wanglab/gogpt-training-data huggingface dataset:
Protein: CUE domain-containing protein 4, mitochondrial (P87238)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Ubiquitin-conjugating enzyme E2-18 kDa
- ERAD-associated E3 ubiquitin-protein ligase doa10
- Protein sip5
- General negative regulator of transcription subunit 3
- ERAD-associated E3 ubiquitin-protein ligase hrd1
- Cell differentiation protein rcd1
- Poly
- Uncharacterized derlin-like protein C365.08c
- Putative general negative regulator of transcription C16C9.04c
- CCR4-Not complex 3'-5'-exoribonuclease subunit Ccr4
Sequence:
MQPEQLAGCAVVLTVTVLTLRWMFRVDKGGEVSESRTSSSGVDNEPPVNSEHVHLVKTVFPHLESSAIAYDLQKTKNVDATIENALRGQPLPLPPRNSSLYARFPLSAGAGASSHSEETTPSHEVTSNVSSGSSASSLASNEHRSLIETYNLSSRISSSDNSSSSTGNEEVRNRSKLPSSKKEREELFRKRKEEMILAARKRMEGKIKGEKQDKN
Protein: Mitochondrial pyruvate carrier 4 (O49636)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Mediates the uptake of pyruvate into mitochondria.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P53157}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Mitochondrial pyruvate carrier 1
- Mitochondrial import inner membrane translocase subunit TIM14-2
- Mitochondrial import inner membrane translocase subunit TIM17-2
- Nicotinamide adenine dinucleotide transporter 2, mitochondrial
- GrpE protein homolog 2
- ATP-dependent zinc metalloprotease FTSH 4, mitochondrial
Sequence:
MATSKLQAIWNHPAGPKTIHFWAPTFKWGISIANIADFAKPPEKLSYPQQIAVTCTGVIWSRYSMVINPKNWNLFSVNVAMAGTGIYQLARKIKHDYATEAEPAVASE
Protein: Integrin alpha-V (Vitronectin receptor) (Vitronectin receptor subunit alpha) (CD antigen CD51) [Cleaved into: Integrin alpha-V heavy chain; Integrin alpha-V light chain] (P06756)
Organism: Homo sapiens (Human)
Function: The alpha-V (ITGAV) integrins are receptors for vitronectin, cytotactin, fibronectin, fibrinogen, laminin, matrix metalloproteinase-2, osteopontin, osteomodulin, prothrombin, thrombospondin and vWF. They recognize the sequence R-G-D in a wide array of ligands. ITGAV:ITGB3 binds to fractalkine (CX3CL1) and may act as its coreceptor in CX3CR1-dependent fractalkine signaling. ITGAV:ITGB3 binds to NRG1 (via EGF domain) and this binding is essential for NRG1-ERBB signaling. ITGAV:ITGB3 binds to FGF1 and this binding is essential for FGF1 signaling. ITGAV:ITGB3 binds to FGF2 and this binding is essential for FGF2 signaling. ITGAV:ITGB3 binds to IGF1 and this binding is essential for IGF1 signaling. ITGAV:ITGB3 binds to IGF2 and this binding is essential for IGF2 signaling. ITGAV:ITGB3 binds to IL1B and this binding is essential for IL1B signaling. ITGAV:ITGB3 binds to PLA2G2A via a site (site 2) which is distinct from the classical ligand-binding site (site 1) and this induces integrin conformational changes and enhanced ligand binding to site 1. ITGAV:ITGB3 and ITGAV:ITGB6 act as receptors for fibrillin-1 (FBN1) and mediate R-G-D-dependent cell adhesion to FBN1. Integrin alpha-V/beta-6 or alpha-V/beta-8 (ITGAV:ITGB6 or ITGAV:ITGB8) mediates R-G-D-dependent release of transforming growth factor beta-1 (TGF-beta-1) from regulatory Latency-associated peptide (LAP), thereby playing a key role in TGF-beta-1 activation. ITGAV:ITGB3 acts as a receptor for CD40LG.
Subcellular location: Cell membrane; Single-pass type I membrane protein. Cell junction, focal adhesion {ECO:0000269|PubMed:17158881}.
