wanglab/gogpt-training-data huggingface dataset:
Protein: Rab11 family-interacting protein 2 (Rab11-FIP2) (NRip11) (Q7L804)
Organism: Homo sapiens (Human)
Function: A Rab11 effector binding preferentially phosphatidylinositol 3,4,5-trisphosphate (PtdInsP3) and phosphatidic acid (PA) and acting in the regulation of the transport of vesicles from the endosomal recycling compartment (ERC) to the plasma membrane. Involved in insulin granule exocytosis. Also involved in receptor-mediated endocytosis and membrane trafficking of recycling endosomes, probably originating from clathrin-coated vesicles. Required in a complex with MYO5B and RAB11 for the transport of NPC1L1 to the plasma membrane. Also acts as a regulator of cell polarity. Plays an essential role in phagocytosis through a mechanism involving TICAM2, RAC1 and CDC42 Rho GTPases for controlling actin-dynamics.
Subcellular location: Cell projection, phagocytic cup {ECO:0000269|PubMed:30883606}. Cell membrane; Peripheral membrane protein. Recycling endosome membrane; Peripheral membrane protein. Note=Translocates with RAB11A from the vesicles of the endocytic recycling compartment (ERC) to the plasma membrane.
Interaction partners:
- Unconventional myosin-Vb
- Ras-related protein Rab-11A
- Ras-related protein Rab-25
- Ras-related protein Rab-11B
- EH domain-containing protein 1
- Rab11 family-interacting protein 3
- Rab11 family-interacting protein 4
- Rab11 family-interacting protein 5
- Rab11 family-interacting protein 1
- EH domain-containing protein 3
Sequence:
MMLSEQAQKWFPTHVQVTVLQAKDLKPKGKSGTNDTYTIIQLGKEKYSTSVAEKTLEPVWKEEASFELPGLLIQGSPEKYILFLIVMHRSLVGLDKFLGQVAINLNDIFEDKQRRKTEWFRLESKQGKRIKNRGEIKVNIQFMRNNMTASMFDLSMKDKTRSPFAKLKDKMKGRKNDGTFSDTSSAIIPSTHMPDANSEFSSGEIQMKSKPKKPFLLGPQRLSSAHSMSDLSGSHMSSEKLKAGTIGQTHLLGHQLDSFGTVPESGSLKSPHRRTLSFDTSKMNQPDSIVDEGELCFGRQNDPFTNVTASLPQKFATLPRKKNPFEESSETWDSSMNLFSKPIEIRKENKREKREKVSLFERVTGKKDSRRSDKLNNGGSDSPCDLKSPNAFSENRQDYFDYESTNPFTAKFRASNIMPSSSFHMSPTSNEDLRKIPDSNPFDATAGYRSLTYEEVLQELVKHKELLRRKDTHIRELEDYIDNLLVRVMEETPSILRVPYEPSRKAGKFSNS
Protein: Malyl-CoA/beta-methylmalyl-CoA/citramalyl-CoA lyase (EC 4.1.3.24) (EC 4.1.3.25) ((3S)-3-carboxy-3-hydroxypropanoyl-CoA glyoxylate-lyase) ((3S)-citramalyl-CoA pyruvate-lyase) ((S)-citramalyl-CoA lyase) (Erythro-beta-methylmalyl-CoA) (L-malyl-CoA lyase) (S5N020)
Organism: Chloroflexus aurantiacus
Function: Involved in the 3-hydroxypropionate cycle used for autotrophic carbon dioxide fixation, and in the glyoxylate assimilation cycle used to regenerate acetyl-CoA and produce pyruvate as universal precursor for biosynthesis. As a part of the 3-hydroxypropionate cycle, it catalyzes the cleavage of (S)-malyl-CoA to yield acetyl-CoA and glyoxylate. As part of the glyoxylate assimilation cycle, it catalyzes the condensation of glyoxylate with propionyl-CoA to yield (2R,3S)-beta-methylmalyl-CoA, and catalyzes the cleavage of (S)-citramalyl-CoA to yield acetyl-CoA and pyruvate.
