunit 7
- Mediator of RNA polymerase II transcription subunit 19
- Mediator of RNA polymerase II transcription subunit 17
- Mediator of RNA polymerase II transcription subunit 14
- Mediator of RNA polymerase II transcription subunit 21
Sequence:
MLPQDDMTDEMKSLASRLEDTTQAFYDLALIVYNLEDTTPSDAIPESLDTLIRDLKSLPDISRKVNNLIPQDVLEYIEQGRNPDVYARQFSELVQKDNQYVNGKLYAIEGFQKAFAEEIKQAYPEVSSVVDKILNEGKVESTVS
Protein: ATPase involved in DNA repair (Q8NR86)
Organism: Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534)
Interaction partners:
- DNA repair exonuclease
- Hypothetical membrane protein
- DNA polymerase I
- ATP-dependent DNA helicase RecQ
- Superfamily II DNA/RNA helicases, SNF2 family
- SWIM-type domain-containing protein
Sequence:
MRIHEIIIDNFRAIEHLELRDIPDQGVIVIHGDNEQGKSSILEAIKTVLNSKHRTTSKTIKAIQPVDRDVPISITLEATVGTVRFRIHKRFLKSTAAELQVIEPRPSNHRGLEAEAALAEILESHLDTSLLDALFMKQGEVEAGISAVGIPTLTSALNAQNGNTEDATEDTALMEAVEKEYLKFYTNSGKANTRFLQFSKQVETLRTDLDEANAEVAKLSSHVDRVKRLEIDRDQATAQLPKAEEELAGRKAELEEAQKVKAQATEILAQFSRAEEQLEQATGAQKRRKELRNKLELAQTEVEKAEAGQENLAQEASREAEEFLALSEKFEAARAAETLAVEKVKAARQSVAGIKNRDRKEHLTVMLGELDRIGQRLYELRSVQHSSVRVSQRDIDALQKAITEVDIQRTLVEAQQGSITLSASTPTDIQLGDDTVSATDAGTTVALDRELTVVVGDVTLVINPGKTAAESRTDFESAEAALAELLDQLDVSDLDQLRERFTAQEQRDADIAELVREQQRMSGGTETTVLRAELEGLHVPEDLDPSISVDDAQTQLNEAEESRELAAEAHKHANAALDGLRSRPVDKALTVFNAQLAALQRNLSSAQVELDRAVAETSDDEVDAAVQRCAEALAGVRVQKQEIEQVLAKTNPDMAQRLCDAAEANVRSYKTAVSDATTELVRLEGLIGVAAGAKERLDKVKSALTAAENRFESEQRRAHAARRLYALMVFYRDESRKRYAAPFADKLSRLAASVFGESADFDLDDELKISSRSIGPRTVDLANLSGGAKEQLAILTRFAIAELVAESSAQGAVPVFIDDALGSTDPERLTRISTLFSDAGKDSQVFVLTCVPDRYNYVEVTQKHSIESLKTANALL
Protein: Dihydrolipoyl dehydrogenase 1, chloroplastic (ptLPD1) (EC 1.8.1.4) (Dihydrolipoamide dehydrogenase 1) (Protein LIPOAMIDE DEHYDROGENASE 1) (Pyruvate dehydrogenase complex E3 subunit 1) (E3-1) (PDC-E3 1) (A8MS68)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Lipoamide dehydrogenase is a component of the plastidial pyruvate dehydrogenase complex (PDC).
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:11056213}.
Interaction partners:
- Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex 1, mitochondrial
- Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial
- 2-oxoglutarate dehydrogenase, mitochondrial
- 2-oxoglutarate dehydrogenase, mitochondrial
- Pyruvate dehydrogenase E1 component subunit alpha-1, mitochondrial
- Dihydrolipoyllysine-residue acetyltransferase component 4 of pyruvate dehydrogenase complex, chloroplastic
- Dihydrolipoyllysine-residue acetyltransferase component 5 of pyruvate dehydrogenase complex, chloroplastic
- Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex 2, mitochondrial
- Pyruvate dehydrogenase E1 component subunit alpha-3, chloroplastic
- Pyruvate dehydrogenase E1 component subunit beta-2, chloroplastic
Sequence:
MQSAMALSFSQTSFTRPNHVLGSSGSVFSTPRSLRFCGLRREAFGFSTSNQLAIRSNRIQFLSRKSFQVSASASSNGNGAPPKSFDYDLIIIGAGVGGHGAALHAVEKGLKTAIIEGDVVGGTCVNRGCVPSKALLAVSGRMRELQNEHHMKSFGLQVSAAGYDRQGVADHANNLATKIRNNLTNSMKAIGVDILTGFGSVLGPQKVKYGKDNIITAKDIIIATGSVPFVPKGIEVDGKTVITSDHALKLESVPEWIAIVGSGYIGLEFSDVYTALGSEVTFIEALDQLMPGFDPEISKLAQRVLINPRKIDYHTGVFASKITPARDGKPVLIELIDAKTKEPKDTLEVDAALIATGRAPFTNGLGLENVNVVTQRGFIPVDERMRVIDGKGTLVPNLYCIGDANGKLMLAHAASAQGISVVEQVSGRDHVLNHLSIPAACFTHPEISMVGLTEPQAKEKGEKEGFKVSVVKTSFKANTKALAENEGEGIAKMIYRPDNGEILGVHIFGLHAADLIHEASNAIALGTRIQDIKLAVHAHPTLSEVLDELFKAAKVESHATTRTGDAKIKLNTNQEDRKGRRRGGDDEKQPSVSKDLKDISTRPSSFFENISVGVLSLLSLIFV
Protein: GTP-binding protein Rit2 (EC 3.6.5.2) (Q5BJQ5)
Organism: Rattus norvegicus (Rat)
Function: Binds and exchanges GTP and GDP.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P70425}. Cell membrane {ECO:0000250|UniProtKB:P70425}. Note=Colocalizes with PLXNB3 at the plasma membrane. {ECO:0000250|UniProtKB:Q99578}.