Interaction partners:
- Vitronectin
- Integrin beta-3
- Integrin beta-6
- Integrin beta-1
- Fibronectin
- Osteopontin
- Integrin beta-8
- Integrin beta-5
- Transforming growth factor beta-1 proprotein
- Integrin beta-2
Sequence:
MAFPPRRRLRLGPRGLPLLLSGLLLPLCRAFNLDVDSPAEYSGPEGSYFGFAVDFFVPSASSRMFLLVGAPKANTTQPGIVEGGQVLKCDWSSTRRCQPIEFDATGNRDYAKDDPLEFKSHQWFGASVRSKQDKILACAPLYHWRTEMKQEREPVGTCFLQDGTKTVEYAPCRSQDIDADGQGFCQGGFSIDFTKADRVLLGGPGSFYWQGQLISDQVAEIVSKYDPNVYSIKYNNQLATRTAQAIFDDSYLGYSVAVGDFNGDGIDDFVSGVPRAARTLGMVYIYDGKNMSSLYNFTGEQMAAYFGFSVAATDINGDDYADVFIGAPLFMDRGSDGKLQEVGQVSVSLQRASGDFQTTKLNGFEVFARFGSAIAPLGDLDQDGFNDIAIAAPYGGEDKKGIVYIFNGRSTGLNAVPSQILEGQWAARSMPPSFGYSMKGATDIDKNGYPDLIVGAFGVDRAILYRARPVITVNAGLEVYPSILNQDNKTCSLPGTALKVSCFNVRFCLKADGKGVLPRKLNFQVELLLDKLKQKGAIRRALFLYSRSPSHSKNMTISRGGLMQCEELIAYLRDESEFRDKLTPITIFMEYRLDYRTAADTTGLQPILNQFTPANISRQAHILLDCGEDNVCKPKLEVSVDSDQKKIYIGDDNPLTLIVKAQNQGEGAYEAELIVSIPLQADFIGVVRNNEALARLSCAFKTENQTRQVVCDLGNPMKAGTQLLAGLRFSVHQQSEMDTSVKFDLQIQSSNLFDKVSPVVSHKVDLAVLAAVEIRGVSSPDHVFLPIPNWEHKENPETEEDVGPVVQHIYELRNNGPSSFSKAMLHLQWPYKYNNNTLLYILHYDIDGPMNCTSDMEINPLRIKISSLQTTEKNDTVAGQGERDHLITKRDLALSEGDIHTLGCGVAQCLKIVCQVGRLDRGKSAILYVKSLLWTETFMNKENQNHSYSLKSSASFNVIEFPYKNLPIEDITNSTLVTTNVTWGIQPAPMPVPVWVIILAVLAGLLLLAVLVFVMYRMGFFKRVRPPQEEQEREQLQPHENGEGNSET
Protein: P-selectin (CD62 antigen-like family member P) (Granule membrane protein 140) (GMP-140) (Leukocyte-endothelial cell adhesion molecule 3) (LECAM3) (Platelet activation dependent granule-external membrane protein) (PADGEM) (CD antigen CD62P) (P98106)
Organism: Rattus norvegicus (Rat)
Function: Ca(2+)-dependent receptor for myeloid cells that binds to carbohydrates on neutrophils and monocytes. Mediates the interaction of activated endothelial cells or platelets with leukocytes. The ligand recognized is sialyl-Lewis X. Mediates rapid rolling of leukocyte rolling over vascular surfaces during the initial steps in inflammation through interaction with SELPLG.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P16109}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P16109}.
Interaction partners:
- Selectin P ligand
- CD44 antigen
- von Willebrand factor
- Signal transducer CD24
- L-selectin
- Golgi apparatus protein 1
- Vascular cell adhesion protein 1
- Tumor necrosis factor receptor superfamily, member 5, isoform CRA_a.
