wanglab/gogpt-training-data huggingface dataset:
Protein: CCN family member 1 (Cellular communication network factor 1) (Cysteine-rich angiogenic inducer 61) (Insulin-like growth factor-binding protein 10) (IBP-10) (IGF-binding protein 10) (IGFBP-10) (Protein CYR61) (Q9ES72)
Organism: Rattus norvegicus (Rat)
Function: Promotes cell proliferation, chemotaxis, angiogenesis and cell adhesion. Appears to play a role in wound healing by up-regulating, in skin fibroblasts, the expression of a number of genes involved in angiogenesis, inflammation and matrix remodeling including VEGA-A, VEGA-C, MMP1, MMP3, TIMP1, uPA, PAI-1 and integrins alpha-3 and alpha-5 (By similarity). CCN1-mediated gene regulation is dependent on heparin-binding (By similarity). Down-regulates the expression of alpha-1 and alpha-2 subunits of collagen type-1 (By similarity). Promotes cell adhesion and adhesive signaling through integrin alpha-6/beta-1, cell migration through integrin alpha-1/beta-5 and cell proliferation through integrin alpha-v/beta-3 (By similarity).
Subcellular location: Secreted.
Interaction partners:
- Ankyrin repeat domain-containing protein 1
- Integrin alpha-V
- Protein c-Fos
Sequence:
MSSSTIKTLAVAVTLLHLTRLALSTCPAACHCPLEAPKCAPGVGLVRDGCGCCKVCAKQLNEDCSKTQPCDHTKGLECNFGASSTALKGICRAQSEGRPCEYNSRIYQNGESFQPNCKHQCTCIDGAVGCIPLCPQELSLPNLGCPNPRLVKVSGQCCEEWVCDEDSIKDSLDDQDDLLGFDASEVELTRNNELIAIGKGSSLKRLPVFGTEPRVLYNPLHAHGQKCIVQTTSWSQCSKSCGTGISTRVTNDNSECRLVKETRICEVRPCGQPVYSSLKKGKKCSKTKKSPEPVRFTYAGCSSVKKYRPKYCGSCVDGRCCTPLQTRTVKMRFRCEDGEMFSKNVMMIQSCKCNYNCPHPNEASFRLYSLFNDIHKFRD
Protein: Ras GTPase activating protein (A0A1D8PFE8)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Ras-like protein 1
- Spindle assembly checkpoint component MAD2
- Protein kinase
- Anaphase promoting complex subunit 1
- Ras2p
- Anaphase-promoting complex subunit 4
- Anaphase promoting complex subunit
- Anaphase promoting complex subunit
- Anaphase-promoting complex subunit 2
- Ras-related protein RSR1
Sequence:
MSDSIMKDDHFIFIQALAKRIESLLPNHTGRSIEEVELDQQFSITRKLLLENNSKDPRTVTYILVTFASILKTINTEFTNNKLKYRDDKSRNSILLICKLLADVLKVSWDRESTIVDDKDFLSNYSKFYYYDTPNRIESSVVSDLVDTFVNMISSSVVRKVVSLVRNEQTLTTLIVAKEESEILREDQLMTKEEETELVIGKIDFYLDTIIRYIATANPEDYYDVLKAKIFRYSQRDATIPLPVLQTYLPLLKFIFFAKVNSVTIVDDTLKALPCIRSNTWKQVYLHFLASSIKAQSFSRTLDYNVLVDLNDTHQTQVARSLFDISFSLFSDESSTNSFNSPFVLIWFFVICLEDVIEVSSDKPLNKLKLTFNKRLKFIMSQLKESSNASSLGSFDSFIHLFHLGARLQAYNQLWHPIYKFSMKFLDEIHQNLIKFGEVRKDDLLVDDDLLFRYDLLTVNFYLAAILINSDKYIRIVINNYKQNQEDLRFNKIFVKIIKGLSEIQTAKKSFFATMKQVTPTLRLMVYGASKILYQYEIRRSINQISQGSINGSSDASTASYIDNEQNSDEVTAATQEAFSRIKTSLDHYTADLFDTDLKKLNSSKNFTTSSSSVLSTSTYRFRVVNGAEELLSDIFRIFAAAPEFYFNDEKLMSKKVYETKPLSESLPPIIRFCHDAIIPIRLAFKSKWIIQGDTRLLDSTKELSLKMVEPTTSLIDIRTDLSVFANFQICCCIIYVTCEACLSISLLNPKFKSCFLFLNSFLQKRTYFNKFVIENPILTNPDTRVYLGFCGDIIHSVEKVLLLSLCTHDISFYNYALQGIDWYLDEVETNKPFYPSEDVRDTLVDTFQKISEDKAVFTGFVSLHKRHRNILRNSKPTKSLYQTWVTIYHRWVRILDTKSSLGNDKTLILRHFTGFLVSTSGCFLSGSLVSEELAANTWPTAPISEFFDKCIELLTSPDMVIQMIIKEALASESQAEVYCLTARKLMETATHYFENNKSDEIAVFLDRAIIVMTSMINVKSEGALYLSTLLPEICQDFIKFINAIDDPCERFKLQLRFCKLGCALELDRTNAGLNGAYKLRNLYSRASLEWLEPAVFYDSALEENIKADDSSSVKTNKEVELSHLALDFAVECSILLRGQVENLLLEVPDGIKEDEINKYKDLSFSVYFSLFYKVIQKYTKATPTNREKHKHHIIIDNILQSITNILQYDSQIGMRFILPMGYHESKKIRSIFLNVFSKMLVHQSKISNREEYPDKLINELTDQFEIFGSIAECASSFEHNLLASAFFEVFSYTGKLNNLFNVLLNTEVALSSRSTDLFRRNSTLTKFLSFYAQTNGVDYLNEVLLPVIKELVDNDVQFEVEKQDNSDTADLFILYLSRIIDSIVNSTDKLPHAFKSVSKAIYDSVSNKFPEAALTAVSSFVFLRFLCPAIISPEQHFKLPINNPKVKRSLMQLVKVLQNMANGTLTSIKWPAIAGKTEELNFYNQKIDGFLKIISTDVTTENQSAELYKPEKPLTSLRYLHKFIYHYFAKIRYNFLFQHSWRCNYSLHDKAVKFKKFDYLVMQMGQPNPGVKLQMSSKLKLLDTNNLDEEEIKLNDFMTKMSIKFSDTPPDAIDVIHSSIFKDGTPAVVVNLKKLSGRPHDFEYLAYKLIETASQVWDNKFYLVYDFTEYYYYIETVTIEYANLIANSGTKLLFSNCQRVYYFNIPRIENPGIMEGVKLVRSKGEKYGTKVYIYSLADPDSIIKNLCLDSETLAINRENKVTFKDVLLYDATTEKFMPVQFKIGRRFVTLCFTNRVKFDYIASVTDGFNPVEVYRISEMNKCEVSNFTGNNDEFTIYLNRGVQLTFRSQDRLEILRYLYFTISRLPREPFSLNNELDYQNERHTMHWFGRLYNIVFQGLLSHDEELKSKAGVLFGSLSTYFEIDFGIRENHASNVPFPADATNFVVTVSAHLAKTFPQMTYRFFKAFFDNFDRIDRETRFTSILYLSPWIQNIYEYVFSNDENGADKTADLLRLFCRLTSIYKDRIPFINDYIWSKLFQEARLVSTLVEEVVAFAIDSKNDNPDWTFIIAVICPSIEVCGEVTSRLLQRINKVVTTDSSIALQSKLFEISVLIKICSSLFFNSYNLAKTYLAELIFFVTLFIDNPVLDVGEDLQKLLMTAIQSFLHKPNLTEAQRAEIDKAIAYFSTPRAKMIFGTSRDVTKRNDAAQAFNKITNIEQFADYLNVFIKAFALHGDRTNWRARWSSNTIDVAFNNYSVFQDRAFLMVGILSKEGISDSNACRTIKLVSNGELNSIDITICVAVAVARILDGLPDSSILPPILIWPQLCFTLLNHAVLYPSGLENVIASITKIMRLGPNYLDTIFEQQQYLEPDLSKFQERHGYIITKENFGVHIFFILGQGLRISQYRHLAIACIKRYFKQRYLMREGKTMDGKFITNNTYAYIFYLYLCCDAKEVEDYLKELEIDRSFISLDDNQKIPKLLIDLLFDNTEVSKILMIHVGFLFCDIQGVDISFKARFIQIYLYMLKNNRELALLVYHIIKPTLMHDLLNTVSVEVVKNISEIVEIVSQCTDYDPEYHKNVVDDILISKKITILKTLRHLKPLSETIDENQIFKPEFDSDIKPIQSMLYRAACSYISGSKLED
Protein: Ammonium transporter Rh type C (Rh glycoprotein kidney) (Rhesus blood group family type C glycoprotein) (Rh family type C glycoprotein) (Rh type C glycoprotein) (Tumor-related protein DRC2) (Q9UBD6)
Organism: Homo sapiens (Human)
Function: Functions as an electroneutral and bidirectional ammonium transporter. May regulate transepithelial ammonia secretion.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15929723}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000269|PubMed:10852913, ECO:0000269|PubMed:12204676}; Multi-pass membrane protein {ECO:0000255}. Note=Also detected at the basolateral membrane and in subapical vesicles. {ECO:0000250}.
