wanglab/gogpt-training-data huggingface dataset:
Protein: t-SNARE domain containing 1 (A0AVG3)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MSYGSIARGGGLGSRGPFGGPSRQGCQPLECARCWTEYGIRHFPCPSPESKLQNRCVGKDGEGDLGPAGTPIVPRARKRGPGVAPEGSRMPEPTSSPTIGPRKDSAAGPHGRMAGPSTTRAKKRKPNFCPQETEVLVSKVSKHHQLLFGTGLLKAEPTRRYRVWSRILQAVNALGYCRRDVVDLKHKWRDLRAVVRRKLGDLRKAAHGPSPGSGKPQALALTPVEQVVAKTFSCQALPSEGFSLEPPRATQVDPCNLQELFQEMSANVFRINSSVTSLERSLQSLGTPSDTQELRDSLHTAQQETNKTIAASASSVKQMAELLRSSCPQERLQQERPQLDRLKTQLSDAIQCYGVVQKKIAEKSRALLPMAQRGSKQQSPQAPFAELADDEKVFNGSDNMWQGQEQALLPDITEEDLEAIRLREEAILQMESNLLDVNQIIKDLASMVSEQGEAVDSIEASLEAASSHAEAARQLLAGASRHQLQRHKIKCCFLSAGVTALLVIIIIIATSVRK
Protein: E3 ubiquitin-protein ligase Os06g0535400 (EC 2.3.2.27) (RING-H2 finger protein Os06g0535400) (RING-type E3 ubiquitin transferase Os06g0535400) (Q5Z5F2)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Possesses E3 ubiquitin-protein ligase in vitro.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MELPWLDLPFTLLTLLLATRLAYDYYGVVAATFTGSFSLQIFLFYCFARWYRHTIAARAAADADGDGGGGAVADEEAAPPVLIPLLEGRGGGGGGAGAASSLANRCFAVVFMVFVPLVIVVFERSQADVVAYALCLANILVMVVWLSPDAAADPASAAKSFLRLSDDEDEGSCSGSGHGAAEDKCCVCLAGMREAQALRDLPRCGHRFHAKCIGKWLTAHPTCPVCRTTAVPPPAPLPASGDHADDAITPV
Protein: Adenylate kinase (EC 2.7.4.3) (ATP-AMP transphosphorylase) (ATP:AMP phosphotransferase) (Adenylate kinase cytosolic and mitochondrial) (Adenylate monophosphate kinase) (Q5B2V8)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. Adenylate kinase activity is critical for regulation of the phosphate utilization and the AMP de novo biosynthesis pathways.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:2040420}. Mitochondrion intermembrane space {ECO:0000255|HAMAP-Rule:MF_03168, ECO:0000269|PubMed:2040420}.
Interaction partners:
- adenine phosphoribosyltransferase
- Adenosine kinase
- Ribonucleoside-diphosphate reductase
- Nucleoside diphosphate kinase
- Ribonucleotide reductase
- Adenylosuccinate lyase
- AMP deaminase
- Adenylate kinase isoenzyme 6 homolog
- Phosphodiesterase
- Pyruvate kinase
Sequence:
MAPITDDVVAGLKSTIGKLEARIEDLESRLGGEPKPKSIAEHMRIILMGPPGAGKGTQAPKIKEKYCVCHLATGDMLRSQVAKKTDLGREAKKIMDQGGLVSDEIMVNMIKSELENNAECKNGFILDGFPRTVAQAERLDEMLVARNQKLQHAIELKIDDALLVARITGRLVHPASGRSYHKIFNPPKEAMKDDITGEPLVQRSDDNAEALKKRLVTYHAQTAPVCDYYKKTGIWRGIDASQEPGQVWKSLLGVFNNKN
Protein: Transcription factor sox9a (SRY-box transcription factor 9a) (Transcription factor SOX-9a) (Q9DFH2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Runt-related transcription factor.
- Col2a1a protein
- Aromatase
- Homeobox protein Dlx2a
- Anti-Mullerian hormone
- Doublesex- and mab-3-related transcription factor 1
- RUNX family transcription factor 2b.
- Forkhead box protein L2
Sequence:
MNLLDPYLKMTDEQEKCLSDAPSPSMSEDSAGSPCPSASGSDTENTRPAENSLLAADGTLGDFKKDEEDKFPVCIREAVSQVLKGYDWTLVPMPVRVNGSSKNKPHVKRPMNAFMVWAQAARRKLADQYPHLHNAELSKTLGKLWRLLNEVEKRPFVEEAERLRVQHKKDHPDYKYQPRRRKSVKNGQSESEDGSEQTHISPNAIFKALQQADSPASSMGEVHSPSEHSGQSQGPPTPPTTPKTDTQPGKADLKREARPLQENTGRPLSINFQDVDIGELSSDVIETFDVNEFDQYLPPNGHQNAPYAGGYAAWMTKPQNGSPQSSQLTPLNPAEPDQPRTTHIKTEQLSPSHYNEQQGSPQHISYGSFNVQHLQHYSTSFPSITRAQYDYSDSHQGGASSYYTHAGGQSSGLYSTFSYMSSSQRPMYTPIADSTGVPSIPQSNHSPQHWDQQPVYTQLSRP
Protein: Universal minicircle sequence binding protein (UMSBP), putative (Q38B00)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MADEASTAKRHRAEGGNNCHRCGQPGHFARECPNVPPGAMGDRACYTCGQPDHLSRDCPSNRGPAPMGGGRACYNCGQPGHFSRECPNMRGGPMGGAPMGGGRACYNCGQPGHFSRECPNMRGGPMGGAPMGGGRACYNCGQPGHFSRECPNMRGGNMGGGRACYHCQQEGHIARECPNAPADAAAGGAAAGGGRACYNCGQPGHLSRACPVK
Protein: FAST kinase domain-containing protein 4 (Protein TBRG4) (Transforming growth factor beta regulator 4) (Q91YM4)
Organism: Mus musculus (Mouse)
Function: Plays a role in processing of mitochondrial RNA precursors and in stabilization of a subset of mature mitochondrial RNA species, such as MT-CO1, MT-CO2, MT-CYB, MT-CO3, MT-ND3, MT-ND5 and MT-ATP8/6. May play a role in cell cycle progression.
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:Q969Z0}.
Interaction partners:
Sequence:
MAVRLMKRCTCLLREATRLVPTVAPVGRLRLAGVSCKTLTSSVSSPSSGSLAELLGKEQVFTPYPEHQELDFLIEKASRPEQLLELLGSDHSLHHNHAALILIRLSYLLSEKPKEKALLAEDARFQRLVKLVDSQITCVWHGTLVKLLRSLYTLVLPQISKELQSVEQEVRWRLRRLKYKHLVFLAESCASFMKEQHSQELLAELLMHLERRWTEINDSRTLVTMMTMAGHLSESLMNHLEDKCLELVEQFGPDELRKVLVTLAAQSRRSVPLLRAISYHLVQKPFPMTKGMLLDLAYAYGKLSFHQTQVSQRLAADLLPFIPSMTPGEVARCAKSFAFLKWLNLPLFEAFTQHLLSRVQDVSLSHVCSVLLAFARLNFHPEQEEDQFFSMVHEKLDPVLGSLEPALQVDLVWALCVLQHVHETELHTVLHPGLHARFLESKSPKDQSTFQKLVHINTTALLEHPEYKGPFLPASAVAPIPSPSNKKMTPLQKELQETLKALLGNTDKGSLEVATQYGWVLDAEVLLDADGHFLPLRNFVAPHLAQPVGNQPLPPGAKRIAFLRWEFPNFNSRSKDLLGRFVLARRHVLAAGFLVVDVPYYEWLDLKSEWQKSAYLKDKMRKAMAEELAK
Protein: Cardioactive peptide (Cardioacceleratory peptide 2a) (Crustacean cardioactive peptide) (CCAP) (Q8WRC7)
Organism: Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm)
Function: Cardioregulatory neurohormone that increases heart beat rate during adult wing inflation; has no effect on beat amplitude. The effect of CCAP is both ino- and chronotropic.
Subcellular location: Secreted {ECO:0000269|PubMed:3925062}.
Interaction partners:
Sequence:
MTVSRVCLLLLVALVYLDCCYAASIPRNFDPRLSEEIVMAPKKRPFCNAFTGCGRKRSQGPPGMPAQDLRTKQYLDEEALGSILDSESAIDELSRQILSEAKLWEAIQEASAEIARRKQKEAYIQ
Protein: Myocyte-specific enhancer factor 2A (Q60929)
Organism: Mus musculus (Mouse)
Function: Transcriptional activator which binds specifically to the MEF2 element, 5'-YTA[AT](4)TAR-3', found in numerous muscle-specific genes. Also involved in the activation of numerous growth factor- and stress-induced genes. Mediates cellular functions not only in skeletal and cardiac muscle development, but also in neuronal differentiation and survival. Plays diverse roles in the control of cell growth, survival and apoptosis via p38 MAPK signaling in muscle-specific and/or growth factor-related transcription. In cerebellar granule neurons, phosphorylated and sumoylated MEF2A represses transcription of NUR77 promoting synaptic differentiation. Associates with chromatin to the ZNF16 promoter (By similarity).
