wanglab/gogpt-training-data huggingface dataset:
Protein: Protein expanded (Q07436)
Organism: Drosophila melanogaster (Fruit fly)
Function: Activates the Hippo/SWH (Sav/Wts/Hpo) signaling pathway, a signaling pathway that plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein Hippo (Hpo), in complex with its regulatory protein Salvador (Sav), phosphorylates and activates Warts (Wts) in complex with its regulatory protein Mats, which in turn phosphorylates and inactivates the Yorkie (Yki) oncoprotein. Ex acts synergistically along with Mer and Kibra to regulate the Hippo signaling pathway. Involved in the control of cell proliferation in imaginal disks. May bind to certain proteins of signal transduction pathways by interaction with their SH3 domains. Required for apical localization of Schip1.
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:20159598}. Note=Apical surface of disk cells.
Interaction partners:
- Transcriptional coactivator yorkie
- Latrophilin Cirl
- Protein kibra
- Serine/threonine-protein kinase hippo
- Moesin/ezrin/radixin homolog 2
- Cadherin-related tumor suppressor
- Protein crumbs
- Serine/threonine-protein kinase Warts
- Supernumerary limbs, isoform B
- G protein beta subunit 5
Sequence:
MRAFCTVSAPLEVCASSAEQLSPGSRFLALRLLGQQQPKTLYFLVDAKSRVREVYTQTCLHFATQGMLDTELFGLAVLIDGEYMFADPESKLSKYGPKSWRSSHTHGLDANGRPLLELHFRVQFYIESPFMLKDETSRHNYYLQLRHNILQRDLPREQAEQALVFLAGLALQADLGDAPPGTSNSKDDSGEETSASPSNGGRGLSATTTLPKISKRANERMLRLSTYVASTSKRETIPLPPSLPPNGADYYRIEDYLPSGLHTPWARSAMRACHREHLGMATAEAELLYIQQACSLHETINAHTYRMRLAKSEQGSGSAWFVVYAKGIKILGGESTNSSSNPETTTFLWPNITKLSFERKKFEIRSGESRITLYAASDEKNKLLLTLCKDTHQWSMKLAARLKEVSKREEEEAAESQRLHASYACSRSLLLPYKSKNEQRISVISSTSSNTTSGIVSDRVHSEDELEIMINTPPAPLAAPSTESLALAHLLDRPSVSRQTSSVGQMSLKDLEEQLAALSVRPQDASSNGATIVTNSSVQRNSMGTTANDSSTATDSPSSQHNIGSQCSSTCSTVVVTSPVNGAGASSSGAPIPVHSTSSSLELGFSHTAQNSALSETSPDDFLSTSAREETESVSGASGVYTLAHGAPPTETSGVYTMHSSELTGQSSEIAESEKSSHYGMFQPQKLEETHVQHSDSVDGKKKEDFRPRSDSNVSTGSSFRGDGSDPTDNKHSLLSAEELTNLIVGRGTYPSRKTVSSSLHSDCDYVTLPLGDQGEEEVDQPPAPPPPYSARHEKTGLCGPPIAKPIPKPIAVVAPKPDSPPCSPPVPPAPIPAPPPAIRRRDPPPYSISSKPRPTSLISVSSSAHPAPSAAGSMSSLKSEEVTARFITTRPQISILKAHTSLIPDGAKPSYAAPHHCSSVASSNGSVCSHQLSQQSLHNSNYAGGSQASLHHHHVPSHHRHSGSAAIGIVPYGLHKSTASLHHQQSCVLLPVIKPRQFLAPPPPSLPRQPPPPPPPNHPHLASHLYEREMARKQLELYQQQLYSDVDYVIYPIQDPAVSQQEYLDAKQGSLLAAMAQAAPPPPHHPYLAMQVSPAIYRSTPYLPLTLSTHSRYASTQNLSDTYVQLPGPGYSPLYSPSMASLCSSYEPPPPPPLHPAALAAAAAAGAGSSSSSMFARSRSDDNILNSLDLLPKGKRLPPPPPPPYVNRRLKKPPMPAPSEKPPPIPSKPIPSRMSPIPPRKPPTLNPHHANSPLTKTSSGAQWAGERPRPDLGLGLGLNRGNNSILAQLQASMVAQSHAQAQAQALDIALLREKSKHLDLPLISALCNDRSLLKQTKVVINPKTGQEMPTSSAQPSGATTNGVANSSAGAGTLSKARKGSTVSHRHPQDKLPPLPVQQLAEANNYVIDPAVMMKQQQQQQQHNKTS