Interaction partners:
- Leukocyte surface antigen CD47
- Band 3 anion transport protein
Sequence:
MAWNTNLRWRLPLTCLLLQVIMVILFGVFVRYDFEADAHWWSERTHKNLSDMENEFYYRYPSFQDVHVMVFVGFGFLMTFLQRYGFSAVGFNFLLAAFGIQWALLMQGWFHFLQDRYIVVGVENLINADFCVASVCVAFGAVLGKVSPIQLLIMTFFQVTLFAVNEFILLNLLKVKDAGGSMTIHTFGAYFGLTVTRILYRRNLEQSKERQNSVYQSDLFAMIGTLFLWMYWPSFNSAISYHGDSQHRAAINTYCSLAACVLTSVAISSALHKKGKLDMVHIQNATLAGGVAVGTAAEMMLMPYGALIIGFVCGIISTLGFVYLTPFLESRLHIQDTCGINNLHGIPGIIGGIVGAVTAASASLEVYGKEGLVHSFDFQGFNGDWTARTQGKFQIYGLLVTLAMALMGGIIVGLILRLPFWGQPSDENCFEDAVYWEMPEGNSTVYIPEDPTFKPSGPSVPSVPMVSPLPMASSVPLVP
Protein: Ran GTPase-activating protein 1 (Protein rna1) (P41391)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: GTPase activator for the nuclear Ras-related regulatory protein spi1 (Ran), converting it to the putatively inactive GDP-bound state.
Subcellular location: Cytoplasm. Cytoplasm, perinuclear region {ECO:0000305}. Note=Possibly enriched in the nuclear periphery.
Interaction partners:
- GTP-binding nuclear protein spi1
- Ran-specific GTPase-activating protein 1
- SUMO-conjugating enzyme ubc9
- Ubiquitin-like protein pmt3/smt3
- Exportin-1
- Protein pim1
- Uncharacterized protein C328.01c
- Ubiquitin-like-specific protease 1
- Brefeldin A resistance protein
- Exportin-T
Sequence:
MSRFSIEGKSLKLDAITTEDEKSVFAVLLEDDSVKEIVLSGNTIGTEAARWLSENIASKKDLEIAEFSDIFTGRVKDEIPEALRLLLQALLKCPKLHTVRLSDNAFGPTAQEPLIDFLSKHTPLEHLYLHNNGLGPQAGAKIARALQELAVNKKAKNAPPLRSIICGRNRLENGSMKEWAKTFQSHRLLHTVKMVQNGIRPEGIEHLLLEGLAYCQELKVLDLQDNTFTHLGSSALAIALKSWPNLRELGLNDCLLSARGAAAVVDAFSKLENIGLQTLRLQYNEIELDAVRTLKTVIDEKMPDLLFLELNGNRFSEEDDVVDEIREVFSTRGRGELDELDDMEELTDEEEEDEEEEAESQSPEPETSEEEKEDKELADELSKAHI
Protein: Cytosolic arginine sensor for mTORC1 subunit 2 (Cellular arginine sensor for mTORC1 protein 2) (GATS-like protein 2) (A6NHX0)
Organism: Homo sapiens (Human)
Function: Functions as a negative regulator of the TORC1 signaling pathway through the GATOR complex. As part of homodimers or heterodimers with CASTOR1, directly binds and inhibits the GATOR subcomplex GATOR2 and thereby mTORC1. Does not directly bind arginine, but binding of arginine to CASTOR1 disrupts the interaction of CASTOR2-containing heterodimers with GATOR2 which can in turn activate mTORC1 and the TORC1 signaling pathway.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:26972053}.
Interaction partners:
- Cytosolic arginine sensor for mTORC1 subunit 1
- GATOR2 complex protein WDR24
- GATOR2 complex protein MIOS
- GATOR2 complex protein WDR59
- Nucleoporin SEH1
- KICSTOR subunit 2
- KICSTOR complex protein ITFG2
- KICSTOR complex protein kaptin
Sequence:
MELHILEHRLQVASVAKESIPLFTYGLIKLAFLSSKTRCKFFSLTETPEDYTIIVDEEGFLELPSSEHLSVADATWLALNVVSGGGSFSSSQPIGVTKIAKSVIAPLADQNISVFMLSTYQTDFILVRERDLPFVTHTLSSEFTILRVVNGETVAAENLGITNGFVKPKLVQRPVIHPLSSPSNRFCVTSLDPDTLPAVATLLMDVMFYSNGVKDPMATGDDCGHIRFFSFSLIEGYISLVMDVQTQQRFPSNLLFTSASGELWKMVRIGGQPLGFDECGIVAQISEPLAAADIPAYYISTFKFDHALVPEENINGVISALKVSQAEKH