Subcellular location: Nucleus.
Interaction partners:
- Homeobox protein Nkx-2.5
- Mitogen-activated protein kinase 14
- Myocyte-specific enhancer factor 2D
- Myocyte-specific enhancer factor 2C
- Nuclear factor of activated T-cells, cytoplasmic 4
- Nuclear factor of activated T-cells, cytoplasmic 3
- Nuclear factor of activated T-cells, cytoplasmic 1
- Nuclear factor of activated T-cells, cytoplasmic 2
- Histone acetyltransferase p300
- Histone deacetylase 4
Sequence:
MGRKKIQITRIMDERNRQVTFTKRKFGLMKKAYELSVLCDCEIALIIFNSSNKLFQYASTDMDKVLLKYTEYNEPHESRTNSDIVETLRKKGLNGCESPDADDYFEHSPLSEDRFSKLNEDSDFIFKRGPPGLPPQNFSMSVTVPVTSPNALSYTNPGSSLVSPSLAASSTLADSSMLSPPPATLHRNVSPGAPQRPPSTGSASGMLSTTDLTVPNGAGNSPVGNGFVNSRASPNLIGNTGANSLGKVMPTKSPPPPGGGSLGMNSRKPDLRVVIPPSSKGMMPPLSEEEELELNAQRISSSQATQPLATPVVSVTTPSLPPQGLVYSAMPTAYNTDYSLTSADLSALQGFTSPGMLSLGQASAWQQHHLGQAALSSLVAGGQLSQGSNLSINTNQNINIKSEPISPPRDRMTPSGFQQQQQQPQQQPPPQPPQPQPRQEMGRSPVDSLSSSSSSYDGSDREDPRGDFHSPIVLGRPPNTEDRESPSVKRMRMDTWVT
Protein: F-box/WD-40 repeat-containing protein At3g52030 (Q9SV01)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MGRTETGDESSARKMRRKVPTSIESLDADILCIIFSFLDLFDLVHCTVVCNSWNAVIKRLKLLQASCRKMHHLGSDSPSSSTSLDRPAEIDVEDFAMKHHKMALLRGRIEIERWEAHSHRVSQCRMKKGLLLTGVGDKVMRLWSLKSYKCMEEYSLPDASSLIDFDFDESKKLEVVSLAWEYFDSVVVVVVEIVGLVGTRISIWRRNGQRSIFPSRAGTFPKGLCMRYIDPEAVVGCEDGTARVFDMYSKTCSQIIRTQGGPITCLSLSDNQLFLSGSSLGRVTVSDPLMDQPVATLKSTITAGGIQTICFNQGTNLAFIGTTGGYVSCWDLRKMDRLWEKRVSPNVVYSIQQLRNDTSVMVAGGIDGVLRMIDQKSGRVLSRVIMDDKFSTTSTRNNQVVIEKRRGKRVSQDMEIDKIERKVRPQISCIAMGMKKMVTAHNGKCISVWKFNLS
Protein: GLIPR1-like protein 1 (Q9DAG6)
Organism: Mus musculus (Mouse)
Function: Required for optimal fertilization at the stage of sperm-oocyte fusion, plays a role in optimizing acrosome function, the translocation of IZUMO1 during the acrosome reaction and the fertilization process. Component of epididymosomes, one type of membranous microvesicules which mediate the transfer of lipids and proteins to spermatozoa plasma membrane during epididymal maturation. Also component of the CD9-positive microvesicules found in the cauda region.
Subcellular location: Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:20219979, ECO:0000269|PubMed:31672133}. Cell membrane {ECO:0000305|PubMed:20219979}; Peripheral membrane protein {ECO:0000305|PubMed:20219979}; Extracellular side {ECO:0000305|PubMed:20219979}. Membrane raft {ECO:0000269|PubMed:31672133}. Secreted {ECO:0000269|PubMed:20219979}. Note=Located in the connecting piece of elongated spermatids and sperm (PubMed:20219979, PubMed:31672133). Also located in the apical region of the sperm head after sperm capacitation (PubMed:20219979, PubMed:31672133). Weakly attached to the cell membrane and later secreted into the extracellular space (PubMed:20219979). Located on sperm equatorial segment and neck (By similarity). Associated with epididymosomes from the caput and cauda epididymis (By similarity). {ECO:0000250|UniProtKB:Q32LB5, ECO:0000269|PubMed:20219979, ECO:0000269|PubMed:31672133}.