Protein: Trace amine-associated receptor 14d (U3JB35)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MNLTAVNQTDMCEDYSCPERSVSLSVYVILYVAAAAVALLTVCGNLLVIISVSHFKQLHTPANILILSLAASDFLTGVFVIPLHLSLVIESCWTSGSVMCLVLKVVDFQATSVSVHTVSLIAVDRFLALSFPFFYSEKISLTVVCTATLLNWLFSFIYNFTLLYVNGNFTDVVCPAVCFAITDEISSIIDLLIVFVMPCTLIIILYTHVFVIAKKHATAIRALQVHNSTESSKNKISDKSERKAAMLLGILVFVFLLCLLPYYITALAIPYNSENTLQIRDVAGIFFFLNSTINPIIYALFYSWFQKSIKLIFTFKVFHKDSSLMNVM
Protein: Inactive protein-tyrosine phosphatase egg-5 (Egg sterile protein 5) (Protein-tyrosine phosphatase-like protein egg-5) (O61789)
Organism: Caenorhabditis elegans
Function: Inactive phosphatase which acts redundantly with egg-4 in the oocyte-to-zygote transition. Required for polarized cortical actin cytoskeleton rearrangement in the oocyte before and after fertilization. Together with egg-4, required for the cortical localization of kinase mbk-2 in maturing oocyte until the end of meiosis I. Also required for kinase mbk-2, pseudophosphatase egg-3 and chitin synthase chs-1 localization to cytoplasmic foci after fertilization.
Subcellular location: Cytoplasm, cell cortex {ECO:0000269|PubMed:19879147}. Note=Localizes to the cell cortex in developing oocytes and in newly fertilized embryos. {ECO:0000269|PubMed:19879147}.
Interaction partners:
- Pumilio domain-containing protein 7
- Chitin-binding domain protein cbd-1
- EGF-like domain-containing protein
- glutamine synthetase
- PUM-HD domain-containing protein
- Inactive protein-tyrosine phosphatase egg-4
- LDL receptor repeat-containing protein egg-1
- CCCH-type zinc finger protein oma-2
- Chondroitin proteoglycan 1
- Embryonic mRna
Sequence:
MALNSEVMFREQINAMRSQAGRKRATSLQSFCSGNTDDSSADSTDNMDMMVDYPQQKGVSCMRARFNSESTLSKSFRKKVKKLAQKDRRSKERLNGNSEEDAIEVPRGAPSTYAAPSKLRKSKALDCLVSEKPKDEGRSEDSGHGADIEMAKGHFNDVRMKVFAARTAMQVEPALVMKTRKALEMKNAVLENHQSPGAFSLHAAYKIAASAESRVGSITPCNKKVTKEAMANLIRSSYDDTEITQELLFSSKFDSKWKGRYTDIYMRRDENGKKPKRPVNGQGWVMPLKSICEKFGINSTFFTNHRIDLKSARDQVLLMRLLSHDQTSTWISDIHPEAVKNETLAEYLLRELDASTMQKRVQAFKANVLADRDRVRVAGQFYNNIRIGKRMFGAARKAKYLSTIIGGMERRFEILENSVNHIPFTHSASDNNQEKCRNPRVHCRDSTRIALQFPRGQYLGDFIHANRISGKPLFNEFIMTQAPMKNTVDDFWRMVWQEEVPYIVMLTSRKEPERCEYYWPKSPSDPAVTVPGGLRIENFGVYQAPDPLFRVTHLRLIGPDREERHVEHWQGDVNNSSNMYSPLNILRLLRNASKPVVIHDHLGVSRAACLVAAEIAICSLLRGPTYKYPVQRAVQFLRQRRPFSIETPMQYIFVHRLVAFFFRDVIGSAKELDVDYERWLQERSERMFLDDLAAPIPGYRLLSPRADPDIVRMVGRPERPNYRREAPDCVGEMPNKVAAVDGILSPAKSVFEF
Protein: Merozoite surface protein P92 (Q8ID66)
Organism: Plasmodium falciparum (isolate 3D7)
Function: During the asexual blood stage, recruits host complement factor H CFH to the surface of merozoites resulting in the down-regulation of the host complement alternative pathway and thus, protecting merozoites from complement-mediated lysis.