Protein: Disintegrin and metalloproteinase domain-containing protein 8 (ADAM 8) (EC 3.4.24.-) (Cell surface antigen MS2) (CD antigen CD156a) (P78325)
Organism: Homo sapiens (Human)
Function: Possible involvement in extravasation of leukocytes.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Large ribosomal subunit protein uL13m
- Ankyrin repeat and SOCS box protein 17
Sequence:
MRGLGLWLLGAMMLPAIAPSRPWALMEQYEVVLPWRLPGPRVRRALPSHLGLHPERVSYVLGATGHNFTLHLRKNRDLLGSGYTETYTAANGSEVTEQPRGQDHCFYQGHVEGYPDSAASLSTCAGLRGFFQVGSDLHLIEPLDEGGEGGRHAVYQAEHLLQTAGTCGVSDDSLGSLLGPRTAAVFRPRPGDSLPSRETRYVELYVVVDNAEFQMLGSEAAVRHRVLEVVNHVDKLYQKLNFRVVLVGLEIWNSQDRFHVSPDPSVTLENLLTWQARQRTRRHLHDNVQLITGVDFTGTTVGFARVSAMCSHSSGAVNQDHSKNPVGVACTMAHEMGHNLGMDHDENVQGCRCQERFEAGRCIMAGSIGSSFPRMFSDCSQAYLESFLERPQSVCLANAPDLSHLVGGPVCGNLFVERGEQCDCGPPEDCRNRCCNSTTCQLAEGAQCAHGTCCQECKVKPAGELCRPKKDMCDLEEFCDGRHPECPEDAFQENGTPCSGGYCYNGACPTLAQQCQAFWGPGGQAAEESCFSYDILPGCKASRYRADMCGVLQCKGGQQPLGRAICIVDVCHALTTEDGTAYEPVPEGTRCGPEKVCWKGRCQDLHVYRSSNCSAQCHNHGVCNHKQECHCHAGWAPPHCAKLLTEVHAASGSLPVFVVVVLVLLAVVLVTLAGIIVYRKARSRILSRNVAPKTTMGRSNPLFHQAASRVPAKGGAPAPSRGPQELVPTTHPGQPARHPASSVALKRPPPAPPVTVSSPPFPVPVYTRQAPKQVIKPTFAPPVPPVKPGAGAANPGPAEGAVGPKVALKPPIQRKQGAGAPTAP
Protein: Chlorophyll(ide) b reductase NOL, chloroplastic (EC 1.1.1.294) (Protein NON-YELLOW COLORING 1-LIKE) (OsNOL) (Protein NYC1-LIKE) (Short-chain dehydrogenase/reductase NOL) (Q84ST4)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Required for chlorophyll b degradation.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:18778405}; Peripheral membrane protein {ECO:0000269|PubMed:18778405}; Stromal side {ECO:0000269|PubMed:18778405}.
Interaction partners:
- 7-hydroxymethyl chlorophyll a reductase, chloroplastic
- Chlorophyll synthase, chloroplastic
- Probable chlorophyll
- Chlorophyllide a oxygenase, chloroplastic
- Os07g0665801 protein
- chlorophyllase
- Os02g0286700 protein
- Chlorophyll a oxygenase, putative, expressed
- ERBB-3 BINDING PROTEIN 1
- Alpha/beta hydrolase-fold family protein
Sequence:
MAATAAYLPLRAQAQVGLAPLRPSGSAAAGARLPGRTARRRLAARGGPEAAGIRAEAVPGGGGVARRAAMVPPYNVLITGSTKGIGYALAKEFLKAGDNVVICSRSAERVESAVTDLKKEFGEQHVWGIVCDVREGKDVKALVDFARDKMKYIDIWINNAGSNAYSYKPLVETSDEALMEVITTNTLGLMICCREAINMMRNQPRGGHIFNIDGAGSDGRPTPRFAAYGATKRSVVHLTKSLQAELQMNEVNNVMVHNLSPGMVTTDLLMSGATTKQAKFFINILAEPANVVADYLVPNIRAIPTNQSMKPTYIRFLTGLKAYSRIFSRIAFGARRNKYVAED
Protein: Epididymis secretory sperm binding protein (Hydroxysteroid (17-beta) dehydrogenase 4, isoform CRA_b) (Hydroxysteroid dehydrogenase 4 isoform 1) (A0A0S2Z4J1)
Organism: Homo sapiens (Human)
Subcellular location: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
Interaction partners:
Sequence:
MGSPLRFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDFKGVGKGSLAADKVVEEIRRRGGKAVANYDSVEEGEKVVKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPNAGSRMTQTVMPEDLVEALKPEYVAPLVLWLCHESCEENGGLFEVGAGWIGKLRWERTLGAIVRQKNHPMTPEAVKANWKKICDFENASKPQSIQESTGSIIEVLSKIDSEGGVSANHTSRATSTATSGFAGAIGQKLPPFSYAYTELEAIMYALGVGASIKDPKDLKFIYEGSSDFSCLPTFGVIIGQKSMMGGGLAEIPGLSINFAKVLHGEQYLELYKPLPRAGKLKCEAVVADVLDKGSGVVIIMDVYSYSEKELICHNQFSLFLVGSGGFGGKRTSDKVKVAVAIPNRPPDAVLTDTTSLNQAALYRLSGDWNPLHIDPNFASLAGFDKPILHGLCTFGFSARRVLQQFADNDVSRFKAIKARFAKPVYPGQTLQTEMWKEGNRIHFQTKVQETGDIVISNAYVDLAPTSGTSAKTPSEGGKLQSTFVFEEIGRRLKDIGPEVVKKVNAVFEWHITKGGNIGAKWTIDLKSGSGKVYQGPAKGAADTTIILSDEDFMEVVLGKLDPQKAFFSGRLKARGNIMLSQKLQMILKDYAKL
Protein: AR781 (AR781, similar to yeast pheromone receptor) (O48720)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- N-lysine methyltransferase
- Eukaryotic aspartyl protease family protein
- Eukaryotic translation initiation factor 4B3
- Plant intracellular Ras-group-related LRR protein 9
- Peptide methionine sulfoxide reductase B6
- Lectin-like protein At3g16530
Sequence:
MEVMSLTAPSSPRQLSGCFLSAPTSPRRFNEFYREFEEAATRNFSDRLTVPFDWEETPGTPRKITNDDDDDIDFAFEIGGKLETTSLFAEELFDGGKIKPLKPPPYLQLDHHHQPQILSPRSPRSPIAHGKNIIRKAFSPRKKPDNVDPFEVAMDKARNGLGEERGRGRRQNSGRRVARSLSPFRVSAYPWEEQEQEQEQEQRDVQEQRKGTLSSIPSTSSSACVSCKSSSSKKWRLKDFLLFRSASEGRARHNKDSVKTFTSLFRKQEDTKNSSSRGRGSSSVSAHEFHYMSKKAETKDLKKKTFLPYMQIGRFAF
Protein: 26S proteasome regulatory subunit 8 homolog (Protein let1) (P41836)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: The 26S proteasome is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex (By similarity).
Subcellular location: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}.
Interaction partners:
- Probable 26S proteasome regulatory subunit rpn9
- 26S proteasome regulatory subunit rpn2
- 26S proteasome regulatory subunit rpn1
- Probable 26S proteasome regulatory subunit rpn6
- 26S proteasome regulatory subunit rpn12
- 26S proteasome regulatory subunit 6B homolog
- 26S proteasome regulatory subunit rpn10
- 26S proteasome regulatory subunit rpn7
- 26S proteasome regulatory subunit rpn502
- 26S proteasome regulatory subunit 4 homolog
Sequence:
MTEVLKTNVLQSNENIVQYYTQKIQDAELAILQKTQNLRRLEAQRNGLNARVRLLREEIQLLQEPGSYVGEVIKTMGKNKVLVKVHPEGKYVVDISPDIDIKEIKPNIRVALRNDSYQLIKILPNKVDPLVSLMMVEKIPDSTYEMVGGLEKQIKEIKEVIELPVKHPELFESLGIPQPKGILLYGPPGTGKTLLARAVAHHTDCKFIRVSGSELVQKYIGEGSRMVRELFVMAREHAPSIIFMDEIDSIGSSRSDSSGGSGDSEVQRTMLELLNQLDGFEATKNIKVIMATNRIDILDPALLRPGRIDRKIEFPPPSAEARAEILRIHSRSMNLTRGIDLKSIAEKMNGASGAELKGVCTEAGMFALRERRVHVTQEDFELAVAKVLNKGDSGEMSLQKLFK
Protein: Novobiocin biosynthesis protein H (EC 6.-.-.-) (Q9L9G0)
Organism: Streptomyces niveus (Streptomyces spheroides)
Function: Together with NovI, involved in the formation of a beta-OH-Tyr intermediate in the novobiocin biosynthesis pathway, an aminocoumarin family antibiotic that targets bacterial DNA gyrases. The ATP-dependent AMP-binding region activates L-Tyr as L-tyrosyl-AMP and then transfers the L-tyrosyl group to the acyl carrier domain through thioester formation to form a tyrosyl-S intermediate that is covalently tethered to NovH (L-Tyr-S-NovH).