Interaction partners:
- RAF proto-oncogene serine/threonine-protein kinase
- Serine/threonine-protein kinase A-Raf
Sequence:
MEAENEAHCCPGSSSGGSREYKVVMLGAGGVGKSAVTMQFISHQFPDYHDPTIEDAYKTQVRIDNEPAYLDILDTAGQAEFTAMREQYMRGGEGFIICYSVTDRQSFQEAAKFKELIFQVRHTYEIPLVLVGNKIDLEQFRQVSTEEGMTLARDYNCAFFETSAALRFGIDDAFQGLVREIRRKESMLSLVERKLKRKDSLWKKIKASLKKKRENMI
Protein: EG:67A9.1 protein (Q9TVM9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAELKFEAPLAKFEETDEWGGCDFISSQNAINDTLNLNLKDSSAGGKPDATKLRLLEDAVRDAHVSKNGGGVVGGGAGSISPNCNTLQGGSLIEIGLSDVGLVPGEGAGVGLDGLEKRSLAVGDHVDNFTETFGGSLEDLVNTFDEKITKCFGNYEENVEELAPVQVRSQEEIMNECQMWWTITGNFGNILPIDWSKSYTRQMHMPTLNLGQNHTKQQQQNRNQQQQLHNQSHQAYPHTNGLGSGSGSGLDAQTPGDEFNDLTSEDEAVANDLDMHALILNGLNGDMDDQPIKTVEEVIKEIDDIMDEAESPLDEPETCDSEVIEKAREVLGAPLYAEELQYLTTTQLNELYMEMEVLIQELSETLINELALRDELEFEKELKNSFISLLLAVQNKRRQYHVEKKRGKFQGPEPKYLTTVIPYHLENGTPNNQSLQVLIKVLKAINEDSPTVPALLTDYILKVLCPT
Protein: Phosphatidylinositol-glycan-specific phospholipase D (PI-G PLD) (EC 3.1.4.50) (Glycoprotein phospholipase D) (Glycosyl-phosphatidylinositol-specific phospholipase D) (GPI-PLD) (GPI-specific phospholipase D) (O70362)
Organism: Mus musculus (Mouse)
Function: This protein hydrolyzes the inositol phosphate linkage in proteins anchored by phosphatidylinositol glycans (GPI-anchor) thus releasing these proteins from the membrane.
Subcellular location: Secreted. Note=Associated with the High-Density Lipoproteins (HDL). {ECO:0000250}.