Subcellular location: Cell surface {ECO:0000269|PubMed:16203726}. Cell membrane {ECO:0000269|PubMed:16203726}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:16203726}. Note=Present on the surface of merozoite. {ECO:0000269|PubMed:16203726}.
Interaction partners:
- Merozoite surface protein P38
- Merozoite surface protein 9
- Merozoite surface protein P12
- Merozoite surface protein P41
Sequence:
MFAVNLKICIFLSLVSFLLQCKNTLANVTFEQKVQTNLSHDKNGDIVYGHREFKGGIYAFLGYDNCTIEVNKTVNGIDWNEKKDVKVSGNNNIAVVYSIFTSEEKMILIFKCDNKFYITKYGKEFKWSDPKVIDVSNVIGTNTTPAVYSGSLLSMNNDFEKYILVCENHSQNYINVVDQEYMREIRLLGKCMLSFDEGNNWKNEVMNLYSDEGYTKINTLRLSDYGGKILVKGTNAQNLNQTIRSIILLCSNLHDWKLFCGLPTIRFRKDISVENLTYLNTYHLAIVKNEDKLQLAFTYDLFETFDPQYLNTEFNGVSHYFVLAPDEMVYLFYHGNEKKNYVIKIKTVPRKIGCELNTNDTVNKIYTYTYKYIYNNKLSAKTCKVPSSHLKYSSDGLYKLFEVRLPKDIKVTENCFRYSFLSDLNNKYHTTIIKTRVINKLEDYVEVQFHFPIYYTKFLYNYKSTYCVLSNNYRIVVEFDYIRNHIDLDFPFDTDTVKLYSNESVTHAFRNNTEKTHVHKFPKGTYMTSYFSYEKEYVISNYIEEPFSTTFTILTQTQMNVHFMAGGQKYKYEGIDLTDSSPNYELSLNSLSDSQNVDIFVSKFDNNKTIGFVCPVKSSYDGLNCFDNVYIKNKTLVKIEYLFGENDIFVVPQRRIYKTEGTAMESLLYLNNNNVKKLIDDKSIIHFYCECNVNNNVIKVNYYISPFYDENSIKQEINKKDQEITMINKTIPQDEKDILFNNEKVVPLSNEPQEIIQPPIQEKLNTTDPSKAYIYGANIIFIAIISIISLSISSFI
Protein: Inner kinetochore subunit mal2 (CENP-O homolog) (Constitutive centromere-associated network protein mal2) (Sim4 complex subunit mal2) (Q10290)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the kinetochore, a multiprotein complex that assembles on centromeric DNA and attaches chromosomes to spindle microtubules, mediating chromosome segregation and sister chromatid segregation during meiosis and mitosis. Component of the inner kinetochore COMA complex, which connects centromere-associated proteins and the outer kinetochore. COMA interacts with other inner kinetochore proteins to form the inner kinetochore constitutive centromere-associated network (CCAN), which serves as a structural platform for outer kinetochore assembly.
Subcellular location: Nucleus. Chromosome, centromere, kinetochore. Chromosome, centromere.