Interaction partners:
Sequence:
MFNTRANKASDQSPTIPTESATLAELWERTVRSRPSSPAIVTNGETLSYDEVNARANRLARLLLDEGAGPGRLVALALPRSSHLVISVLAVAKAGAVFLPLDVNHPRERLSYQLADARPALLCTVRSAAARLPDGIEMPRVLLDSPERTAVLDALPDTDLTDDERGGPLAATDLAYVIYTSGSTGRPKGVALTGAGLPALAAAKVAAMRVTGDSRVLQFASPGFDAYLTELLAAFTAGATLVVPGTDTLAGDPLRRALRDGRVSHAVLPPAAVATMSPDAVPDLRVLVVAGEACPAGLVERWAPGRLLINAYGPTECTVCATMTGPLTPTDEVTIGRPIPGVSVYILDAERRPAAPGEIGELYLSGAGLAQGYLNSPDLTAQMFVPNPFAADGERMYRTGDLASRRADGDILFHGRIDDQVELRGFRVELGEVESVLSQHPDVAQAVAALWTDPAEGPQLVTYVVPAPGTTPSAGELREHAGRFLPDFMVPSAFTTIDAVPLTPGGKTDRAGLPDPVKATQPAGLGPRTPAEKVLCDIFRDLFDLVEIDVRSNFFEMGGNSILAVDLIQRAQEAGLTLMPRTVIDHPTIEQLAAIATLEE
Protein: Rap phosphatase (Tetratricopeptide repeat protein) (R9RWQ9)
Organism: Bacillus subtilis subsp. subtilis NCIB 3610 = ATCC 6051 = DSM 10
Interaction partners:
Sequence:
MSVSDLIPYHYVTTDINHWYVVIKQGRVEKAKEMKRKVEKEFDMMEKNEKVAVYLQLLKLRHEIMLSYLEPDSVKNIDGVYSDLKKTRENMAPESLTNTIEFYYNFFTGMYHFRTRDLVIALTYYREAEKYLDLLDANANTDKAEFYFKVSEVYYYMKETHFSMNYAQRAYSIFKEQKDAQGNLTYGKEMVQCQFVIFGNWLDKMCYEDALETAEKALKDALEIGEQHLIGSAHFTVGLCYNNLEELDNAEKHFQIAYEIHKDRKHIYESKAIFNLAYVKAKKNDLKAALELYQEGQKVAARHNNQEVTEKLKLVKGLYLSFDLQTLREVFKFFEEKNLYGDMEEYAVAVADFLTNKEDRHDAVDFYQMAIEARKQIQRGKHLNEKM
Protein: protein-tyrosine-phosphatase (EC 3.1.3.48) (K7EIE9)
Organism: Homo sapiens (Human)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004308}.
Interaction partners:
Sequence:
XKYRMGLIQTPDQLRFSYMAIIEGAKCIKGDSSIQKRWKELSKEDLSPAFDHSPNKIMTEKYNGNRIGLEEEKLTGDRCTGLSSKMQDTMEENSESALRKRIREDRKATTAQKVQQMKQRLNENERKRKRHRLLLIHQISAVKNFSYFEFS
Protein: Altered inheritance of mitochondria protein 36, mitochondrial (Found in mitochondria protein 39) (Q5ALN1)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Mitochondrion membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MFARLVPRLQPQLLSKRVLTARYPMLTTTPIYHQTPMQIIKRNYVIVHRERKKEPVIRYLFYMLVASWVAIYFVANRVDKKKPPQQSFTEREFQSYEEETGLKRRNKLISHTMNSKYKFYVIPYVHDEEELKKVANLLQHKDENATVKIIDPAQLIEEQKKDEGMKYHYLLEDLDEQGRPYPPGLITAVIKQEIYKILNTREGTFDTNFIIKNYPQTTNEAIKFENDISDIQKCLILHYDMLNELPKNKTDEEQRAIKNVDGYFDSVGKSKTLVEKFDPMDKEFEEIMLEDI
Protein: Phosphoacetylglucosamine mutase (PAGM) (EC 5.4.2.3) (Acetylglucosamine phosphomutase) (N-acetylglucosamine-phosphate mutase) (Q4WJF0)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Interaction partners:
- UDP-N-acetylglucosamine diphosphorylase
- Glucosamine 6-phosphate N-acetyltransferase
- N-acetylglucosamine-6-phosphate deacetylase
- N-acetylglucosamine-6-phosphate deacetylase
- N-acetyl-D-glucosamine kinase
- glutamine--fructose-6-phosphate transaminase
- Glutamine amidotransferase, putative
- Phosphoglucomutase
- Glucose-6-phosphate isomerase
- Galactose-1-phosphate uridylyltransferase
Sequence:
MASPAVRKAISDAALQYAKPEGKIFQYGTAGFRMKADLLNTVVYAVGLLATLRSKKLSGQWIGVMVTASHNPAEDNGVKLVDPMVSSYGTFDGGMKGEFADGEMLEAEWEAYATKLANAPLENIGDVYDELVKEIDVSMENPARVVFARDTRASGSRLIGVLSAALTATEAEFIDMKFMTTPQLHYVVRCKNTLGTHYEYGEPTEQGYYEKLAAAFKRVMRGVKVKGSLTVDCANGVGGPKLRELIKYLPEDTGLDIKIVNDDVINPDSLNFECGADYVKTKQRAPPSSKASILDRCASLDGDADRIVYYFLDGGNVFRLLDGDRIATLAASFIGDLARSAGIAQKLKIGVVQTAYANGSSTEYIEKVLKLPSVCTNTGVKHLHHAAMRFDVGVYFEANGHGTITFSENALKTIKNTEPQSPAQQRSLECLQALTDLINQAVGDAISDMLLVEAILAHKGWTPKEWLATYTDLPSRLVRVEVADRSIFKAYDAERKLESPPGLQAKIDSLQSRYNKGRSFARASGTEDAVRVYAEAASRSEADDLATRVANAVRDAGTVKEILQAS
