wanglab/gogpt-training-data huggingface dataset:
Protein: CROL ALPHA (Crooked legs, isoform A) (Crooked legs, isoform E) (Crooked legs, isoform I) (O61360)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MQHVSAASSVPSVVTPVVTTGGTTITLGGPPPLPKSEHKEDGKPPHGIEMYKVNIEDISQLFTYHEVFGKIHGDVVNHQLAAAHGGQLPPPPPLPPQVTSHAASAAAAAAAASTNNAAVAAVMASANAAAAAAAAASAGGGLPPATSGNGGQQVTVTTTSSSTSSGGSTTSGGTTTTAGELLMPKMEGGIHGVDGSGNGGNGGGQNVALAPDGTPIATGTHVCDICGKMFQFRYQLIVHRRYHSERKPFMCQVCGQGFTTSQDLTRHGKIHIGGPMFTCIVCFNVFANNTSLERHMKRHSTDKPFACTICQKTFARKEHLDNHFRSHTGETPFRCQYCAKTFTRKEHMVNHVRKHTGETPHRCDICKKSFTRKEHYVNHYMWHTGQTPHQCDVCGKKYTRKEHLANHMRSHTNETPFRCEICGKSFSRKEHFTNHILWHTGETPHRCDFCSKTFTRKEHLLNHVRQHTGESPHRCSYCMKTFTRKEHLVNHIRQHTGETPFKCTYCTKAFTRKDHMVNHVRQHTGESPHKCTYCTKTFTRKEHLTNHVRQHTGDSPHRCSYCKKTFTRKEHLTNHVRLHTGDSPHKCEYCQKTFTRKEHLNNHMRQHSSDNPHCCNVCNKPFTRKEHLINHMSRCHTGDRPFTCETCGKSFPLKGNLLFHQRSHTKGQEMERPFACEKCPKNFICKGHLVSHMRSHSGEKPHACTLCSKAFVERGNLKRHMKMNHPDAMMPPPPVHPHPQIPAGVLTQVKQEVKPIIIPHHSATTTMHTIQQITAGAAGGAGAVQLTPGLVPLVTSTLISHNAAAQQQSQKQQAAAAAAAQQQAAAAAAAQQQAAQQQAAAAHQQHQQQVAAQHQQQAAVAAHQQQQQQLQQQQQLLQLSIQQAAHHHQQEQHRQQQQQQHQQQQQQQHHQQQQQGHPQAPPPQQQQQPPPIALISDPSALARAAIQLQHLPANVEQHPVVY
Protein: ATP-dependent RNA helicase DBP10 (EC 3.6.4.13) (DEAD box protein 10) (Q12389)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits and is required for the normal formation of 25S and 5.8S rRNAs.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:10871363}.
Interaction partners:
- 25S rRNA
- Nuclear GTP-binding protein NUG1
- Ribosome biogenesis protein ERB1
- Ribosome biogenesis protein RPF2
- Nucleolar complex protein 2
- Pescadillo homolog
- Ribosome biogenesis protein 15
- 27S pre-rRNA
- Nucleolar GTP-binding protein 1
- Ribosome biogenesis protein NSA1
Sequence:
MAGVQKRKRDLEDQDDNGSEEDDIAFDIANEIALNDSESDANDSDSEVEADYGPNDVQDVIEYSSDEEEGVNNKKKAENKDIKKKKNSKKEIAAFPMLEMSDDENNASGKTQTGDDEDDVNEYFSTNNLEKTKHKKGSFPSFGLSKIVLNNIKRKGFRQPTPIQRKTIPLILQSRDIVGMARTGSGKTAAFILPMVEKLKSHSGKIGARAVILSPSRELAMQTFNVFKDFARGTELRSVLLTGGDSLEEQFGMMMTNPDVIIATPGRFLHLKVEMNLDLKSVEYVVFDEADRLFEMGFQEQLNELLASLPTTRQTLLFSATLPNSLVDFVKAGLVNPVLVRLDAETKVSENLEMLFLSSKNADREANLLYILQEIIKIPLATSEQLQKLQNSNNEADSDSDDENDRQKKRRNFKKEKFRKQKMPAANELPSEKATILFVPTRHHVEYISQLLRDCGYLISYIYGTLDQHARKRQLYNFRAGLTSILVVTDVAARGVDIPMLANVINYTLPGSSKIFVHRVGRTARAGNKGWAYSIVAENELPYLLDLELFLGKKILLTPMYDSLVDVMKKRWIDEGKPEYQFQPPKLSYTKRLVLGSCPRLDVEGLGDLYKNLMSSNFDLQLAKKTAMKAEKLYYRTRTSASPESLKRSKEIISSGWDAQNAFFGKNEEKEKLDFLAKLQNRRNKETVFEFTRNPDDEMAVFMKRRRKQLAPIQRKATERRELLEKERMAGLSHSIEDEILKGDDGETGYTVSEDALKEFEDADQLLEAQENENKKKKKPKSFKDPTFFLSHYAPAGDIQDKQLQITNGFANDAAQAAYDLNSDDKVQVHKQTATVKWDKKRKKYVNTQGIDNKKYIIGESGQKIAASFRSGRFDDWSKARNLKPLKVGSRETSIPSNLLEDPSQGPAANGRTVRGKFKHKQMKAPKMPDKHRDNYYSQKKKVEKALQSGISVKGYNNAPGLRSELKSTEQIRKDRIIAEKKRAKNARPSKKRKF