Interaction partners:
- Inner kinetochore subunit mis15
- Inner kinetochore subunit mis6
- Inner kinetochore subunit fta1
- Kinetochore protein mis13
- Inner kinetochore subunit mis17
- Inner kinetochore subunit fta2
- Inner kinetochore subunit fta7
- Inner kinetochore subunit cnl2
- Inner kinetochore subunit fta4
- Kinetochore protein mis14
Sequence:
MDDEEGNATLIDEISVLEARRDVLLDELKSLDNATLSDLVQKPELSKNLSVNNEFLKETPLNQPALHYDRLSGISFFQPNDPEELSRKTLLVKNKKTGAIETAPSIPLLGVRFDIMLNPVNIGFTNLSENPISSASGMDEELEGGNRFDVPYYIIFRVFHDSFALYKYTIPSFLNIQEWADEYLTGKNPERFRIFLWKVDKLLTAYICRKNALLQINKSLTIDGTNISANLSCTHLVIQIPKVIQATLVCSSESTRVVKSRIYQYSDENWKRDHRLELSLLDNKRWVNILVSHLTAPESHASL
Protein: Cyclin-A2-4 (G2/mitotic-specific cyclin-A2-4) (CycA2;4) (Q9C968)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Cyclin-dependent kinase B2-1
- Cyclin-dependent kinase B1-2
- Cyclin-dependent kinase B1-1
- Cyclin-dependent kinase B2-2
- Cyclin-dependent kinase A-1
- Cell division control protein 6 homolog
- Wee1-like protein kinase
- Cyclin-dependent kinases regulatory subunit 1
- Cyclin-dependent kinases regulatory subunit 2
- Origin of replication complex subunit 2
Sequence:
MGKENAVSGNSIPIHGRPVTRALASALRASSKLITSSEVAATTQNQGRVLRAKSKRTALDEKKANAPKKRAVLKDITNVTCENSYTSCFSVAVENIKQIKKGRQSSSSSKVASSSATSQVTDAKVEVVSNSAGASLSVFTDTSLGTNETSYSIIAKPSSRSPPRPFGTVERSCGGASSPKFVDIDSDDKDPLLCSLYAPDIYYNLRVAELKRRPFPDFMEKTQRDVTETMRGILVDWLVEVSEEYTLVPDTLYLTVYLIDWFLHGNYVERQRLQLLGITCMLIASKYEEIHAPRIEEFCFITDNTYTRDQVLEMESQVLKHFSFQIYTPTSKTFLRRFLRAAQVSFPNQSLEMEFLANYLTELTLMDYPFLKFLPSIIAASAVFLAKWTLNQSSHPWNPTLEHYTTYKASDLKASVHALQDLQLNTKGCSLNSIRMKYRQDKFKSVAVFSSGELPDKLFIS
Protein: DNA-directed RNA polymerases I and III subunit RPAC2 (RNA polymerases I and III subunit AC2) (AC19) (DNA-directed RNA polymerase I subunit D) (RNA polymerase I and III subunit D) (Q9VIZ0)
Organism: Drosophila melanogaster (Fruit fly)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common core component of RNA polymerases I and III which synthesize ribosomal RNA precursors and small RNAs, such as 5S rRNA and tRNAs, respectively (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- DNA-directed RNA polymerase I subunit RPA1
- RNA polymerase I subunit F
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
- DNA-directed RNA polymerases I, II, and III subunit RPABC2
- DNA-directed RNA polymerases I, II, and III subunit RPABC5
- DNA-directed RNA polymerase subunit
- DNA-directed RNA polymerases I and III subunit RPAC1
- DNA-directed RNA polymerases I, II, and III subunit RPABC4
- DNA-directed RNA polymerase II subunit RPB3
Sequence:
MGALAELAGDEKNGEGSRTFVFTNEGHTLGNALKTIIARYPEVDFCGYTIPHPTEQKLHFRIQSRRDRAIDILKRGLEDLEGLCDHTIVTFEKEMAEFNAMKVEN
Protein: ditrans,polycis-polyprenyl diphosphate synthase [(2E,6E)-farnesyldiphosphate specific] (EC 2.5.1.87) (Q8H0V2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004586}.