Interaction partners:
- Glucosaminyl-phosphatidylinositol-acyltransferase PIGW
- N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase
- Apolipoprotein A-II
- Apolipoprotein A-IV
- Apolipoprotein M
- Apolipoprotein C-III
- Serum paraoxonase/arylesterase 1
- Serum amyloid A-4 protein
Sequence:
MSAGRLWSSLLLLLPLFCSKSSSCGLSTHVEIGHRALEFLRLQDGRINYKELILEHQDAYQAGTVFPDAFYPSICKRGKYHDVSERTHWTPFLNASIHYIRENYPLPWEKDTEKLVAFLFGITSHMVADLSWHNLGFLRTMGAIDFYNSYSDAHSAGDFGGDVLSQFEFNFNYLSRRWYVPVRDLLRIYDNLYGRKVITKDVLVDCTYLQFLEMHGEMFAVSKLYSTYSTKSPFLVEQFQDYFLGGLDDMAFWSTNIYRLTSFMLENGTSDCNLPENPLFISCDGRNHTLSGSKVQKNDFHRNLTMFISRDIRKNLNYTERGVFYSTGSWARPESVTFMYQTLERNLRLMLAGSSQKNLNHVSSPSASYTLSVPYARLGWVMTSADLNQDGHGDLVVGAPGYSHPGRFQIGRVYIIYGNDLGLPPIDLDLNKEGILEGFQPSGRFGSALAVLDFNQDGLPDLAVGAPSVGSGQLTYNGSVYVYYGSQQGRLSSSPNVTISCKDTYCNLGWTLLATDADGDGRHDLVISSPFAPGGRKQKGIVATFYSHPRRNDKELLTLEEADWKVNGEEDFSWFGYSLHGVTVANRSLLLIGSPTWKNVSRMARSSHKKNQEEKSLGKVYGYFLPNRQSTITISGDKAMGKLGTSLSSGYVRVNGTLTQVLLVGAPTHDDVSKMAFLTMTLHQGGATRMYELAPEKTQPALLSTFSGDRRFSRFGSVLHLTDLDDDGLDEIIMAAPLRITDVTSGLLGGEDGRVYIYNGMYTTLGDMTGKCKSWMTPCPEEKAQYVLTSPEASSRFGSSLVSVRSKGRNQVVVAAGRSSWGARLSGALHVYSFSSD
Protein: Cytochrome b-c1 complex subunit Rieske, mitochondrial (EC 7.1.1.8) (Q9VQ29)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion inner membrane {ECO:0000255|RuleBase:RU004495}; Single-pass membrane protein {ECO:0000250|UniProtKB:P08067}.
Interaction partners:
- Cytochrome c1, heme protein, mitochondrial
- NADH dehydrogenase iron-sulfur protein 4
- Cytochrome b-c1 complex subunit 7
- AT02348p
- Cytochrome c oxidase subunit 7C, mitochondrial
- Cytochrome c1, heme protein, mitochondrial
- Cytochrome b-c1 complex subunit 6
- Cytochrome b-c1 complex subunit 8
- Cytochrome c oxidase subunit 2
- Cytochrome c oxidase subunit 5A, mitochondrial
Sequence:
MMNAVSRAYVRGGAQVLSTGLKASGVAVNSMANRQAHTDLQVPDFSAYRRESVKDSRRRNDTAEERKAFSYLMVGAGAVGGAYAAKGLVNTFIGSMSASAEVLAMAKIEIKLSDIPEGKSVTFKWRGKPLFIRHRTAAEIETERNVPTSTLRDPEADDQRVIKPEWLVVIGVCTHLGCVPIANAGDWGGYYCPCHGSHYDASGRIRKGPAPLNLEVPTHEFPNEGLLVVG
Protein: Ubiquitin/ISG15-conjugating enzyme E2 L6 (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme L6) (Retinoic acid-induced gene B protein) (RIG-B) (UbcH8) (Ubiquitin carrier protein L6) (Ubiquitin-protein ligase L6) (O14933)
Organism: Homo sapiens (Human)
Function: Catalyzes the covalent attachment of ubiquitin or ISG15 to other proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. Promotes ubiquitination and subsequent proteasomal degradation of FLT3.
Interaction partners:
- E3 ubiquitin-protein ligase parkin
- Ubiquitin-like modifier-activating enzyme 7
- Ubiquitin-ribosomal protein eS31 fusion protein
- Ubiquitin-ribosomal protein eL40 fusion protein
- Ubiquitin-like protein ISG15
- Polyubiquitin-C
- Polyubiquitin-B
- E3 ubiquitin/ISG15 ligase TRIM25
- E3 ISG15--protein ligase HERC5
- E3 ubiquitin-protein ligase SIAH1
Sequence:
MMASMRVVKELEDLQKKPPPYLRNLSSDDANVLVWHALLLPDQPPYHLKAFNLRISFPPEYPFKPPMIKFTTKIYHPNVDENGQICLPIISSENWKPCTKTCQVLEALNVLVNRPNIREPLRMDLADLLTQNPELFRKNAEEFTLRFGVDRPS
Protein: NK2 homeobox 2b (NK2 transcription factor related 2b) (Nkx2.2b protein) (Q5BJA8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
- NK2 transcription factor-related, locus 9
- Forkhead box A sequence
Sequence:
MSLKNSKSGFTVRDILDLPDTNDEGSVSEDTEDEQDEGLNANQKKQHDSSRDALWLGSSCGHKYPVPSASPEELNPELSADESVDRESSEDSGKKRKRRILFSKTQTFELERRFRQQRYLSAPEREHLAKLLHLTPTQVKIWFQNHRYKVKRARAEKGLDPYLLSPRRVSIPVLVRDGRPCHLLGPQDITASIPPATAPFTAFNMKPFPQIHHSHNNIVTHLTSSVNHLGHMQPWSW