Protein: G protein-coupled receptor 107 (G5E994)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MAALAPVGSPASRGPRLAAGLRLLPMLGLLQLLAEPGLGRVHHLALKDDVRHKVHLNTFGFFKDGYMVVNVSSLSLNEPEDKDVTIGFSLDRTKNDGFSSYLDEDVNYCILKKQSVSVTLLILDISRSEVRVKSPPEAGTQLPKIIFSRDEKVLGQSQEPNVNPASAGNQTQKTQDGGKSKRSTVDSKAMGEKSFSVHNNGGAVSFQFFFNISTDDQEGLYSLYFHKCLGKELPSDKFTFSLDIEITEKNPDSYLSAGEIPLPKLYISMAFFFFLSGTIWIHILRKRRNDVFKIHWLMAALPFTKSLSLVFHAIDYHYISSQGFPIEGWAVVYYITHLLKGALLFITIALIGTGWAFIKHILSDKDKKIFMIVIPLQVLANVAYIIIESTEEGTTEYGLWKDSLFLVDLLCCGAILFPVVWSIRHLQEASATDGKGDSMGPLQQRANLRAGSRIAAINLAKLKLFRHYYVLIVCYIYFTRIIAFLLKLAVPFQWKWLYQLLDETATLVFFVLTGYKFRPASDNPYLQLSQEEEDLEMESVVTTSGVMESMKKVKKVTNGSVEPQGEWEGAV
Protein: V-type proton ATPase subunit H (A0A0G2K9J2)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- V-type proton ATPase subunit F
- V-type proton ATPase 21 kDa proteolipid subunit c''
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase subunit D
- V-type proton ATPase 16 kDa proteolipid subunit c
- V-type proton ATPase proteolipid subunit
- V-type proton ATPase subunit C 1
- V-type proton ATPase subunit S1
- V-type proton ATPase subunit B, brain isoform
- V-type proton ATPase subunit E 1
Sequence:
MTKMDIRGAVDAAVPTNIIAAKAAEVRANKVNWQSYLQGQMISAEDCEFIQRFEMKRCSEEKQEMLQTEGSQCAKTFINLMTHISKEQTVQYILTMVDDMLQENHQRVSIFFDYAKRSKSTAWPYFLPMLNRQDPFTVHMAARIIAKLAAWGKELMEGSDLNYYFNWIKTQLSSQKLRGSGVAVETGTISASDSSQYVQCVAGCLQLMLRVNEYRFAWVEADGVNCIMGVLSNKCGFQLQYQMIFSIWLLAFSPQMCEHLRRYNIIPVLSDILQESVKEKVTRIILAAFRNFLEKSTERETRQEYALAMIQCKVLKQLENLEQQKYDDEDISEDIKFLLEKLGESVQDLSSFDEYSSELKSGRLEWSPVHKSEKFWRENAVRLNEKNYELLKILTKLLEVSDDPQVLAVAAHDVGEYVRHYPRGKRVVLLISFES
Protein: Zinc finger CCCH domain-containing protein 23 (AtC3H23) (Protein ATCTH) (O82307)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Small ribosomal subunit protein eS12z
Sequence:
MMIGENKNRPHPTIHIPQWDQINDPTATISSPFSSVNLNSVNDYPHSPSPYLDSFASLFRYLPSNELTNDSDSSSGDESSPLTDSFSSDEFRIYEFKIRRCARGRSHDWTECPFAHPGEKARRRDPRKFHYSGTACPEFRKGSCRRGDSCEFSHGVFECWLHPSRYRTQPCKDGTSCRRRICFFAHTTEQLRVLPCSLDPDLGFFSGLATSPTSILVSPSFSPPSESPPLSPSTGELIASMRKMQLNGGGCSWSSPMRSAVRLPFSSSLRPIQAATWPRIREFEIEEAPAMEFVESGKELRAEMYARLSRENSLG
Protein: DNA damage-binding protein 1a (UV-damaged DNA-binding protein 1a) (DDB1a) (Q9M0V3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of light signal transduction machinery. Involved in repression of photomorphogenesis in darkness by participating in the CDD complex, a complex probably required to regulate the activity of ubiquitin conjugating enzymes (E2s). Repression of photomorphogenesis is probably mediated by ubiquitination and subsequent degradation of photomorphogenesis-promoting factors such as HY5, HYH and LAF1. Plays a role in DNA repair by forming with DDB2 the UV-damaged DNA-binding protein complex (UV-DDB). Component of the CUL4-RBX1-DDB1-PRL1 E3 ubiquitin-protein ligase complex.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18551167, ECO:0000269|PubMed:26147561}. Nucleus {ECO:0000269|PubMed:18551167, ECO:0000269|PubMed:26147561}. Note=Translocates to the nucleus upon exposure to UV (PubMed:18551167). Excluded from the nucleus when in complex with farnesylated ASG2 (PubMed:26147561). {ECO:0000269|PubMed:18551167, ECO:0000269|PubMed:26147561}.