Interaction partners:
Sequence:
MDSNQSMRLLSAWIGQIGDLGLNLLWRFIHIVVSLWYIVSGIFEAIESYAITLGLNKKYGSIDLEKLRCLAVVVDIEAAQDVANVVELLQWLTTIGVKQVGLFDSQGLLKKSKDLILETVPGSMLLEEIEKDVAPDGKRIALEFISSSDNKEAVMKAANILLQRYLKSSHPEDDKGEDFFTESHLNDALRVVGENVHVPDLLLVYGPIRSHLGFPAWRLRYTEIVHMGTLKYMRYGSLLKAIHKFTGVHQNYGT
Protein: RGS domain-containing protein (H2KYQ7)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MAGSNSSAMSLDTTDFDFTSTIPSTPSSFDDFFLIPTPAKTSRRRFTVAPSDIIRLKRRLVQHRPNRGPISRTLSYLRSKMDLALSTSSLYPSRDDVRQWEISFESLLNNKFGCALFRQFLKKEFSDENMDFWLECEEFKKMKDGKKSTTQKAIEIYSEFVAEHSPKEVNLDSDTRAATKAAVEAGCKPDTFALAQSRVEQLMSKDSYRRFLRDRLFLDLLESYEITDKEDKPSSSKDKN
Protein: DNA-binding protein Fis (P57902)
Organism: Pasteurella multocida (strain Pm70)
Function: Activates ribosomal RNA transcription. Plays a direct role in upstream activation of rRNA promoters.
Interaction partners:
- tRNA-dihydrouridine synthase B
- cAMP-activated global transcriptional regulator CRP
- RNA-binding protein Hfq
Sequence:
MLEQQRNPADALTVSVLNSQSQVTNKPLRDSVKQALRNYLSQLDGQDVNELYELVLAEVEHPMLDMVMQYTRGNQTRAATMLGINRGTLRKKLKKYGMG
Protein: Actin-related protein 2/3 complex subunit 1 (Arp2/3 complex 41 kDa subunit) (p41-ARC) (P78774)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Functions as component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks.
Subcellular location: Cytoplasm, cytoskeleton, actin patch.
Interaction partners:
- Actin-related protein 2/3 complex subunit 2
- Actin-related protein 2/3 complex subunit 3
- Actin-related protein 2/3 complex subunit 5
- Actin-related protein 3
- Actin-related protein 2/3 complex subunit 4
- Actin-related protein 2
- Actin
- Actin-binding protein wsp1
- Structure-specific endonuclease subunit slx4
- Protein dip1
Sequence:
MATSQVLHILPKPSYEHAFNSQRTEFVTTTATNQVELYEQDGNGWKHARTFSDHDKIVTCVDWAPKSNRIVTCSQDRNAYVYEKRPDGTWKQTLVLLRLNRAATFVRWSPNEDKFAVGSGARVISVCYFEQENDWWVSKHLKRPLRSTILSLDWHPNNVLLAAGCADRKAYVLSAYVRDVDAKPEASVWGSRLPFNTVCAEYPSGGWVHAVGFSPSGNALAYAGHDSSVTIAYPSAPEQPPRALITVKLSQLPLRSLLWANESAIVAAGYNYSPILLQGNESGWAHTRDLDAGTSKTSFTHTGNTGEGREEEGPVSFTALRSTFRNMDLKGSSQSISSLPTVHQNMIATLRPYAGTPGNITAFTSSGTDGRVVLWTL
Protein: Chemokine-like factor (Q9JK79)
Organism: Rattus norvegicus (Rat)
Function: May play an important role in inflammation and regeneration of skeletal muscle (By similarity). Essential for embryonic development (By similarity).
Subcellular location: [Isoform CKLF1]: Secreted {ECO:0000250|UniProtKB:Q9UBR5}.; SUBCELLULAR LOCATION: [Isoform CKLF2]: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- CKLF-like MARVEL transmembrane domain containing 6
- CKLF-like MARVEL transmembrane domain containing 4
- Similar to chemokine-like factor super family 7, isoform CRA_a.
- CKLF-like MARVEL transmembrane domain containing 3
- CKLF-like MARVEL transmembrane domain containing 8
- CKLF-like MARVEL transmembrane domain containing 5
Sequence:
MDSPQKVVDHQPFCLSLKCFVKTLRLVVTVASMIFFIVAQAPEPYIVITGFEVTIILFLIALYMCSLDKTMRSFFWPLLDVINSVVTTLFMLIVSVSALIPETSTMIMVGGVFGFLTVICTVADCALMCQKLRFRPHGPYQNRSATDVDDS
Protein: Elongation factor 1-alpha-B/C (EF-1-alpha-B/C) (P0CT55)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
Subcellular location: Cytoplasm.