- Intercellular adhesion molecule 1
- Platelet glycoprotein Ib alpha chain
Sequence:
MAGCPKGSWKPRLRSVVLGAAQLIWLSALISELVNRKKVATWTYNYSTKAYSWNNSRAFCKRHFTDLVAIQNKNEIAHLNDVIPYVNSYYWIGIRKINNKWTWVGTNKTLTAEAENWADNEPNNKRNNQDCVEIYIKSNSAPGKWNDEPCFKRKRALCYTASCQDMSCNSQGERIETIGSYTCSCYPGFYGPECEYVQECGKFDIPQHVLMNCSHPLGDFSFSSQCTFSCPEGYDLNGPSEMQCLASGIWTNNPPQCKAVQCQSLEAPLHGTMDCTHPLAAFAYDSSCKFECQPGYRMRGSDILHCTDSGQWSEPLPTCEAIACEPLESPLHGSMDCFPSTGAFGYNSSCTFRCTEGFVLMGNDAIHCADLGQWTAPAPVCEALQCQEFPVPSKAQVSCSDPFGPLKYQSACSFSCDEGSLLVGASVIRCLATGHWSEAPPECQAVSCTPLLSPENGTMTCIQPLGHSNYKSTCQFMCDEGFYLSGPERLDCSPSGHWTGSPPMCEAIKCPEIFAPEQGSLDCSHVHGEFSVGSTCHFSCNEEFELLGSRNVECTVSGRWSAPPPTCKGVTSLPVPSVRCPALTTPGQGTMSCRHHLESFGPNTTCYFGCKTGFTLRGANSLRCGASGQWTAVTPVCRAVKCSELHMDTAVAMNCSNPWGNFSYGSTCAFHCPEGQSLNGSARTTCGEDGHWSDAMPTCQAGTLTIQEALTYLGGALASTSGLAVGGTLLALLRKRLRKKDDGKCPLNPHSHLGTYGVFTNAAYDPTP
Protein: Putative CC-type chemokine U83 (P52461)
Organism: Human herpesvirus 6B (strain Z29) (HHV-6 variant B) (Human B lymphotropic virus)
Interaction partners:
Sequence:
MAIGFIGSSPDAELSSENSRISSSVLLGCLLCCTDWSAVVPGKTETFRKPFVAIMIKKLKSCFAAYLSDLEQGSMCDMANASPTSLELGLSKLDKES
Protein: Group IIE secretory phospholipase A2 (GIIE sPLA2) (sPLA2-IIE) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase 2E) (Q9QUL3)
Organism: Mus musculus (Mouse)
Function: Secretory calcium-dependent phospholipase A2 that primarily targets extracellular phospholipids. Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity), releasing various unsaturated fatty acids including oleoate, linoleoate, arachidonate, docosahexaenoate and lysophosphatidylethanolamines in preference to lysophosphatidylcholines (By similarity). In response to high-fat diet, hydrolyzes minor lipoprotein phospholipids including phosphatidylserines, phosphatidylinositols and phosphatidylglycerols, altering lipoprotein composition and fat storage in adipose tissue and liver. May act in an autocrine and paracrine manner (By similarity). Contributes to lipid remodeling of cellular membranes and generation of lipid mediators involved in pathogen clearance. Cleaves sn-2 fatty acyl chains of phosphatidylglycerols and phosphatidylethanolamines, which are major components of membrane phospholipids in bacteria (By similarity). Acts as a hair follicle phospholipase A2. Selectively releases lysophosphatidylethanolamines (LPE) and various unsaturated fatty acids in skin to regulate hair follicle homeostasis. May regulate the inflammatory response by releasing arachidonate, a precursor of prostaglandins and leukotrienes. Upon allergen exposure, may participate in allergic inflammatory response by enhancing leukotriene C4 synthesis and degranulation in mast cells.
Subcellular location: Secreted {ECO:0000269|PubMed:11922621}. Cytoplasm {ECO:0000269|PubMed:11922621}. Note=Through binding to heparan sulfate proteoglycan, may be localized to cytoplasmic compartments enriched in anionic phospholipids. {ECO:0000250|UniProtKB:Q9NZK7}.
Interaction partners:
- Group 3 secretory phospholipase A2
- Group XIIA secretory phospholipase A2
- Group XIIB secretory phospholipase A2-like protein
- Cytochrome P450 2E1
- Phospholipase A and acyltransferase 3
- Phospholipase A2
- Group 10 secretory phospholipase A2
- Group IIF secretory phospholipase A2
- Group IID secretory phospholipase A2
- Polyunsaturated fatty acid lipoxygenase ALOX8
Sequence:
MKPPIALACLCLLVPLAGGNLVQFGVMIERMTGKPALQYNDYGCYCGVGGSHWPVDETDWCCHAHDCCYGRLEKLGCDPKLEKYLFSITRDNIFCAGRTACQRHTCECDKRAALCFRHNLNTYNRKYAHYPNKLCTGPTPPC
Protein: Glycosylphosphatidylinositol anchor attachment 1 (E9PQ31)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGLLSDPVRRRALARLVLRLNAPLCVLSYVAGIAWFLALVFPPLTQRTYMSENAMGSTMVEEQFAGGDRARAFARDFAAHRKKSGQAVGLLLALAAHFRGQIYWAKDIVFLVTEHDLLGTEAWLEAYHDVNVTGMQSSPLQGRAGAIQAAVALELSSDVVTSLDVAVEGLNGQLPNLDLLNLFQTFCQKGGLLCTLQGKLQPEDWTSLDGPLQGLQTLLLMVLRQASGRPHGSHGLFLRYRVEALTLRGINSFRQYKYDLVAVGKALEGMFRKLNHLLERLHQSFFLYLLPGLSRFVSIGLYMPAVGFLLLVLGLKALELWMQLHEAGMGLEEPGGAPGPSVPLPPSQ
Protein: Suppressor of cytokine signaling 3 (Q7ZUC6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Tyrosine-protein kinase JAK1
- Tyrosine-protein kinase.