Interaction partners:
- Protein DAMAGED DNA-BINDING 2
- Cullin-4
- WD repeat-containing protein ATCSA-1
- DET1- and DDB1-associated protein 1
- Light-mediated development protein DET1
- Putative cullin-like protein 4
- Transducin/WD40 repeat-like superfamily protein
- Cullin-like protein 5
- Transducin/WD40 repeat-like superfamily protein
- Protein ALTERED SEED GERMINATION 2
Sequence:
MSSWNYVVTAHKPTSVTHSCVGNFTSPQELNLIVAKCTRIEIHLLTPQGLQPMLDVPIYGRIATLELFRPHGEAQDFLFIATERYKFCVLQWDPESSELITRAMGDVSDRIGRPTDNGQIGIIDPDCRLIGLHLYDGLFKVIPFDNKGQLKEAFNIRLEELQVLDIKFLFGCAKPTIAVLYQDNKDARHVKTYEVSLKDKDFVEGPWSQNSLDNGADLLIPVPPPLCGVLIIGEETIVYCSASAFKAIPIRPSITKAYGRVDVDGSRYLLGDHAGMIHLLVITHEKEKVTGLKIELLGETSIASTISYLDNAVVFVGSSYGDSQLVKLNLHPDAKGSYVEVLERYINLGPIVDFCVVDLERQGQGQVVTCSGAFKDGSLRVVRNGIGINEQASVELQGIKGMWSLKSSIDEAFDTFLVVSFISETRILAMNLEDELEETEIEGFLSQVQTLFCHDAVYNQLVQVTSNSVRLVSSTTRELRDEWHAPAGFTVNVATANASQVLLATGGGHLVYLEIGDGKLTEVQHALLEYEVSCLDINPIGDNPNYSQLAAVGMWTDISVRIFSLPELTLITKEQLGGEIIPRSVLLCAFEGISYLLCALGDGHLLNFQMDTTTGQLKDRKKVSLGTQPITLRTFSSKSATHVFAASDRPTVIYSSNKKLLYSNVNLKEVSHMCPFNSAAFPDSLAIAREGELTIGTIDDIQKLHIRTIPLGEHARRICHQEQTRTFGICSLGNQSNSEESEMHFVRLLDDQTFEFMSTYPLDSFEYGCSILSCSFTEDKNVYYCVGTAYVLPEENEPTKGRILVFIVEDGRLQLIAEKETKGAVYSLNAFNGKLLAAINQKIQLYKWMLRDDGTRELQSECGHHGHILALYVQTRGDFIVVGDLMKSISLLLYKHEEGAIEERARDYNANWMSAVEILDDDIYLGAENNFNLLTVKKNSEGATDEERGRLEVVGEYHLGEFVNRFRHGSLVMRLPDSEIGQIPTVIFGTVNGVIGVIASLPQEQYTFLEKLQSSLRKVIKGVGGLSHEQWRSFNNEKRTAEARNFLDGDLIESFLDLSRNKMEDISKSMNVQVEELCKRVEELTRLH
Protein: Putative zinc metalloproteinase C607.06c (EC 3.4.24.-) (Q9US12)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- CDP-diacylglycerol--serine O-phosphatidyltransferase
- Mitochondrial inner membrane protease atp23
- Cys-Gly metallodipeptidase dug1
- Mitochondrial intermediate peptidase
Sequence:
MSQIILDNISQNETVYNRFVIIHGRVGPRASYCPQTINVKHHENSFPEQTWVVTDLYFKAIIHVVPGDNTILFTTDDGGKLELQVYYQLLVDNPFYCIAFIVGKDSDLSFDAPHGAKNDIDEGIRKLRCAAYLWQAFTAECMYRNGYGRRSFRIEESVQPDTMSCLSPWGTERLTATINILRSDKTAEEIRSVPPDQLFHIAGDAVDKLHLPEPWHYMCMFLDTRYDPSTQKIRGHVALGGGTDMHKLGVFGSHSLHSFPSALEYVVPVFSDARRIPSYLANDANESSTIWECANIGIGAMLHELGHTLGCPHQPDGIMLRSYPIFNRSFTTREFECVRTGSKGLAPVLAKDECSWHHLDMLRFFYHPCFKLPSDPTYPSDIETNYFVKGETITFVNSTGIFLIEIEYNGQTKGWKEFNPPVGEASLTDAEIRSLSNASSNQDYRVRVLSRNFKCIDLNNVPEIIKNAKVESSFGTVYRSERYGLRGCNGKELSNILIAPEKFKPTKIRVHCGLALDGIEVFFGDESVLLGNRGGSPHDFEIQGSQIVGFQIRCGAWVDGISIVLENGKTSPFYGNANGGGLKSYLVPKGFQLVGFYGTLGPFMDSIGFFIK