Interaction partners:
Sequence:
MRKLAHNFYKPLAIGAPEPIRELPVRPERVVHFFPPHVEKIRARIPEVAKQVDVLCGNLEDAIPMDAKEAARNGFIEVVKATDFGDTALWVRVNALNSPWVLDDIAEIVAAVGNKLDVIMIPKVEGPWDIHFVDQYLALLEARHQIKKPILIHALLETAQGMVNLEEIAGASPRMHGFSLGPADLAASRGMKTTRVGGGHPFYGVLADPQEGQAERPFYQQDLWHYTIARMVDVAVAHGLRAFYGPFGDIKDEAACEAQFRNAFLLGCTGAWSLAPNQIPIAKRVFSPDVNEVLFAKRILEAMPDGSGVAMIDGKMQDDATWKQAKVIVDLARMIAKKDPDLAQAYGL
Protein: Proton-associated sugar transporter A (PAST-A) (Solute carrier family 45 member 1) (Q8K4S3)
Organism: Rattus norvegicus (Rat)
Function: Proton-associated glucose transporter in the brain.
Subcellular location: Membrane {ECO:0000269|PubMed:12417639}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MIPPAGSTPPGEALIPSVAPQDFWRSPISGYSGSVTRHISHRANNFKRHPKRRKYIRPSPPPPPNTPCPIELVDFEDLHPQRSFWELLFNGCILFGIEFSYAMETAYVTPVLLQMGLPDQLYSLVWFISPILGFLLQPLLGAWSDRCTSRFGRRRPFILVLAIGALLGLSLLLNGRDIGMALADTATNHKWGILLTVCGVVLMDFSADSADNPSHAYMMDVCGPVDQDRGLNIHALMAGLGGGFGYVVGGIHWDKTSFGRALGGQLRVIYIFTAITLSVTTVFTLVSIPERPLRPLGEKRTAMKSPSLPLPPSPPVLLEEGAGDTLPSTTATSLYASFSSPISPPSPLTPKYGSFISRDSSLTGINEFASSFGTSNIDSVLIDCFTAGHDNYLALPSSVPRQAISVSFPRAPDGFYCQERGLERREGPLTLGLDGDVLRVGSLDTSKPRASGILKRPQTLALPDVAGGNGPETSRRRNVTFSQQVANILLNGVKYESELTGSSEQSEQPLSLRRLCSTIYNMPRPVRNLCVNHFLGWLSFEGMLLFYTDFMGEVVFQGDPKAPHASEAYQKYNSGVTMGCWGMCIYAFSAAFYSAILEKLEECLSVRTLYFIAYLLFGLGTGLATLSRNLYVVLSLCTHYGILFSTLCTLPYSLLCDYYQSKKFAGSSADGTRRGMGVDISLLSCQYFLAQILVSLVLGPLTSAVGSANGVMYFASLVSFLGCLYSSLCVTYEIPSADAADEERQPLLLNV
Protein: DNA polymerase beta (EC 2.7.7.7) (5'-deoxyribose-phosphate lyase) (5'-dRP lyase) (EC 4.2.99.-) (AP lyase) (EC 4.2.99.18) (Q27958)
Organism: Bos taurus (Bovine)
Function: Repair polymerase that plays a key role in base-excision repair. Has 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity that removes the 5' sugar phosphate and also acts as a DNA polymerase that adds one nucleotide to the 3' end of the arising single-nucleotide gap. Conducts 'gap-filling' DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P06746}. Cytoplasm {ECO:0000250|UniProtKB:P06746}. Note=Cytoplasmic in normal conditions. Translocates to the nucleus following DNA damage. {ECO:0000250|UniProtKB:P06746}.