Protein: Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial (EC 1.3.8.5) (2-methyl branched chain acyl-CoA dehydrogenase) (2-methylbutyryl-coenzyme A dehydrogenase) (Q95U46)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MMNSLKKLPVRMLANAARQQSAAMSSATGLPPPLTFLTDDEKMMKETVAKLAQEQIQPLVKKMDFEHKFDPSVLKAVFENGLMGIEIDTELGGSGCNFMTNIVVVEELSKIDPAVAAFVDIHNTLVNSLMIKFGNAEQKAKYLPKLAQEYAGSFALTEPGAGSDAFSLKTVAKKDGSHYVINGSKMWISNSDVAGVFLIFANAKPEDGYRGITTFIVDRETPGLIVNKPEDKLGIRASGTCQLTFDNVRVPEENILGTFGHGYKYAAGFLNEGRIGIAAQMVGLAQGTFDATIPYLLERKQFGDAIYNFQSMQHQIATVATEIEAARLMTYNAARLQEQGVPFQKEAAMAKYYASEVAQRAAIKCVDWMGGVGFTRDFPQEKYYRDVKIGAIYEGTTNMQLSTIAKCIKKDYAA
Protein: Myosin-binding protein C, cardiac-type (Cardiac MyBP-C) (C-protein, cardiac muscle isoform) (P56741)
Organism: Rattus norvegicus (Rat)
Function: Thick filament-associated protein located in the crossbridge region of vertebrate striated muscle a bands. In vitro it binds MHC, F-actin and native thin filaments, and modifies the activity of actin-activated myosin ATPase. It may modulate muscle contraction or may play a more structural role.
Interaction partners:
- Myosin-6
- Myosin-7
- Troponin I, cardiac muscle
- Troponin T, cardiac muscle
- Myosin light chain 3
- Myosin regulatory light chain 2, ventricular/cardiac muscle isoform
- Uncharacterized protein.
- Actin, alpha cardiac muscle 1
- Tropomyosin alpha-1 chain
- F-actin cross-linking protein
Sequence:
MPEPGKRPVSAFTKKPRSVEVTAGSAAVFEAETERSGLKVQWQRDGSDIAANDKYGLAAEGKRHTLTVRDVGPDDQGSYAVIAGSSKVKFDLKVTEPAPPEKAESAVAPTSMEAPETPKEVPALATQLEGNVSSPEGSVSVTQDGSVAGSQGAPDDPIGLFLMRPQDGEVTVGGSIVFSARVAGASLLKPPVVKWFKGKWVDLSSKVGQHLQLHDSYDRASKVYLFELHITDAQATSAGGYRCEVSTKDKFDSCNFNLTVHEAIGSGDLDLRSAFRRTSLAGTGRRTSDSHEDAGTLDFSSLLKKSSFRRDSKLEAPAEEDVWEILRQAPPSEYERIAFQHGVTDLRGMLKRLKGMKHDEKKSTAFQKKLEPAYQVNKGHKIRLTVELADPDAEVKWLKNGQEIQMSGRYIFESIGAKRTLTISQCSLADDAAYQCVVGGEKCSTELFVKEPPVLITRSLEDQLVMVGQRVEFECEVSEEGAQVKWLKDGVELTREETFKYRFKKDGRKHHLIINEATLEDAGHYAVRTSGGQALAELIVQEKKLEVYQSIADLAVGAKDQAVFKCEVSDENVRGVWLKNGKELVPDNRIKVSHIGRVHKLTIDDVTPADEADYSFVPEGFACNLSAKLHFMEVKIDFVPRQEPPKIHLDCPGSTPDTIVVVAGNKLRLDVPISGDPAPTVIWQKTITQGKKASAGPPPGAPEDAGADEEWVFDKKLLCETEGRVRVETTKDRSVFTVEGAEKEDEGVYTVTVKNPVGEDQVNLTVKVIDVPDAPAAPKISNVGEDSCIVQWEPPAYDGGQPVLGYILERKKKKSYRWMRLNFDLLRELSHEARRMIEGVAYEMRVYAVNAVGMSRPSPASQPFMPIGPPGEPTHLTVEDVSDTTVSLKWRPPERVGAGGLDGYSVEYCQEGCSEWVTALQGLTERTSLLVKDLPTGARLLFRVRAHNVAGPGGPIITKEPVTVQEILQRPRLQLPRHLRQTIQKKVGEPVNLLIPFQGKPRPQVTWTKEGQPLAGEEVSIRNSPTDTILFIRAAHRTHSGTYQVTVRIENMEDKATLVLQIVDKPSPPLDIRVVETWGFSVALEWKPPQDDGNTEIWGYTVQKADKKTMEWFTVLEHYRQTHCVVSELIIGNGYYFRVFSHNMVGSSDRAAATKEPIFIPRPGITYEPPKYKALDFSEAPSFTQPLTNRSIIAGYNAILCCAVRGSPKPKISWFKNGLDLGEDARFRMFCKQGVLTLEIRKPCPYDGGVYVCRATNLQGEAQCECRLEVRVPQ
Protein: Protein arginine N-methyltransferase 3 (EC 2.1.1.319) (Heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 3) (Q922H1)
Organism: Mus musculus (Mouse)
Function: Protein-arginine N-methyltransferase that catalyzes both the monomethylation and asymmetric dimethylation of the guanidino nitrogens of arginine residues in target proteins, and therefore falls into the group of type I methyltransferases (By similarity). May regulate retinoic acid synthesis and signaling by inhibiting ALDH1A1 retinal dehydrogenase activity (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000305|PubMed:15473865}. Nucleus {ECO:0000250|UniProtKB:O60678}.