Interaction partners:
Sequence:
MALKKKLNFLWTLVLYLIASRLPKAFGKDLPRVPTITDPKFIDAFLNIHNELRRKVQPPAADMNQLFWDQQLAKLAKAWTRECKLAHNPCIKQRYECLEDYDFIGENIYLGRIETQPEDVVINWYNESKYFNFDFNTCSEMCGHYTQVVWAKTVKIGCAVSNCPNLKGFSAGLFVCNYSPAGNFIGFRPYTRGDSCSMCGQKTCENSLCRPMNRKTPHHKAACHVLVLGFILQSLL
Protein: Epstein-Barr nuclear antigen 4 (EBNA-4) (EBV nuclear antigen 4) (Epstein-Barr nuclear antigen 3B) (EBNA-3B) (EBV nuclear antigen 3B) (P03203)
Organism: Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
Function: May be involved in transcriptional regulation of both viral and cellular genes by interacting with the host DNA-binding protein RBPJ.
Subcellular location: Host nucleus {ECO:0000269|PubMed:2161150}.
Interaction partners:
Sequence:
MKKAWLSRAQQADAGGASGSEDPPDYGDQGNVTQVGSEPISPEIGPFELSAASEDDPQSGPVEENLDAAAREEEEPHEQEHNGGDDPLDVHTRQPRFVDVNPTQAPVIQLVHAVYDSMLQSDLRPLGSLFLEQNLNIEEFIWMCMTVRHRCQAIRKKPLPIVKQRRWKLLSSCRSWRMGYRTHNLKVNSFESGGDNVHPVLVTATLGCDEGTRHATTYSAGIVQIPRISDQNQKIETAFLMARRARSLSAERYTLFFDLVSSGNTLYAIWIGLGTKNRVSFIEFVGWLCKKDHTHIREWFRQCTGRPKAAKPWLRAHPVAIPYDDPLTNEEIDLAYARGQAMNIEAPRLPDDPIIVEDDDESEEIEAESDEEEDKSGMESLKNIPQTLPYNPTVYGRPAVFDRKSDAKSTKKCRAIVTDFSVIKAIEEEHRKKKAARTEQPRATPESQAPTVVLQRPPTQQEPGPVGPLSVQARLEPWQPLPGPQVTAVLLHEESMQGVQVHGSMLDLLEKDDEVMEQRVMATLLPPVPQQPRAGRRGPCVFTGDLGIESDEPASTEPVHDQLLPAPGPDPLEIQPLTSPTTSQLSSSAPSCAQTPWPVVQPSQTPDDPTKQSRPPETAAPRQWPMPLRPIPMRPLRMQPIPFNHPVGPTPHQTPQVEITPYKPTWAQIGHIPYQPTPTGPATMLLRQWAPATMQTPPRAPTPMSPPEVPPVPRQRPRGAPTPTPPPQVPPVPRQRPRGAPTPTPPPQVLPTPMQLALRAPAGQQGPTKQILRQLLTGGVKKGRPSLKLQAALERQAAAGWQPSPGSGTSDKIVQAPIFYPPVLQPIQVMGQGGSPTAMAASAVTQAPTEYTRERRGVGPMPPTDIPPSKRAKIEAYTEPEMPHGGASHSPVVILENVGQGQQQTLECGGTAKQERDMLGLGDIAVSSPSSSETSNDE
Protein: Keratin 83 (A0A8I6AFC7)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MTCGFQTGNFGCASACGPRPGRCCITAAPYRGISCYRGLSGGFGSRSVCGAFRSGSCGRSFGYRSGGVCGPSPPCITTVSVNESLLTPLNLEIDPNAQCVKHEEKEQIKCLNSRFAAFIDKVRFLEQQNKLLETKWQFFQNRKCCESNVEPLFEGYIETLRREAECVEADSGRLAAELNHAQEAMEGYKKRYEEEVALRATAENEFVALKKDVDCAYLRKSDLEANAEALTQEIDFLRRLYEEETRILHAHISDTSVIVKMDNSRDLNMDCVIAEIKAQYDDIASRSRAEAESWYRTKCEEIKATVIRHGETLRRTREEINELNRIIQRLTAEIENAKCQNTKLEAAVTQSEQQGEAALTDARCKLAELEAALQKAKQDMACLLKEYQEVMNSKLGLDIEIATYRRLLEGEEQRTDPAFVLTGVSSSRGGVVCGDLCVSGSRPVTGSVCSAPCSGNVAVSTGLCAPCGSGPCHQGRRCAFLWWACNVT
Protein: Myelin and lymphocyte protein (T-lymphocyte maturation-associated protein) (VIP17 proteolipid) (Q28296)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Function: Could be an important component in vesicular trafficking cycling between the Golgi complex and the apical plasma membrane. Could be involved in myelin biogenesis and/or myelin function.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Myelin associated oligodendrocyte basic protein.