Protein: Cip1-interacting zinc-finger protein (Q70KX6)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MLQRALLLQQLQGLDQFAMPPATYDGASLTMPTATLGNLRAFNVTAPSLAAPSLTPPQMVTPNLQQFFPQATRQSLLGPPPVGVPINPSQLNHSGRNTQKQARTPSSTTPNRKTVPLEDREDPTEGSEEATELQMDTCEDQDSLVGPDSMLSEPQVPEPEPFETLEPPAKRCRSSEESTEKGPTGQPQARVQPQTQMTAPKQTQTPDRLPEPPEVQMLPRIQPQALQIQTQPKLLRQAQTQTSPEHLAPQQDQVPTQAQSQEQTSEKTQDQPQTWPQGSVPPPEQASGPACATEPQLSSHAAEAGSDPDKALPEPVSAQSSEDRSREASAGGLDLGECEKRAGEMLGMWGAGSSLKVTILQSSNSRAFNTTPLTSGPRPGDSTSATPAIASTPSKQSLQFFCYICKASSSSQQEFQDHMSEAQHQQRLGEIQHSSQTCLLSLLPMPRDILEKEAEDPPPKRWCNTCQVYYVGDLIQHRRTQEHKVAKQSLRPFCTICNRYFKTPRKFVEHVKSQGHKDKAQELKTLEKETGSPDEDHFITVDAVGCFESGQEEDEDDDEEEEEEGEIEAEEEFCKQVKPRETSSEQGKGSETYNPNTAYGEDFLVPVMGYVCQICHKFYDSNSELRLSHCKSLAHFENLQKYKAKNPSPPPTRPVSRKCAINARNALTALFTSSHQPSPQDTVKMPSKVKPGSPGLPPPLRRSTRLKT
Protein: polyribonucleotide nucleotidyltransferase (EC 2.7.7.8) (Q95RX7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MTFSSGRLARFANGTAVCQMGDTAVMVTAVAKAKPNPGQGFMPLVVDYRLKNAASGRIPMNFMRRELGPSEKEILSARLIDRSLRPLFHKDYRTETQLVCNMLAMDAVHSPDVLAINAASMALSLSDIPWNGPIGAVRVGLCDGEVLINPTRRELQTSQLDLVVSATKQNLVVMLEGKGNVVLQQDLLKAIKQGTREAQFIIHEIERLQKAYGRQKREVEVAAEVDPELGKAVRSMCEMRLREIFQDSTHDKMSRDNAVNEVRSNVIDKVWSSFPDTEPSLITEQFNQTSRTIFRELIFERGLRCDGRDYDQLRNISCQVDMYKPLHGSALFQRGQTQVFCTVSLDSQESAMKLDSLAALDSGGLKAKNFMLHYEFPPYATGEVGRIGPVGRREMGHGALAERSLLPTLPNDYPFTVRLTSEVLESNGSSSMASVCGGSLALMDAGVPVSAPAAGVAIGLVTKFENDDTKHLQDYRILTDILGIEDYMGDMDMKVAGTRKGFTAIQADLKIPGIPLKVVMESLQKATDAKSNILDIMSEAIREPRKYPKESWPVSETLTVEPQQRAQLIGPSGLHMKRIYLETGTSLTAVDETHFNVFAPSQAAMDEAKELIEGYMVKERVPDLEFGGIYTAKITELRDTGVMVILYPSMPPALLHNSQLDQRKIAHPSALNLEVGQEIQVKYFGRDPVSGFMRLSRKVLQGPALGIPRSLNKSAGESGT
Protein: Tubulin alpha-1A chain (EC 3.6.5.-) (Alpha-tubulin 1) (Tubulin alpha-1 chain) [Cleaved into: Detyrosinated tubulin alpha-1A chain] (P68370)
Organism: Rattus norvegicus (Rat)
Function: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Subcellular location: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:P68369}.