Interaction partners:
- Elongation factor 1-gamma
- Elongation factor 1-beta
- Eukaryotic translation initiation factor 5A-1
- Elongation factor 3
- Adenylyl-sulfate kinase
- Elongation factor 1-alpha-A
- Eukaryotic peptide chain release factor subunit 1
- Elongation factor 1-alpha-B
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein uS3
Sequence:
MGKEKGHINVVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEATELGKGSFKYAWVLDKLKAERERGITIDIALWKFETPKYNVTVIDAPGHRDFIKNMITGTSQADCAILIIGGGTGEFEAGISKDGQTREHALLAYTLGVKQLIVAVNKMDTTGWSQARFEEIVKETSNFIKKVGFNPKTVPFVPVSGFQGDNMIEPTTNMPWYQGWQKETKAGVVKGKTLLEAIDSIEPPARPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKPGMIVTFAPAGVTTEVKSVEMHHESLDAGLPGDNVGFNVKNVSVKDIRRGNVCGDSKNDPPMGCASFTAQVIILNHPGQISAGYSPVLDCHTAHIACKFAELIEKIDRRSGKKIEESPKFVKSGDACIAKMVPSKPMCVEAFTDYAPLGRFAVRDMRQTVAVGVIKAVEKVAPGAAKVTKAAVKAGAKK
Protein: Sugar transport protein 8 (Hexose transporter 8) (Q9SBA7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Mediates an active uptake of hexoses, probably by sugar/hydrogen symport.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- TRM32-like protein
- Transducin/WD40 repeat-like superfamily protein
- Germin-like protein subfamily 2 member 3
- Major facilitator superfamily protein
- At2g34355
- Protein DETOXIFICATION 22
- Major facilitator superfamily protein
Sequence:
MAVVISSNGNSKSFDAKMTVYVFICVIIAAVGGLIFGYDIGISGGVTAMDDFLKEFFPSVYERKKHAHENNYCKYDNQFLQLFTSSLYLAALVASFFASATCSKLGRRPTMQLASIFFLIGVGLAAGAVNIYMLIIGRILLGFGVGFGNQAVPLFLSEIAPARLRGGLNIVFQLMVTIGILIANIVNYFTSSIHPYGWRIALGGAGIPALILLFGSLLICETPTSLIERNKTKEGKETLKKIRGVEDVDEEYESIVHACDIARQVKDPYTKLMKPASRPPFVIGMLLQFFQQFTGINAIMFYAPVLFQTVGFGNDAALLSAVVTGTINVLSTFVGIFLVDKTGRRFLLLQSSVHMLICQLVIGIILAKDLDVTGTLARPQALVVVIFVCVYVMGFAWSWGPLGWLIPSETFPLETRTEGFALAVSCNMFFTFVIAQAFLSMLCAMKSGIFFFFSGWIVVMGLFALFFVPETKGVSIDDMRDSVWKLHWYWKRFMLEEDEHDVEKRTD
Protein: Claudin-17 (P56750)
Organism: Homo sapiens (Human)
Function: Channel-forming tight junction protein with selectivity for anions, including chloride and bicarbonate, and for solutes smaller than 9 Angstrom in diameter. In the kidney proximal tubule, may be involved in quantitative reabsorption of filtered anions. Does not affect water permeability.