Sequence:
MAPAAASGGSSLPSGFSVFTTFPDLLFIFEFIFGGLVWILIASSLVPIPLVQGWVMFVSVFCFMATTALLVLYIIGAHGGENSWVTLDAAYHCIAALFYLSASVLEALATIGMQEGYTYKQYHENISAVVFSYVATLLYVVHAVFSLIRWKSS
Protein: 2-methoxy-6-polyprenyl-1,4-benzoquinol methylase, mitochondrial (EC 2.1.1.201) (Ubiquinone biosynthesis methyltransferase COQ5) (Q5HYK3)
Organism: Homo sapiens (Human)
Function: Methyltransferase required for the conversion of 2-polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2).
Subcellular location: Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03191, ECO:0000269|PubMed:25152161, ECO:0000269|PubMed:27499296, ECO:0000269|PubMed:35614220}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03191, ECO:0000269|PubMed:25152161}; Matrix side {ECO:0000255|HAMAP-Rule:MF_03191, ECO:0000269|PubMed:25152161}.
Interaction partners:
- NADPH-dependent 3-demethoxyubiquinone 3-hydroxylase, mitochondrial
- Ubiquinone biosynthesis monooxygenase COQ6, mitochondrial
- Ubiquinone biosynthesis O-methyltransferase, mitochondrial
- Ubiquinone biosynthesis protein COQ9
- Ubiquinone biosynthesis protein COQ4 homolog, mitochondrial
- Atypical kinase COQ8A, mitochondrial
- Atypical kinase COQ8B, mitochondrial
- All trans-polyprenyl-diphosphate synthase PDSS1
- 4-hydroxybenzoate polyprenyltransferase, mitochondrial
- All trans-polyprenyl-diphosphate synthase PDSS2
Sequence:
MAAPGSCALWSYCGRGWSRAMRGCQLLGLRSSWPGDLLSARLLSQEKRAAETHFGFETVSEEEKGGKVYQVFESVAKKYDVMNDMMSLGIHRVWKDLLLWKMHPLPGTQLLDVAGGTGDIAFRFLNYVQSQHQRKQKRQLRAQQNLSWEEIAKEYQNEEDSLGGSRVVVCDINKEMLKVGKQKALAQGYRAGLAWVLGDAEELPFDDDKFDIYTIAFGIRNVTHIDQALQEAHRVLKPGGRFLCLEFSQVNNPLISRLYDLYSFQVIPVLGEVIAGDWKSYQYLVESIRRFPSQEEFKDMIEDAGFHKVTYESLTSGIVAIHSGFKL
Protein: Trigger factor (TF) (EC 5.2.1.8) (PPIase) (C4ZTJ3)
Organism: Escherichia coli (strain K12 / MC4100 / BW2952)
Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Subcellular location: Cytoplasm. Note=About half TF is bound to the ribosome near the polypeptide exit tunnel while the other half is free in the cytoplasm. {ECO:0000255|HAMAP-Rule:MF_00303}.
Interaction partners:
Sequence:
MQVSVETTQGLGRRVTITIAADSIETAVKSELVNVAKKVRIDGFRKGKVPMNIVAQRYGASVRQDVLGDLMSRNFIDAIIKEKINPAGAPTYVPGEYKLGEDFTYSVEFEVYPEVELQGLEAIEVEKPIVEVTDADVDGMLDTLRKQQATWKEKDGAVEAEDRVTIDFTGSVDGEEFEGGKASDFVLAMGQGRMIPGFEDGIKGHKAGEEFTIDVTFPEEYHAENLKGKAAKFAINLKKVEERELPELTAEFIKRFGVEDGSVEGLRAEVRKNMERELKSAIRNRVKSQAIEGLVKANDIDVPAALIDSEIDVLRRQAAQRFGGNEKQALELPRELFEEQAKRRVVVGLLLGEVIRTNELKADEERVKGLIEEMASAYEDPKEVIEFYSKNKELMDNMRNVALEEQAVEAVLAKAKVTEKETTFNELMNQQA
Protein: Aminoglycoside 2'-N-acetyltransferase (EC 2.3.1.-) (AAC(2')-Ic) (P9WQG9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: May catalyze the coenzyme A-dependent acetylation of the 2' hydroxyl or amino group of a broad spectrum of aminoglycosides and confer resistance to aminoglycosides (By similarity). In vitro assays show no significant increase of resistance to aminoglycosides, possibly due to low expression in a heterologous system.