Interaction partners:
- Small ribosomal subunit protein uS5
- Protein arginine N-methyltransferase 5
- Protein arginine N-methyltransferase 1
- Band 4.1-like protein 3
- Programmed cell death protein 2-like
- Histone-lysine N-methyltransferase SETD7
- Methylosome protein WDR77
Sequence:
MCSLAAGNGRGAELGPEPLELSDSGDDAGWEDEDADTEPAHGRQHTPCLFCDRLFASAEETFSHCKLEHQFNIDSMVHKHGLEFYGYIKLINFIRLKNPTVEYMNSIYNPVPWEKDEYLKPVLEDDLLLQFDVEDLYEPVSTPFSYPNGLSESASVVEKLKHMEARALSAEAALARAREDLQKMKQFAQDFVMNVDVRTCSSTTTIADLQEDEDGVYFSSYGHYGIHEEMLKDKVRTESYRDFIYQNPHIFKDKVVLDVGCGTGILSMFAAKVGAKKVIAVDQSEILYQAMDIIRLNKLEDTIVLIKGKIEEVSLPVEKVDVIISEWMGYFLLFESMLDSVLYAKSKYLAKGGSVYPDICTISLVAVSDVSKHADRIAFWDDVYGFNMSCMKKAVIPEAVVEVVDHKTLISDPCDIKHIDCHTTSISDLEFSSDFTLRTTKTAMCTAVAGYFDIYFEKNCHNRVVFSTGPQSTKTHWKQTVFLLEKPFPVKAGEALKGKITVHKNKKDPRSLIVTLTLNSSTQTYSLQ
Protein: Ubiquitin associated protein 1 (A0A6G6AA68)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MASKKLGADFHGTFSYLDDVPFKTGDKFKTPAKVGLPIGFSLPDCLQVVREVQYDFSLEKKTIEWAEEIKKIEEAEREAECKIAEAEAKVNSKSGPEGDSKMSFSKTHSTATMPPPINPILASLQHNSILTPTRVSSSATKQKVLSPPHIKADFNLADFECEEDPFDNLELKTIDEKEELRNILVGTTGPIMAQLLDNNLPRGGSGSVLQDEEVLASLERATLDFKPLHKPNGFITLPQLGNCEKMSLSSKVSLPPIPAVSNIKSLSFPKLDSDDSNQKTAKLASTFHSTSCLRNGTFQNSLKPSTQSSASELNGHHTLGLSALNLDSGTEMPALTSSQMPSLSVLSVCTEESSPPNTGPTVTPPNFSVSQVPNMPSCPQAYSELQMLSPSERQCVETVVNMGYSYECVLRAMKKKGENIEQILDYLFAHGQLCEKGFDPLLVEEALEMHQCSEEKMMEFLQLMSKFKEMGFELKDIKEVLLLHNNDQDNALEDLMARAGAS
Protein: BUB1 N-terminal domain-containing protein (O02053)
Organism: Caenorhabditis elegans
Interaction partners:
- Mitotic spindle assembly checkpoint protein MAD2A
- WD repeat-containing protein fzy-1
- Mitotic checkpoint protein bub-3
- MAD related
- Kinetochore protein ndc-80
- Cell division cycle protein 23 homolog
- Outer kinetochore KNL1 complex subunit knl-1
- Kinetochore protein Nuf2 homolog
- Kinetochore-associated protein rod-1
- Centromere/kinetochore protein zw10 homolog
Sequence:
MAEEPYVFTLKKRNNDDAEDDWDRYSENVRPTRRGRKIDALKRNVEEVVTEETARLKLDQLLEELQNLECSEESEELQKILDFCSWFEEKLAIGFHKVYYELLWKIISRHGFLEKYKEDERMLKIWEKMADNSAGHAHDIYQFAISRKSLVKCAALYARWSQSVELAGAYVEARRVLILARTNCAVPIQIVNDAEDALEMREMRRHLQERDSDDDEEEEETRKAFTNLPVIGDNHTVPIVRLPSMCSDTTKKAMKFDTGNVERVNPVCKDNQMQPFEVLSYTDADDVEYLRNVHELHAHIERYAIKETTNPSITGSSTSEAAAVTIYPVSSSEFEVWTVEGSGPTKAKARMAIKRVFKDLSFEEYAASLLPNHPSMVRATAKKLDFDETL