Interaction partners:
- Tubulin alpha-1B chain
- Tubulin beta-4B chain
- Kinesin-like protein
- Small vasohibin-binding protein
- Tubulin beta-2B chain
- Microtubule-associated protein tau
- Tubulin beta-2A chain
- Tubulin beta-5 chain
- Cell division control protein 42 homolog
- Tubulin beta chain
Sequence:
MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSVEGEGEEEGEEY
Protein: Serine/threonine-protein kinase Nek2 (EC 2.7.11.1) (Never in mitosis A-related kinase 2) (NimA-related protein kinase 2) (O35942)
Organism: Mus musculus (Mouse)
Function: Protein kinase which is involved in the control of centrosome separation and bipolar spindle formation in mitotic cells and chromatin condensation in meiotic cells. Regulates centrosome separation (essential for the formation of bipolar spindles and high-fidelity chromosome separation) by phosphorylating centrosomal proteins such as CROCC, CEP250 and NINL, resulting in their displacement from the centrosomes. Regulates kinetochore microtubule attachment stability in mitosis via phosphorylation of NDC80. Involved in regulation of mitotic checkpoint protein complex via phosphorylation of CDC20 and MAD2L1. Plays an active role in chromatin condensation during the first meiotic division through phosphorylation of HMGA2. Phosphorylates: PPP1CC; SGO1; NECAB3 and NPM1. Essential for localization of MAD2L1 to kinetochore and MAPK1 and NPM1 to the centrosome. Phosphorylates CEP68 and CNTLN directly or indirectly (By similarity). NEK2-mediated phosphorylation of CEP68 promotes CEP68 dissociation from the centrosome and its degradation at the onset of mitosis (By similarity). Phosphorylates and activates NEK11 in G1/S-arrested cells. Involved in the regulation of centrosome disjunction (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:9187143}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P51955}. Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P51955}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}. Chromosome, centromere {ECO:0000269|PubMed:9187143}. Note=STK3/MST2 and SAV1 are required for its targeting to the centrosome. Colocalizes with SGO1 and MAD1L1 at the kinetochore. Not associated with kinetochore in the interphase but becomes associated with it upon the breakdown of the nuclear envelope. Has a nucleolar targeting/ retention activity via a coiled-coil domain at the C-terminal end (By similarity). {ECO:0000250}.
Interaction partners:
- Mitotic checkpoint serine/threonine-protein kinase BUB1 beta
- Cell division cycle protein 20 homolog
- Anaphase-promoting complex subunit 4
- Mitotic spindle assembly checkpoint protein MAD2A
- Cell division cycle protein 27 homolog
- Fizzy-related protein homolog
- Mitotic checkpoint serine/threonine-protein kinase BUB1
- Centromere protein F
- Kinetochore protein Nuf2
- Anaphase-promoting complex subunit 1
Sequence:
MPSRVEDYEVLHSIGTGSYGRCQKIRRKSDGKILVWKELDYGSMTEVEKQMLVSEVNLLRELKHPNIVSYYDRIIDRTNTTLYIVMEYCEGGDLASVISKGTKDRQYLEEEFVLRVMTQLTLALKECHRRSDGGHTVLHRDLKPANVFLDSKHNVKLGDFGLARILNHDTSFAKTFVGTPYYMSPEQMSCLSYNEKSDIWSLGCLLYELCALMPPFTAFNQKELAGKIREGRFRRIPYRYSDGLNDLITRMLNLKDYHRPSVEEILESPLIADLVAEEQRRNLERRGRRSGEPSKLPDSSPVLSELKLKERQLQDREQALRAREDILEQKERELCIRERLAEDKLARAESLMKNYSLLKEHRLLCLAGGPELDLPSSAMKKKVHFHGESKENTARSENSESYLAKSKCRDLKKRLHAAQLRAQALADIEKNYQLKSRQILGMR
Protein: Drosomycin-like 5 (Drosomycin-like E) (Drosomycin-like G) (GEO10021p1) (Q9VZR2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Dorsal-related immunity factor Dif
- Embryonic polarity protein dorsal
Sequence:
MQIKFLYLFLAVMTIFILGAKEADADCLSGRYGGPCAVWDNETCRRVCKEEGRSSGHCSPSLKCWCEGC
Protein: Ras GTPase-activating protein 3 (GAP1(IP4BP)) (Ins P4-binding protein) (R-ras GAP) (Q9QYJ2)
Organism: Rattus norvegicus (Rat)
Function: Inhibitory regulator of the Ras-cyclic AMP pathway. Binds inositol tetrakisphosphate (IP4) (By similarity).