Interaction partners:
- Carboxyltransferase domain-containing protein
- Carboxyltransferase domain-containing protein
- Proline-rich antigen homolog
- Bifunctional AAC/APH
- Probable periplasmic iron-transport lipoprotein
Sequence:
MHTQVHTARLVHTADLDSETRQDIRQMVTGAFAGDFTETDWEHTLGGMHALIWHHGAIIAHAAVIQRRLIYRGNALRCGYVEGVAVRADWRGQRLVSALLDAVEQVMRGAYQLGALSSSARARRLYASRGWLPWHGPTSVLAPTGPVRTPDDDGTVFVLPIDISLDTSAELMCDWRAGDVW
Protein: 32 kDa beta-galactoside-binding lectin lec-3 (32 kDa GBP) (Q09581)
Organism: Caenorhabditis elegans
Function: Binds galactose.
Interaction partners:
- N-acyl-aliphatic-L-amino acid amidohydrolase
- DUF1080 domain-containing protein
- RRM domain-containing protein
- RRM domain-containing protein
- Galectin
Sequence:
MAEPKSFNIPYRSKLTERIEPGQTLIIRGKTIDESKRFNINLHKDSPDFSGNDVPLHLSIRFDEGKIVYNAYTKGTWGKEERAKNPIKKGDDFDIRIRAHDSKFQVSINHKEVKNFEHRIPLNSVSHLSIDGDVVLNHVQWGGKYYPVPYESGIAADGLVPGKTLVVYGTPEKKAKKFNINLLKKNGDIALHFNPRFDEKANGFMCAKPTPGSVVRNSLVNGEWGNEEREGKNPFERLTAFDLEIRNEEFAFQIFVNGERFASYAHRVDPHDIAGLQIQGDIELTGIQVVNNQPAQE
Protein: C3H1-type domain-containing protein (Q38DY2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MIFPSAAEPQPTQPFFLAAPMMYNPLPPTPPQTSPVVPQCVYMWAAVPVPPVVRPLMMPNNNLSTTVLLLGTSGDGYTKEASVEPAAGNSKVSPSSLCRHHLRSRCNRRNCRFSHGEDPNEWVAK
Protein: Acyl-protein thioesterase 1 (APT-1) (EC 3.1.2.-) (Lysophospholipase 1) (Lysophospholipase I) (LPL-I) (LysoPLA I) (Palmitoyl-protein hydrolase) (EC 3.1.2.22) (P70470)
Organism: Rattus norvegicus (Rat)
Function: Acts as a acyl-protein thioesterase hydrolyzing fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins or HRAS. Has depalmitoylating activity toward KCNMA1 (By similarity). Could also depalmitoylate ADRB2 (By similarity). Acts as a lysophospholipase hydrolyzing various lysophospholipids including lysophosphatidylcholine (lyso-PC), lysophosphatidylethanolamine (lyso-PE), lysophosphatidylinositol (lyso-PI) and lysophosphatidylserine (lyso-PS). Has much higher thioesterase activity than lysophospholipase activity (By similarity). Contributes to the production of lysophosphatidic acid (LPA) during blood coagulation by recognizing and cleaving plasma phospholipids to generate lysophospholipids which in turn act as substrates for ENPP2 to produce LPA (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9624183}. Cell membrane {ECO:0000250|UniProtKB:O75608}. Nucleus membrane {ECO:0000250|UniProtKB:O75608}. Endoplasmic reticulum {ECO:0000250|UniProtKB:O75608}. Note=Shows predominantly a cytoplasmic localization with a weak expression in the cell membrane, nuclear membrane and endoplasmic reticulum. {ECO:0000250|UniProtKB:O75608}.