Subcellular location: Cell junction, tight junction {ECO:0000269|PubMed:22402829, ECO:0000269|PubMed:26194246}. Basolateral cell membrane {ECO:0000269|PubMed:20375010}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Claudin-12
- Claudin-16
- Claudin-25
- Claudin-34
- Tight junction protein ZO-3
- Occludin
- Tight junction protein 1
- Claudin-24
- Claudin-11
- Claudin-23
Sequence:
MAFYPLQIAGLVLGFLGMVGTLATTLLPQWRVSAFVGSNIIVFERLWEGLWMNCIRQARVRLQCKFYSSLLALPPALETARALMCVAVALSLIALLIGICGMKQVQCTGSNERAKAYLLGTSGVLFILTGIFVLIPVSWTANIIIRDFYNPAIHIGQKRELGAALFLGWASAAVLFIGGGLLCGFCCCNRKKQGYRYPVPGYRVPHTDKRRNTTMLSKTSTSYV
Protein: Protein phosphatase 1 regulatory inhibitor subunit 16B (Ankyrin repeat domain-containing protein 4) (CAAX box protein TIMAP) (TGF-beta-inhibited membrane-associated protein) (hTIMAP) (Q96T49)
Organism: Homo sapiens (Human)
Function: Regulator of protein phosphatase 1 (PP1) that acts as a positive regulator of pulmonary endothelial cell (EC) barrier function. Involved in the regulation of the PI3K/AKT signaling pathway, angiogenesis and endothelial cell proliferation. Regulates angiogenesis and endothelial cell proliferation through the control of ECE1 dephosphorylation, trafficking and activity (By similarity). Protects the endothelial barrier from lipopolysaccharide (LPS)-induced vascular leakage (By similarity). Involved in the regulation of endothelial cell filopodia extension (By similarity). May be a downstream target for TGF-beta1 signaling cascade in endothelial cells. Involved in PKA-mediated moesin dephosphorylation which is important in EC barrier protection against thrombin stimulation. Promotes the interaction of PPP1CA with RPSA/LAMR1 and in turn facilitates the dephosphorylation of RPSA/LAMR1. Involved in the dephosphorylation of EEF1A1.
Subcellular location: Cell membrane {ECO:0000269|PubMed:18586956, ECO:0000269|PubMed:26497934}. Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Nucleus {ECO:0000269|PubMed:18586956}. Cell projection {ECO:0000269|PubMed:25007873}. Note=Colocalizes with RPSA/LAMR1 in the cell membrane (PubMed:16263087). Localizes to the perinuclear region (By similarity). Colocalizes with PTEN at the tip of EC projections (PubMed:25007873). {ECO:0000250|UniProtKB:Q95N27, ECO:0000269|PubMed:16263087, ECO:0000269|PubMed:25007873}.
Interaction partners:
- Serine/threonine-protein phosphatase PP1-beta catalytic subunit
- Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
- Small ribosomal subunit protein uS2
- Protein phosphatase 1 regulatory subunit 7
Sequence:
MASHVDLLTELQLLEKVPTLERLRAAQKRRAQQLKKWAQYEQDLQHRKRKHERKRSTGGRRKKVSFEASVALLEASLRNDAEEVRYFLKNKVSPDLCNEDGLTALHQCCIDNFEEIVKLLLSHGANVNAKDNELWTPLHAAATCGHINLVKILVQYGADLLAVNSDGNMPYDLCEDEPTLDVIETCMAYQGITQEKINEMRVAPEQQMIADIHCMIAAGQDLDWIDAQGATLLHIAGANGYLRAAELLLDHGVRVDVKDWDGWEPLHAAAFWGQMQMAELLVSHGASLSARTSMDEMPIDLCEEEEFKVLLLELKHKHDVIMKSQLRHKSSLSRRTSSAGSRGKVVRRASLSDRTNLYRKEYEGEAILWQRSAAEDQRTSTYNGDIRETRTDQENKDPNPRLEKPVLLSEFPTKIPRGELDMPVENGLRAPVSAYQYALANGDVWKVHEVPDYSMAYGNPGVADATPPWSSYKEQSPQTLLELKRQRAAAKLLSHPFLSTHLGSSMARTGESSSEGKAPLIGGRTSPYSSNGTSVYYTVTSGDPPLLKFKAPIEEMEEKVHGCCRIS
Protein: Diacylglycerol kinase epsilon (DAG kinase epsilon) (EC 2.7.1.107) (Diglyceride kinase epsilon) (DGK-epsilon) (P52429)
Organism: Homo sapiens (Human)
Function: Membrane-bound diacylglycerol kinase that converts diacylglycerol/DAG into phosphatidic acid/phosphatidate/PA and regulates the respective levels of these two bioactive lipids. Thereby, acts as a central switch between the signaling pathways activated by these second messengers with different cellular targets and opposite effects in numerous biological processes. Also plays an important role in the biosynthesis of complex lipids. Displays specificity for diacylglycerol substrates with an arachidonoyl acyl chain at the sn-2 position, with the highest activity toward 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol the main diacylglycerol intermediate within the phosphatidylinositol turnover cycle. Can also phosphorylate diacylglycerol substrates with a linoleoyl acyl chain at the sn-2 position but much less efficiently.