- Leptin receptor.
- Tyrosine-protein kinase.
- Tyrosine-protein kinase
- Signal transducer and activator of transcription
- Insulin receptor substrate 1
- Insulin receptor substrate 2
- Tyrosine-protein kinase receptor
- Suppressor of cytokine signaling 3
Sequence:
MITHSKLDNAMSSGLFDASMRLPFYHFKTFSSKVQFQLVQHTIRMLQESGFYWGAISGKEANHLLSSEPSGTFLVRDSSDNRHFFTLSVKTESGTKNLRVQCDNKSFFLQTDSKSMQSVPRFDCVLRLVQHYMPRSALSIGIPRSSYYIYTGGEKIPLELLRPLQCSMSSLQHLCRKTVNGHTDVSSKREHLPQQLKDFLQEYDAPI
Protein: Putative 26S proteasome non-ATPase regulatory subunit 8 homolog B (26S proteasome regulatory subunit RPN12b) (AtRPN12b) (26S proteasome regulatory subunit S14 homolog B) (Q9FHY0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.
Interaction partners:
- 26S proteasome non-ATPase regulatory subunit 11 homolog
- 26S proteasome regulatory subunit 6B homolog
- 26S proteasome non-ATPase regulatory subunit 4 homolog
- 26S proteasome regulatory subunit 7 homolog B
- 26S proteasome regulatory subunit 6A homolog B
- 26S proteasome regulatory subunit RPN13
- 26S proteasome regulatory subunit 6A homolog A
- Proteasome subunit beta type-4
- Proteasome subunit beta type-6
- Putative proteasome subunit alpha type-4-B
Sequence:
MDPQLMEVSQQFERFKAAFIIKDFDTCSSLLSQLKLFDHYLISLSLNALLLLTCALFFLCTRNRIPPSPQENLIMGLNLLRLLVQNRIAEFHTELGLLSSATLENPCIKHAVELEQSFMEGAYNRVLSARQTAPDETYVYFMDLLAKTIRDEIAGCSEKAYDHLSISEGCKMLLFSSDQQLLTYVNEEHPEWEVKDGLVVFQKTRETAPCKEIPSLQLINQTLSYTRELERIL
Protein: Alpha-ketoglutarate-dependent dioxygenase alkB homolog 6 (EC 1.14.11.-) (Alkylated DNA repair protein alkB homolog 6) (Q3KRA9)
Organism: Homo sapiens (Human)
Function: Probable dioxygenase that requires molecular oxygen, alpha-ketoglutarate and iron.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17979886}. Nucleus {ECO:0000269|PubMed:17979886}.
Interaction partners:
- Nucleic acid dioxygenase ALKBH1
- Mediator of RNA polymerase II transcription subunit 29
- Alpha-ketoglutarate-dependent dioxygenase alkB homolog 7, mitochondrial
- 2-oxoglutarate and iron-dependent oxygenase JMJD4
- Alpha-ketoglutarate-dependent dioxygenase alkB homolog 4
- DNA oxidative demethylase ALKBH2
Sequence:
MEEQDARVPALEPFRVEQAPPVIYYVPDFISKEEEEYLLRQVFNAPKPKWTQLSGRKLQNWGGLPHPRGMVPERLPPWLQRYVDKVSNLSLFGGLPANHVLVNQYLPGEGIMPHEDGPLYYPTVSTISLGSHTVLDFYEPRRPEDDDPTEQPRPPPRPTTSLLLEPRSLLVLRGPAYTRLLHGIAAARVDALDAASSPPNAAACPSARPGACLVRGTRVSLTIRRVPRVLRAGLLLGK
Protein: Meiosis 1 arrest protein (Meiosis 1-arresting protein) (Meiosis 1-associated protein) (Spermatogenesis-associated protein 37) (Q8TC57)
Organism: Homo sapiens (Human)
Function: Required for meiosis I progression during spermatogenesis.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- N-acetylglucosamine-6-phosphate deacetylase
- N-acetylglucosamine-6-phosphate deacetylase