Interaction partners:
- Ras-related protein R-Ras
- Ras-related protein M-Ras
- GTPase NRas
- RAS protein activator like 2
- GTPase HRas
Sequence:
MAVEEEGLRVFQSVRIKIGEAKNLPSYPGPNKMRDCYCTVNLDQEEVFRTKIVEKSLCPFYGEDFYCEIPRSFRHLSFYIFDRDVFRRDSIIGKVAIQKEDLQRYHNRDTWFQLQHVDADSEVQGKVHLELRLSEVITDTGVVCHKLAARIFECQGLPIVNGQCDPYATVTLAGPFRSEAKKTKVKKKTNNPQFDEVFYFEVTRPCSYSKKSHFDFEEEDVDKLEIRVDLWNASNLKFGDEFLGELRIPLHVLRYASSYEAWYFLQPRDNGSKSVKPDDLGSLRLNVVYTEDHVFSSEYYSPLRDLLLKSADVEPVSASAAHILGEVCRDKQEAAIPLVRLLLHYGRVVPFISAIASAEVKRTQDPNTIFRGNSLTSKCIDETMKLAGMHYLHVTLKPTIEEICQSHKSCEIDPVKLKDGENLENNMESLRQYVDRIFSVITKSGVSCPTVMCDIFFSLREAAAKRFQDDLDVRYTAVSSFIFLRFFAPAILSPNLFQLTPHHTDPQTSRTLTLISKTIQTLGSLSKSKSASFKESYMATFYEFFNEQKYADAVKNFLDLISSSGRRDPKSIEQPILLKEGFMIKRAQGRKRFGMKNFKKRWFRLTNHEFTYQKSKGDQPLCNIPIENILAVERLEEESFRMKNMFQVIQPERALYIQANNCVEAKDWIDILTKVSQCNQKRLTVFHPSAYLNGHWLCCRASSDTAIGCTPCTGGLPANIQLDIDGDRETERIYSLFNLYMGKLEKMQEACGSKSVYDGPEQEEYSTFIIDDPQETYRTLKQVIAGVGTLEQEHAQYRRNKFKKTRYGSQEHPIGDKSFQNYIRQQSEISTHSI
Protein: Sla2p (A0A1D8PRF5)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Clathrin heavy chain
- Clathrin light chain
- Actin cytoskeleton-regulatory complex protein SLA1
- Epsin
- Actin cytoskeleton-regulatory complex protein PAN1
- Actin cytoskeleton-regulatory complex protein END3
- ENTH domain-containing protein
- Vacuolar protein sorting-associated protein 1
- Actin
- Actin-binding protein
Sequence:
MSRAEVDLQTSVKKACNADEVPPKRKHVRACIVYTWDHKNSRAFWNAVKIQPLQSNEVQLFKALIMIHKVLQEGHPNTLKDGYRNRDFIASLATVFPSHGSAYGRLINQYDKYILQKLDFHRNNPGFNGTFEYEEYISLRAVNDPNEGYEALLNLMDLQDSINDLQKLIFATINQSHSNLCKVSALVPLIAESYGIYKFCISMLRAMYQQLGEDDALSGLVERFDSQHFMLRDFYTDCHAIKFLTSLITIPRLPNSAPNLKVTDDGQPISRPRSVSTTDTNNNNNNTNNTTPQLSSQPTSQFEQPPVAPAIDQLVGQQTGYLYQQQQEQERIQQQLELQRQQQLQQQQEQQRLFEQQQRDQERRFMEEQQALQMQQTQQQQHIGRVSELEHDLLMFKNQYDNDQQLLQQYDSRVKSLENEMSALNSTATQQIASKDEQIKNLEDQIANWTKKYESLAKLYSQLRQEHLNLLAKFKKIQQKISSAQESIMKKEKLEKDLKAKNVELADLIRERDRARLDLDRLKANKDQEIEKLQAEVRELTLTQQESGKLQSLNLSSIMTKHQSELDKLKNQLAERELKLTNLGDSEQLQSKLRDTEMELQITNESLDNALAELHRTKEDQDDIINAQIDHILLANVEKFKNLIDIFLENSVKRVLDTKHELVSPVQAGNLNASPEYVLSIIELCSDTATEFATIFNSFIAEDRNEDESSFSDIILSTSSLTSSINDLTLNAKGMTKNIVGGDNFEEKIYQLVSQILDETIGFFQNLKSEKLNKFDDIDDKIDAVIDGNYQLQTSLKSLGQYIDTLTANTNVIKVHKNGNLEELFDDEMQQTVDTISLASKFLNDLMANPQLYNGNGGNIEVDEMLLACAKAITDAVAELIKASIKSQQEIISKGGTTKSDFYKKNSRWTEGLISASKAVAGATNVLIHTADGVLKQSNSHEELIVASNEVAASTAQLVAASRVKANFVSQAQDNLEIASSNVSKACKSLVVKVEGLLIRKDEEGEKEKENIDLTKLTPYEGKTLEMEQQVKILKLENSILAARKRLAEIRKQEYKTPETVFD
Protein: Transformer-2 protein homolog (Q54Y98)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Sequence-specific RNA-binding protein which participates in the control of pre-mRNA splicing.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Small ribosomal subunit protein eS30