Interaction partners:
- Glycerophosphocholine phosphodiesterase GPCPD1
- Lysosomal phospholipase A and acyltransferase
- Lysophospholipid acyltransferase 5
- Phospholipase B1, membrane-associated
- Phosphatidylcholine-sterol acyltransferase
- lysophospholipase
- Lysophosphatidylcholine acyltransferase 4
- Membrane-bound glycerophospholipid O-acyltransferase 2
- Patatin-like phospholipase domain-containing protein 7
- Membrane bound O-acyltransferase domain containing 1
Sequence:
MCGNNMSAPMPAVVPAARKATAAVIFLHGLGDTGHGWAEAFAGIKSSHIKYICPHAPVMPVTLNMSMMMPSWFDIIGLSPDSQEDESGIKQAAETVKALIDQEVKNGIPSNRIILGGFSQGGALSLYTALTTQQKLAGVTALSCWLPLRASFSQGPINSANRDISVLQCHGDCDPLVPLMFGSLTVERLKGLVNPANVTFKVYEGMMHSSCQQEMMDVKYFIDKLLPPID
Protein: Auxin canalization protein (DUF828) (Q8VY20)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- ADP-ribosylation factor GTPase-activating protein AGD7
Sequence:
MEKLMVPTWRPDPVYRPPETPLEPMEFLARSWSVSALEVSKALTPPNPQILLSKTEEEEEEEPISSVVDGDGDTEDTGLVTGNPFSFACSETSQMVMDRILSHSQEVSPRTSGRLSHSSGPLNGSLTDSPPVSPPESDDIKQFCRANKNSLNSVNSQFRSTAATPGPITATATQSKTVGRWLKDRREKKKEETRAHNAQIHAAVSVAGVAAAVAAIAAATAASSSCGKDEQMAKTDMAVASAATLVAAQCVEAAEVMGAEREYLASVVSSAVNVRSAGDIMTLTAGAATALRGVQTLKARAMKEVWNIASVIPMDKGLTSTGGSSNNVNGSNGSSSSSHSGELVQQENFLGTCSREWLARGCELLKRTRKGDLHWKIVSVYINKMNQVMLKMKSRHVGGTFTKKKKNIVLDVIKNVPAWPGRHLLEGGDDLRYFGLKTVMRGDVEFEVKSQREYEMWTQGVSRLLVLAAERKFRM
Protein: Ribonuclease H2 subunit B (Ribonuclease HI subunit B) (A0A2R8Y687)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGLSSCYCPEYLKDASKKMKNGLMFVKLVNPCSGEGAIYLFNMCLQQLFEVKVFKEKHHSWFINQSVQSGGLLHFATPVDPLFLLLHYLIKADKEGKFQPLDQVVVDNVFPNCILLLKLPGLEKLLHHVTEEKGNPEIDNKKYYKYSKEKTLKWLEKKVNQTVAALKTNNVNVSSRVQSTAFFSGDQASTDKEEDYIRYAHGLISDYIPKELSDDLSKYLKLPEPSASLPNPPSKKIKLSDEPVEAKEDYTKFNTKDLKTEKVYQLVIL
Protein: DNA replication licensing factor MCM3 (EC 3.6.4.12) (Q5ZMN2)
Organism: Gallus gallus (Chicken)
Function: Acts as component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. Core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and around which the replisome is built. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. Required for the entry in S phase and for cell division.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P25205}. Chromosome {ECO:0000250|UniProtKB:P25205}. Note=Associated with chromatin before the formation of nuclei and detaches from it as DNA replication progresses. {ECO:0000250|UniProtKB:P25205}.
Interaction partners:
- DNA helicase
- Cell division cycle 45.
- Cell division control protein
- DNA replication licensing factor MCM6
- Chromatin licensing and DNA replication factor 1.
- DNA replication licensing factor MCM5
- DNA replication licensing factor MCM4
- Uncharacterized protein.
- Cell division cycle 7.