Sequence:
MHPGRTTGKGPSTHTQIDQQPPRLLIVHIALPSWADICTNLCEALQNFFSLACSLMGPSRMSLFSLYMVQDQHECILPFVQVKGNFARLQTCISELRMLQREGCFRSQGASLRLAVEDGLQQFKQYSRHVTTRAALTYTSLEITILTSQPGKEVVKQLEEGLKDTDLARVRRFQVVEVTKGILEHVDSASPVEDTSNDESSILGTDIDLQTIDNDIVSMEIFFKAWLHNSGTDQEQIHLLLSSQCFSNISRPRDNPMCLKCDLQERLLCPSLLAGTADGSLRMDDPKGDFITLYQMASQSSASHYKLQVIKALKSSGLCESLTYGLPFILRPTSCWQLDWDELETNQQHFHALCHSLLKREWLLLAKGEPPGPGHSQRIPASTFYVIMPSHSLTLLVKAVATRELMLPSTFPLLPEDPHDDSLKNVESMLDSLELEPTYNPLHVQSHLYSHLSSIYAKPQGRLHPHWESRAPRKHPCKTGQLQTNRARATVAPLPMTPVPGRASKMPAASKSSSDAFFLPSEWEKDPSRP
Protein: GTP-binding protein 4 (Chronic renal failure gene protein) (GTP-binding protein NGB) (Nucleolar GTP-binding protein 1) (Q99ME9)
Organism: Mus musculus (Mouse)
Function: Involved in the biogenesis of the 60S ribosomal subunit. Acts as TP53 repressor, preventing TP53 stabilization and cell cycle arrest.
Subcellular location: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9BZE4}.
Interaction partners:
- Ribosome biogenesis protein NSA2 homolog
- Pescadillo homolog
- Nucleolar GTP-binding protein 2
- mRNA turnover protein 4 homolog
- Ribosome production factor 2 homolog
- Ribosome biogenesis protein NOP53
- MKI67 FHA domain-interacting nucleolar phosphoprotein
- ATP-dependent RNA helicase DDX18
- Ribosome biogenesis protein BRX1 homolog
- Ribosome biogenesis protein WDR12
Sequence:
MAHYNFKKITVVPSAKDFIDLTLSKTQRKTPTVIHKHYQIHRIRHFYMRKVKFTQQNYHDRLSQILSDFPKLDDIHPFYADLMNILYDKDHYKLALGQINIAKNLVDNVAKDYVRLMKYGDSLYRCKQLKRAALGRMCTIIKRQRQSLEYLEQVRQHLSRLPTIDPNTRTLLLCGYPNVGKSSFINKVTRADVDVQPYAFTTKSLFVGHMDYKYLRWQVVDTPGILDHPLEDRNTIEMQAITALAHLRAAVLYVMDLSEQCGHGLKEQLELFQNIRPLFINKPLIVVANKCDVKRIAELSEEDQKIFLDLQAEGFPVIETSTLTEEGVIQVKTEACDRLLAHRVETKMKGNKVNEVLNRLHLAVPNKRDDKERPPFIPEGVIARRKRMEIEEPKKKRERDLELEMGDDYILDLQKYWDLMNSSEKYDKIPEIWEGHNVADYIDPAIMKKLEELEKEEELRTAAGEYDSDSESEDEEMMEIRQLAKQIREKKKLKILQSKEKNKQGPRMPRTAKKVQRADLENEMRSLGVDMDDKNNAHYAVQARRSRSVTRKRKREESVPPSSTARSRSCSRTPRDVSGLRDVKMVKKAKTMMKKAQKKMNRLGKKGEADRHVFDMKPKHLLSGKRKAGKKDRR
Protein: Dynein axonemal intermediate chain 4 (WD repeat-containing protein 78) (F1QHZ6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Plays a critical role in the assembly of axonemal dynein complex (By similarity). Plays a key role in ciliary motility.
Subcellular location: Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:E9PYY5}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:E9PYY5}. Dynein axonemal particle {ECO:0000250|UniProtKB:Q6GPB9}.
Interaction partners:
- Dynein axonemal intermediate chain 3
- Dynein axonemal heavy chain 3.
- Dynein axonemal heavy chain 10
- Dynein light chain Tctex-type 5
- Dynein axonemal heavy chain 2
- Dynein, axonemal, heavy chain 6.
- WD repeat-containing protein 37
- Dynein, axonemal, heavy chain 1.
- Dynein, axonemal, heavy chain 9.