Sequence:
MEVADRMMSNGVDNDRRSSPSPHRGNGDMNNGNGNGNRDSRERSPPRGNSRERSPPRGGSPNRGGSPNRGGSPNRGGSPNRGGSPSRDDKRRYGNGGNGETRNRLANTASPSNVLGVFGLAPQTEERDLKDEFSRFGKIDHVDLIMDRKTGRSKCFGFVYFENKEDAVRAKEECQDLQLHGKSIRTDFSATKKPHEPTPGKYFGNPRYDSRRSPPRFSPYGGGDRYGRGDYGGRGGGGDRYGRDDRGGDRYGRDDRGGDRYGGRDDRGGDRYGGRDERGGDRGGDRYGRDDRDRHREDSRDRYNDRGGDRYNDRFRDERPRDSYRR
Protein: Protein kinase domain-containing protein (Q38CA8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MAFLLRAIGFTESIPGFPYTPCSGSSTTTADTPTITWTMRQGECDESKRSVTIFSVNLADMEPRKRELVRHAMKRAKSLLLPGILRCYGAAEHRDTVYLATEPCEPLSKMKCGQMGSPLATSGDDDDEGEAFNDIVALGLKAVGSAVSALHKNKLIHGNVGRDSVFVISTGEWRLFGLELVSGFDDVGSSYLSYCSLLPAYRRPPETQHTNYESGGKTCAIDSWGLACLIYEVLGVNDQTSGKLSQSCSTEDLRSCRTLPRTLQSGFSGLCAVNPKMRHDVDRFLRTSDFIISSDYVQSMQMLDDYSLKDAAERERFMEHLANVVHTFPRDACKHLVLQKLRASFTFGILPGVVDTVVKIAARMPSPEEYATHVSPVIVALFRSKERMVRLRILQHAAELLPQMPPAVVDGEVWSEYASGFESPIAAIREHSARALVPIAPLLTEKRIVNDVPKYIAQLQQDSEGPIRTNATIALCLIADTIPAEYRSKLFAQRFGRMLKDPFAPSRTAALRSFHTTLKHFTAQDIAELVIPGVSPLSMDKVAEVRAVALDVIHAAVSRLDANHREISSSTANEGNVIPPAGVVNNNTNGAGNEVKGSNAALDTKGWGSSGSSSVIQLESTTKGGMENSIPAASKASPFPQKVWGSQSSPSVREDDEESWGEEIQMKPQKLRLHGTATRNGTGAVVPDSLTSDDHPEDKRTLKIRKKGIGASRLS
Protein: TBC1 domain family member 3 (Prostate cancer gene 17 protein) (Protein TRE17-alpha) (Rab GTPase-activating protein PRC17) (Q8IZP1)
Organism: Homo sapiens (Human)
Function: Acts as a GTPase activating protein for RAB5. Does not act on RAB4 or RAB11.
Subcellular location: Cell membrane {ECO:0000269|PubMed:23578663}; Lipid-anchor {ECO:0000269|PubMed:23578663}. Note=Associated with lipid rafts.
Interaction partners:
- Ubiquitin carboxyl-terminal hydrolase 32
Sequence:
MDVVEVAGSWWAQEREDIIMKYEKGHRAGLPEDKGPKPFRSYNNNVDHLGIVHETELPPLTAREAKQIRREISRKSKWVDMLGDWEKYKSSRKLIDRAYKGMPMNIRGPMWSVLLNTEEMKLKNPGRYQIMKEKGKRSSEHIQRIDRDVSGTLRKHIFFRDRYGTKQRELLHILLAYEEYNPEVGYCRDLSHIAALFLLYLPEEDAFWALVQLLASERHSLQGFHSPNGGTVQGLQDQQEHVVATSQPKTMGHQDKKDLCGQCSPLGCLIRILIDGISLGLTLRLWDVYLVEGEQALMPITRIAFKVQQKRLTKTSRCGPWARFCNRFVDTWARDEDTVLKHLRASMKKLTRKKGDLPPPAKPEQGSSASRPVPASRGGKTLCKGDRQAPPGPPARFPRPIWSASPPRAPRSSTPCPGGAVREDTYPVGTQGVPSPALAQGGPQGSWRFLQWNSMPRLPTDLDVEGPWFRHYDFRQSCWVRAISQEDQLAPCWQAEHPAERVRSAFAAPSTDSDQGTPFRARDEQQCAPTSGPCLCGLHLESSQFPPGF
Protein: Extracellular sulfatase Sulf-2 (hSulf-2) (Arylsulfatase) (EC 3.1.6.1) (N-acetylglucosamine-6-sulfatase) (EC 3.1.6.14) [Cleaved into: Extracellular sulfatase Sulf-2 secreted form] (Q8IWU5)
Organism: Homo sapiens (Human)
Function: Exhibits arylsulfatase activity and highly specific endoglucosamine-6-sulfatase activity. It can remove sulfate from the C-6 position of glucosamine within specific subregions of intact heparin.