- DNA replication complex GINS protein PSF1
Sequence:
MAAPAGGLGDAELREAQRDYLDFLDDEEDQGVYHGKVRDMISDNQYRLLVNINDLRRRNEKRANRLLSNAFEELIAFQRALKDFVASVDATYAKQYEDFYIGLEGSFGSKHVSPRTLTACFLSCIVCVEGIVTKCSLIRPKVVRSVHYCPATKKTIERRYTDLTSLDAFPSSTVYPTKDEENNPLETEYGLSVYKDHQTISIQEMPEKAPAGQLPRSVDVILDDDLVDKVKPGDRIQVVGTYRCLPGKKGGYTSGTFRTILIACHIKQMSKDARPLYSANDVAKIKRFSKSRSKDIFNQLARSLAPSIHGHEFIKKALLCMLLGGVEKVLENGSRIRGDINILLIGDPSVAKSQLLRYVLGTAPRAVGTTGRGSSGVGLTAAVTTDQETGERRLEAGAMVLADRGVVCIDEFDKMSDIDRTAIHEVMEQGRVTIAKAGIHARLNSRCSVLAAANPVYGRYDQYKTPMENIGLQDSLLSRFDLLFIMLDQMDSEQDREISDHVLRMHRYRNPNEQDGDAMPLGSAVEILATDDPDFAQEEEQELQVYEKHDDLLHGPNRRKEKIVSMEFMRKYIHVAKMIKPVLTQESADYIAEEYSSLRSQNQMNSDIARTSPVTARTLETLIRLSTAHAKARMSKTVDLQDAEAALELVQFAYFKKVLEKEKKRKKQVEDDSETEKEEEEEETQPEKEGRKQRRKKARTEGEEESYDPYDFSDAEQEMPEVQAHTPKTPESSATGEAKKPELADPRLKAFKAALLEVFKSSHAQSVGLKNVMESINRDNPEPFSLAGVKVALAHMQDDNQIMVSDDIIFLI
Protein: Btk-PH-domain binding protein (Myeloid/lymphoid or mixed-lineage leukemia (Trithorax homolog, Drosophila) translocated to, 1) (Myeloid/lymphoid or mixed-lineage leukemia; translocated to, 1) (Q9ERL0)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00376}.
Interaction partners:
- AF4/FMR2 family member 4
- AF4/FMR2 family member 1
- RNA polymerase II elongation factor ELL
- RNA polymerase II elongation factor ELL2
- Protein AF-9
- Cyclin-dependent kinase 9
- Cyclin-T1
- Histone-lysine N-methyltransferase, H3 lysine-79 specific
- ELL-associated factor 1
- RNA polymerase II elongation factor ELL3
Sequence:
MDNQCTVQVKLELGHRAQLRKKPTTEGFTHDWMVFVRGPEQCDIQHFVEKVIFRLHDSFPKPKRVCKEPPYKVEESGYAGFIMLIEVYFKNKEEPRKVCFTYDLFLNLEGNPPVNHLRCEKLTFNNPTTEFRCKLLMAGGVMVMPEGADTVSRPSPDYPMLPTIPLSAFSDPKKNKPSHGSKDANKESGKASKPHKVAREHRERPRKDSESRSCSKEPEREPKSAKDAARKLPKEEKAPVPKAAFKEPKMALKETKLESLSPKGVPQPPTLPKASSKRPAATDSPKLSAKKPKKSGSKGTRRAPGTSPRASSFPDKKVARDKNSKGDKGKAESEPREAKRTLQTEDSNSEDEASFRSESAQSSPANASSSSDSSSDSDFEPSQNHSQGPLRSMVEDLQSEGSDEDDSSSGEENTGKANPGRESRLSFSDSESDNSADSCLPGREPLPPQKPPPPSSKVSGRRSPEPCSKPEKMLKKATYDKAYTDELVELHRRLMALRERNVLQQIVNLIEETGHFNVTNTTFDFDLFSLDESTVRKLQSCLEAVAT
Protein: Protein HEATR9 (HEAT repeat-containing protein 9) (A2RTY3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAYEKSTDISDVSRSMFLYPWLEYPDKTKELRKAMAPVHLPLSCYQMPKEEFPPSPECWRQHPSKPNSVPYCYFKKPEIYTHWHDLYDQREEREAEKMLRKMRDDCRYIKEVHQTHIKMFHLPMSKLTIKSEMRSRPLEPTQDPLKWQRLRELTKSLESPREDEQFYAAQALGCLRISDKFVMEALQQVAQTGPEKVKYEAYRTLAILGCLNKHVIRALIKQLKEKNEGQRMETLTGLRMALNSWAAVSKDKRTQVGDEGKLVPVLQTLIKKSSSEASLEAALCLGFLRPCSNMVQEFLLQCLCQGLKTQRMKALRMLVKVMHVHSAPVIKAILDQLCSSSVLEDRFEATQMLKTIGLEQIQAQGLEELTFNLLRRKTHNEPFLAVRQAVAQTVEELKLKPTMMNLVEAQLMNPDATARQEAVISLGVLGIRSPQVFHLLLDLLDAENHQAVKKSLQETLILCASIDPWIQNKLKNKVLSVYEAPKTNVKAEPTRFQKEPENPEELTIQDFRLAKLNPLFIAKSITKVGQKKTPAFPPCCSKPRKHRPQVIGPWQPRIKKQLRVLAEIAK