- Radial spoke head protein 9 homolog
Sequence:
MSNTTVTQKRRTLKVAKSSKTLNVSSGVFRPNQSTTKSINPLFSGKSFGSTGDSKVVDKISAQTPKHTAMVVDENGQDVTPHPLYNPDPGVLQSKQGKVFTALDTSLTTMTEFPSIAFQTTNASLTGPFTRSFFGSASASRISQTAESVTDETKDLLVKQDLSNSISDIQSHREEPKEQLRENILDSTANCYLSETETIWLLDIPAVSVSVESEDAEAVKERNNAYTELCKNRQGNDKYVERSMQTFSDASKTKEVQCDSITMVDKAVMCTVWDMYDSFNNISDVSANTVVSSERHEATIPESSSEGHLVHPKRSNQSLSVVSTVSTVSGSSTHIEKMACVLPLDEEPDLQLILQSDKLKQDLALMERVVLANVFQPKLAAYRQLPIIEDPDCVQMVMEEESWTEQSKNSHCPFLERLWDFSCELTMGRNVSCMVWNKKNPDLLAVGYGQVEFKNPNSGLVCCWSLKNPTWPDRVFHCESGVTALDFSASNANQLAVGMYDGTIAIYNVQTSEQTPITDSSDCANLHTSPVWQLTWIDHEDGLAADKGEILVSVSSDGRISKWIHYKSMECVDLMKLKIHDLQWKRHISSLTPGMCFDFHPNDSKIYLVGTEEGHIHKCSSSYNEQYLESYKAHKRPVYKVTWSPFCSDVFLSCSSDWTIQLWRQDLQIPVMGFTSGQRVVFDIMWSPHCATVFGAVSEGKVEIWDLRVSSLDPTLVNWTSPGVNPTALLFSPETDCVLVGDSEGQVTVYKLKNITAGGGSQGETLEDVIQSTLSSQH
Protein: Probable cation-transporting ATPase W08D2.5 (EC 7.2.2.-) (Q27533)
Organism: Caenorhabditis elegans
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Glutathione-independent glyoxalase DJR-1.2
- Leucine-rich repeat serine/threonine-protein kinase 1
- Glutathione-independent glyoxalase DJR-1.1
- E3 ubiquitin-protein ligase parkin
- DnaJ homolog subfamily C member 10
- Vacuolar protein sorting-associated protein 35
- MAM domain-containing protein
Sequence:
MTLESGDHTLTLFAYRTGPFRTILFYALTVLTLGIFRLILHWKQKWDVKMRMVPCTFEAAEYIYIIDNHNVSELQPVLRKSNATIPTENGEMRKVPELRWFVYRKLEYVWIDDLNSDESVDEISDNDNCWKTSFEIANRIPCRSLLAVSESNFGLTLSEISRRLEFYGRNEIVVQLRPILYLLVMEVITPFYVFQIFSVTVWYNDEYAYYASLIVILSLGSIVMDVYQIRTQEIRLRSMVHSTESVEVIREGTEMTIGSDQLVPGDILLIPPHGCLMQCDSVLMNGTVIVNESVLTGESVPITKVALTDETNDSVFNIEKNSKNVLFCGTQVLQTRFYRGKKVKAIVLRTAYSTLKGQLVRSIMYPKPVDFRFTKDLFKFILFLACISGCGFIYTIIVMIMRGNTLRRIIVRSLDIITITVPPALPAAMSVGIINAQLRLKKKEIFCISPSTINTCGAINVVCFDKTGTLTEDGLDFHVVRPVMSAVNQEIQKVKLEKSNRTEFMGEMTELTSRNGLPFDGDLVKAIATCHSLTRINGVLHGDPLDLILFQKTGWTMEEGIEGDIEEETQRFDNVQPSIIKPTDDKSAEYSVIRQFTFSSSLQRMSVIVFDPREDRPDNMMLYSKGSPEMILSLCDPNTVPEDYLLQVNSYAQHGFRLIAVARRPLDLNFNKASKVKRDAVECDLEMLGLIVMENRVKPVTLGVINQLNRANIRTVMVTGDNLLTGLSVARECGIIRPSKRAFLVEHVPGELDEYGRTKIFVKQSVSSSDEVIEDDASVSISMCSSTWKGSSEGDGFSPTNTEVETPNPVTADSLGHLIASSYHLAISGPTFAVIVHEYPELVDQLCSVCDVFARMAPDQKQSLVEQLQQIDYTVAMCGDGANDCAALKAAHAGISLSDAEASIAAPFTSKVPDIRCVPTVISEGRAALVTSFGIFKYMAGYSLTQFVTVMHLYWISNILTDGQFMYIDMFLITMFALLFGNTPAFYRLAHTPPPTRLLSIASMTSVVGQLIIIGVVQFIVFFSTSQQPWFTPYQPPVDDEVEDKRSMQGTALFCVSMFQYIILALVYSKGPPFRGNLWSNKPMCALTIFATLLCLFIVIWPTELVLKTLGNVELPSLTFRIFIVIVGAVNAAVSYGFETLFVDFFLLGYWERYKKKRSIEAIIDYVPTTNSDHIRRPSINGVTSSRTESTLLSAEGQQLHMTTSKNGKGGENPHSSALFERLISRIGGEPTWLTNPIPPHSLSEPEEPEKLERTY
Protein: Cytochrome c oxidase subunit 4 (Q9VIQ8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004434, ECO:0000256|RuleBase:RU367145}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004434, ECO:0000256|RuleBase:RU367145}.