Subcellular location: Endoplasmic reticulum {ECO:0000250|UniProtKB:Q8VI60}. Golgi apparatus, Golgi stack {ECO:0000250|UniProtKB:Q8VI60}. Cell surface {ECO:0000269|PubMed:12368295, ECO:0000269|PubMed:35294879}.; SUBCELLULAR LOCATION: [Extracellular sulfatase Sulf-2 secreted form]: Secreted {ECO:0000269|PubMed:12368295, ECO:0000269|PubMed:30788513, ECO:0000269|PubMed:35294879}.
Interaction partners:
- Glypican-3
Sequence:
MGPPSLVLCLLSATVFSLLGGSSAFLSHHRLKGRFQRDRRNIRPNIILVLTDDQDVELGSMQVMNKTRRIMEQGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNENCSSPSWQAQHESRTFAVYLNSTGYRTAFFGKYLNEYNGSYVPPGWKEWVGLLKNSRFYNYTLCRNGVKEKHGSDYSKDYLTDLITNDSVSFFRTSKKMYPHRPVLMVISHAAPHGPEDSAPQYSRLFPNASQHITPSYNYAPNPDKHWIMRYTGPMKPIHMEFTNMLQRKRLQTLMSVDDSMETIYNMLVETGELDNTYIVYTADHGYHIGQFGLVKGKSMPYEFDIRVPFYVRGPNVEAGCLNPHIVLNIDLAPTILDIAGLDIPADMDGKSILKLLDTERPVNRFHLKKKMRVWRDSFLVERGKLLHKRDNDKVDAQEENFLPKYQRVKDLCQRAEYQTACEQLGQKWQCVEDATGKLKLHKCKGPMRLGGSRALSNLVPKYYGQGSEACTCDSGDYKLSLAGRRKKLFKKKYKASYVRSRSIRSVAIEVDGRVYHVGLGDAAQPRNLTKRHWPGAPEDQDDKDGGDFSGTGGLPDYSAANPIKVTHRCYILENDTVQCDLDLYKSLQAWKDHKLHIDHEIETLQNKIKNLREVRGHLKKKRPEECDCHKISYHTQHKGRLKHRGSSLHPFRKGLQEKDKVWLLREQKRKKKLRKLLKRLQNNDTCSMPGLTCFTHDNQHWQTAPFWTLGPFCACTSANNNTYWCMRTINETHNFLFCEFATGFLEYFDLNTDPYQLMNAVNTLDRDVLNQLHVQLMELRSCKGYKQCNPRTRNMDLGLKDGGSYEQYRQFQRRKWPEMKRPSSKSLGQLWEGWEG
Protein: Holo-[acyl-carrier-protein] synthase (Holo-ACP synthase) (EC 2.7.8.7) (4'-phosphopantetheinyl transferase AcpS) (P0A2W6)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Function: Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00101}.
Interaction partners:
Sequence:
MIVGHGIDIEELASIESAVTRHEGFAKRVLTAQEMERFTSLKGRRQIEYLAGRWSAKEAFSKAMGTGISKLGFQDLEVLNNERGAPYFSQAPFSGKIWLSISHTDQFVTASVILEENHES
Protein: Synaptophysin (BM89 antigen) (Major synaptic vesicle protein p38) (Q62277)
Organism: Mus musculus (Mouse)
Function: Possibly involved in structural functions as organizing other membrane components or in targeting the vesicles to the plasma membrane (By similarity). Involved in the regulation of short-term and long-term synaptic plasticity.
Subcellular location: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:24995978}; Multi-pass membrane protein {ECO:0000255}. Synapse, synaptosome {ECO:0000250|UniProtKB:P08247}.
Interaction partners:
- Vesicle-associated membrane protein 2
- Synapsin-1
- Ras-related protein Rab-3A
- Synaptosomal-associated protein 25
- Synaptic vesicle glycoprotein 2A
- Synaptotagmin-1
- Disks large homolog 4
- Vesicular glutamate transporter 1
- DnaJ homolog subfamily C member 5
- Protein bassoon
Sequence:
MLLLADMDVVNQLVAGGQFRVVKEPLGFVKVLQWVFAIFAFATCGSYTGELRLSVECANKTESALNIEVEFEYPFRLHQVYFDAPSCVKGGTTKIFLVGDYSSSAEFFVTVAVFAFLYSMGALATYIFLQNKYRENNKGPMMDFLATAVFAFMWLVSSSAWAKGLSDVKMATDPENIIKEMPMCRQTGNTCKELRDPVTSGLNTSVVFGFLNLVLWVGNLWFVFKETGWAAPFMRAPPGAPEKQPAPGDAYGDAGYGQGPGGYGPQDSYGPQGGYQPDYGQPASGGGGGYGPQGDYGQQGYGQQGAPTSFSNQM