Subcellular location: Membrane {ECO:0000269|PubMed:23542698}; Single-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:23542698}.
Interaction partners:
- Lipoprotein lipase
- Dihydroxyacetone phosphate acyltransferase
- Glycerol-3-phosphate dehydrogenase, mitochondrial
- Thrombomodulin
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2
- Complement factor B
- Complement factor H-related protein 5
- Complement factor H-related protein 1
- Cyanocobalamin reductase / alkylcobalamin dealkylase
- Complement factor H
Sequence:
MEAERRPAPGSPSEGLFADGHLILWTLCSVLLPVFITFWCSLQRSRRQLHRRDIFRKSKHGWRDTDLFSQPTYCCVCAQHILQGAFCDCCGLRVDEGCLRKADKRFQCKEIMLKNDTKVLDAMPHHWIRGNVPLCSYCMVCKQQCGCQPKLCDYRCIWCQKTVHDECMKNSLKNEKCDFGEFKNLIIPPSYLTSINQMRKDKKTDYEVLASKLGKQWTPLIILANSRSGTNMGEGLLGEFRILLNPVQVFDVTKTPPIKALQLCTLLPYYSARVLVCGGDGTVGWVLDAVDDMKIKGQEKYIPQVAVLPLGTGNDLSNTLGWGTGYAGEIPVAQVLRNVMEADGIKLDRWKVQVTNKGYYNLRKPKEFTMNNYFSVGPDALMALNFHAHREKAPSLFSSRILNKAVYLFYGTKDCLVQECKDLNKKVELELDGERVALPSLEGIIVLNIGYWGGGCRLWEGMGDETYPLARHDDGLLEVVGVYGSFHCAQIQVKLANPFRIGQAHTVRLILKCSMMPMQVDGEPWAQGPCTVTITHKTHAMMLYFSGEQTDDDISSTSDQEDIKATE
Protein: Prostacyclin receptor (Prostaglandin I2 receptor) (PGI receptor) (PGI2 receptor) (Prostanoid IP receptor) (P43119)
Organism: Homo sapiens (Human)
Function: Receptor for prostacyclin (prostaglandin I2 or PGI2). The activity of this receptor is mediated by G(s) proteins which activate adenylate cyclase.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Guanine nucleotide-binding protein G
- Prostacyclin synthase
- Thromboxane A2 receptor
- Prostaglandin G/H synthase 1
Sequence:
MADSCRNLTYVRGSVGPATSTLMFVAGVVGNGLALGILSARRPARPSAFAVLVTGLAATDLLGTSFLSPAVFVAYARNSSLLGLARGGPALCDAFAFAMTFFGLASMLILFAMAVERCLALSHPYLYAQLDGPRCARLALPAIYAFCVLFCALPLLGLGQHQQYCPGSWCFLRMRWAQPGGAAFSLAYAGLVALLVAAIFLCNGSVTLSLCRMYRQQKRHQGSLGPRPRTGEDEVDHLILLALMTVVMAVCSLPLTIRCFTQAVAPDSSSEMGDLLAFRFYAFNPILDPWVFILFRKAVFQRLKLWVCCLCLGPAHGDSQTPLSQLASGRRDPRAPSAPVGKEGSCVPLSAWGEGQVEPLPPTQQSSGSAVGTSSKAEASVACSLC
Protein: Uncharacterized protein Rv3395c (P9WKZ9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- UmuC domain-containing protein
- Error-prone DNA polymerase
- Probable membrane protein
- Uncharacterized protein Rv2100
- HNH nuclease domain-containing protein
- Fe2OG dioxygenase domain-containing protein
- DNA polymerase IV 1
- DNA polymerase IV 2
- LexA repressor
Sequence:
MTAAFASDQRLENGAEQLESLRRQMALLSEKVSGGPSRSGDLVPAGPVSLPPGTVGVLSGARSLLLSMVASVTAAGGNAAIVGQPDIGLLAAVEMGADLSRLAVIPDPGTDPVEVAAVLIDGMDLVVLGLGGRRVTRARARAVVARARQKGCTLLVTDGDWQGVSTRLAARVCGYEITPALRGVPTPGLGRISGVRLQINGRGR