Interaction partners:
- Cytochrome c oxidase subunit 7C, mitochondrial
- Cyclope, isoform A
- Cytochrome c oxidase subunit 5B, isoform A
- Cytochrome c oxidase subunit
- Levy, isoform A
- Cytochrome c oxidase subunit 5A, mitochondrial
- AT02348p
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome b-c1 complex subunit 8
- NADH dehydrogenase 1 alpha subcomplex subunit 9, mitochondrial
Sequence:
MALRLLNSAVLRQLASQLPKSAQVGSVAAVHTLDKIGKREIVGYGWNGTACYADRVDYPLPAVRFREPTNEINALRAKEQGDWKKLSTQEIKALYRASFCQTIAEVQAGSGEWKLHLGVSLLFCAAAIWVAVLMNIFVYDELPVTFDEEHQKAQLQRIIDLEINPVTGLTSKWDYENKKWKN
Protein: RAN binding protein 9 (F1LVV3)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- GID complex subunit 8 homolog
- RAN binding protein 10
- Muskelin
- WD repeat-containing protein 26
- RCG33430, isoform CRA_a.
- Neural cell adhesion molecule L1
- Required for meiotic nuclear division 5 homolog A
- Armadillo repeat-containing protein 8
- E3 ubiquitin-protein transferase MAEA
- Probable ATP-dependent RNA helicase DDX4
Sequence:
MGELNWIPGHGKTPKDAASVRATHPIPAACGIYYFEVKIVSKGRDGYMGIGLSAQGVNMNRLPGWDKHSYGYHGDDGHSFCSSGTGQPYGPTFTTGDVIGCCVNLINNTCFYTKNGHSLGIAFTDLPPNLYPTVGLQTPGEVVDANFGQHPFVFDIEDYMREWRTKIQAQIDRFPIGDREGEWQTMIQKMVSSYLVHHGYCATAEAFARSTDQTVLEELASIKNRQRIQKLVLAGRMGEAIETTQQLYPSLLERNPNLLFTLKVRQFIEMVNGTDSEVRCLGGRSPKSQDSYPVSPRPFSSPSMSPSHGMSIHSLAPGKGSTAHFPGFESCSNGVISNKAHQSYCHSKHQLSSLNVPELNSINVSRSQQVNNFTSNDVDMETDHYSNGVGETSSNGFLNGSSKHDHEMEDCDTEMEVDCSQLRRQLCGGSQAAIERMIHFGRELQAMSEQLRRECGKNTANKKMLKDAFSLLAYSDPWNSPVGNQLDPIQREPVCSALNSAILETHNLPKQPPLALAMGQATQCLGLMARAGVGSCAFATVEDYLH
Protein: Claudin-11 (Q99P82)
Organism: Rattus norvegicus (Rat)
Function: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity.
Subcellular location: Cell junction, tight junction. Cell membrane {ECO:0000250|UniProtKB:O75508}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Tight junction protein ZO-1
- Occludin
- Tight junction protein 3
- Claudin
- Claudin-3
- Claudin
- Claudin
- Claudin
- Claudin-1
- Claudin-5
Sequence:
MVATCLQVVGFVTSFVGWIGIIVTTSTNDWVVTCSYTIPTCRKMDELGSKGLWADCVMATGLHHCKPLVDILILPGYAQACRALMIAASVLGLPGILLLLTVLPCIRMGHEPGVAKYRRAQLAGVLLILLALCAIVATIWFPVCAHREITIVSFGYSLYAGWIGAVMCLVGGCVIVCCSGDAQSFGENRFYYSSGSSSPTHAKSAHV
Protein: Paraflagellar rod component (Q580G8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- ODAD1 central coiled coil region domain-containing protein
Sequence:
MSATYPERRPYATTVPHSGYLSKPTLPPVEALRILSSTVGIDLPRSVRHSANTLLRRSPTPRSVSPTRGVQLFKPPTLETATPFEFQEKDYHKSQQSVLNVQLSNAVEELFKVWRVKVRDLMHYLDSFPCEAGHSFSRTNGALSSFFEGYRTTDITPMTAHQLVNDFKLCTSVSMLDEIQNSPEVLGDQVRAALDALLNAKHFLAPLENFVDRLEPIAAFALPDKRPECLDGTRGPVWPSKVAVALHEKFHYDPSEYVLAELRKSDQPIERLENRVLQVKERKEDAIDREIPGDALNYLTTQVDLSNDLLLMNKARMELVYLHGKDIQEMKRMLEDLIVDARHSVELLKGRVERDMPLVKKDIDGVYQDVENTQKHIKDLDQKNAEANKAAHEAYSKLNDTEVELWVLLTDTIRKLVDIAGEKEAFVRNEMRLRELRGRDMAIAEELLAAQQSYFSRLRKSEDVLKRWENAAETYEAYVQAYVPTLLKKIHDAEEADKDLYNREAQNYVRRYEMFEYAVEEGRATRSVHVDRLQTLQRSKLLDVERALSTLDPFADKYRKELDEAQAQLDEGLAFIQLVENLAKERRGEVEPILQHVISYNRTLQTKTLEIEAEAEAQALLLRDGPATEGAPSTMNTVDAKVDTSLLQSARGSSGKRPATAAVSEVTHFCDAPPTSAALRLRSVVDANNMMCTVSHPHVMARTVGINHEEAFLEKYRRFTDEEQVAVEGVAGRVRQSNTSLEMLGEKYNNKDYIRMLLLSPGAKQSNSATEAAVEECA
Protein: Translation termination factor SUP35 (Q6Q7I0)
Organism: Saccharomyces cerevisiae (Baker's yeast)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
NNQQNYQQYSQNGNQQQGNNRYQGYQAYNAQAQPAGGYYQNYQGYSGYQQGGYQQYNPDAGYQQQYNPQGGYQQYNPQGGYQQQFNPQGGRGNYKNFNYNNNLQGYQAGFQPQSQGMSLNDFQKQQKQAAPKPKKTLKLVSSSGIKLANATKKVGTKPAESDKKEEEKSAETKEPTKEPTKVEEPVKKEEKPVQTEEKTEEKSELPKVEDLKISESTHNTNNANVTSADALIKEQEEEVDDEVVNDMFGGKDHVSLIFMGHVDAGKSTMGGNLLYLTGSVDKRTIEKYEREAKDAGRQGWYLSWVMDTNKEERNDGKTIEVGKAYFETEKRRYTILDAPGHKMYVSEMIGGASQADVGVLVISARKGEYETGFERGGQTREHALLAKTQGVNKMVVVVNKMDDPTVNWSKERYDQCVSNVSNFLRAIGYNIKTDV
Protein: Spermidine/putrescine-binding periplasmic protein (SPBP) (P0AFK9)
Organism: Escherichia coli (strain K12)
Function: Required for the activity of the bacterial periplasmic transport system of putrescine and spermidine. Polyamine binding protein.
Subcellular location: Periplasm {ECO:0000269|PubMed:1939142}.
Interaction partners:
- Spermidine/putrescine import ATP-binding protein PotA
- Spermidine/putrescine transport system permease protein PotB
- Spermidine/putrescine transport system permease protein PotC
- Putrescine transport system permease protein PotI
- Inner membrane ABC transporter permease protein YdcV
- Putrescine transport system permease protein PotH
- Inner membrane ABC transporter permease protein YdcU
- Putrescine transport ATP-binding protein PotG
- Uncharacterized ABC transporter ATP-binding protein YdcT
Sequence:
MKKWSRHLLAAGALALGMSAAHADDNNTLYFYNWTEYVPPGLLEQFTKETGIKVIYSTYESNETMYAKLKTYKDGAYDLVVPSTYYVDKMRKEGMIQKIDKSKLTNFSNLDPDMLNKPFDPNNDYSIPYIWGATAIGVNGDAVDPKSVTSWADLWKPEYKGSLLLTDDAREVFQMALRKLGYSGNTTDPKEIEAAYNELKKLMPNVAAFNSDNPANPYMEGEVNLGMIWNGSAFVARQAGTPIDVVWPKEGGIFWMDSLAIPANAKNKEGALKLINFLLRPDVAKQVAETIGYPTPNLAARKLLSPEVANDKTLYPDAETIKNGEWQNDVGAASSIYEEYYQKLKAGR