Interaction partners:
- X-ray repair cross complementing 1
- Flap endonuclease 1
- DNA ligase
- DNA repair nuclease/redox regulator APEX1
- Bifunctional polynucleotide phosphatase/kinase
- DNA ligase
- Poly [ADP-ribose] polymerase 1
- Ubiquitin carboxyl-terminal hydrolase 47
- Endonuclease 8-like 1 lyase Neil1)
- Poly [ADP-ribose] polymerase
Sequence:
MSKRKAPQETLNGGITDMLTELANFEKNVNQAIHKYNAYRKAASVIAKYPHKIKSGAEAKKLPGVGTKIAEKIDEFLATGKLRKLEKIRQDDTSSSINFLTRVSGIGPSAARKFVDEGIKTLEDLRKNEDKLNHHQRIGLKYFEDFEKRIPREEMLQMQDIVLSEVKKVDSEYIATVCGSFRRGAESSGDMDVLLTHPSFTSESAKQPKLLHRVVEQLQKVRFITDTLSKGETKFMGVCQLPSKNDEKEYPHRRIDIRLIPKDQYYCGVLYFTGSDIFNKNMRAHALEKGFTINEYTIRPLGVTGVAGEPLPVDSEKDIFDYIQWKYREPKDRSE
Protein: Outer kinetochore KNL1 complex subunit spc7 (Kinetochore protein spc7) (NMS complex subunit spc7) (O59757)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Acts as a component of the NMS (Ndc80-MIND-Spc7) super complex which has a role in kinetochore function during late meiotic prophase and throughout the mitotic cell cycle.
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Kinetochore protein mis13
- Kinetochore protein spc24
- Kinetochore protein nuf2
- Kinetochore protein mis14
- Spindle assembly checkpoint protein bub3
- Inner kinetochore subunit mis6
- Kinetochore protein ndc80
- Kinetochore protein spc25
- Inner kinetochore subunit mal2
- Aurora kinase
Sequence:
MPTSPRRNSIATTDNVIGRNKSRKRPHSLGGPGALQELKEHTNPAKGILKSYSSFSVDPAFTGDEDFNDIHTQINNTVIGISSNVMAASKRLQMEDLQQLSRETSRKSLNRRVSFASHARVRWYPKDHQSDSEKSTSNHSTPERTFASDAKNHSPKGPTTTSFSRNETQSSPHSHSASIISDGSDMDIASPIRSTESDMVSEALNAGHPPPSLYPENDDLSIQNPTKALPEAEKALDVHDATREQVNDREETNMDLTIQFQEADSFLSHSESIKGLSSSEQGTVYSLKASHDPSNQTQLSSPNKSSSPTSIEISDFSKNNENHDQSENKEEEEDMMLTRPIEIPQHFSPIARPLTSQEAIVDMDITSNNINLSPVSHFSNGLDLQNLEEAPMNLTRPINANPHLTNHSPNDLTNGEEEMDTTSAFNIENSHLTLLSPIRPSSRSMEEQIMDLTQPISSTNAPTHLNEDDLNQFTSNISSSSKPRKDNNKTANSSKPIPDSEDFMDITRPFNILSPSKEALSEEQPMELTSTVFPCENSTSHLEVEEAAMDETVAFQIRGNNVELPSADKENAEREEIPSYSDKSENFNTTSFTNHERSPNGNNNLKFSKDPNSSSPSRHVVATPTDKLGTRKRRLRYSTSSFDQSTLRRNRLATIRNARKSISTLNDRELLPVNFFEKKVNSGLYKSVERSENYRLGATPLTAEKPFTTEKPLSSLPEEVSRQPTDDKGEQVSNADVDSGLSKTERLTIQQTNEIKHVPTNTTSSVKLPQQPSNEDEKERITTADYADSTSLERLESQEPNRNELVQVGSSNAGNTTSVGMNEHEKSPVKLSKGVSNVDTSLGASTINTNILNQDSGPNEEIPVGNEPEFDTMPTLPNVEPISLSDFLKMTGIEFLDNLTIAKRRETLLPNAEENKKCSIQELLESFYIQFPLLELYKFSCQQLQDYIAEGKDFVTKIEEETLKENPLLFYEYRKASSDMRVLMDSQFLMMKTFARLQAKGDWYEWREGLMQGIKHELNLNLTGMQRSLTHLMDVANVIHPYAQEIQERYNGSITTVQTLKKQKEFANQYDSTLLAQAQEKLEKLKVEVERRRRLLSEKEERRKELAIKIEQVTNSCSDLELRTNAEQDFYAKNQDFEFDEIKRYEEQLLNLKNELGWTIVSLTAGGIKLATNNTALSPYSAEVTVEILRQNFQVNVDIACKFPNESNACSSNVLEHVASSFSKWHSKVFSRNLRLLKKYLNDVSICWEQIVYLVQDFQRLWYHWPFLSVENDDKSIIINVELYLRSVSSKVKVVFGLPIDTIYQTTEVGKFYASTSVAVKQMYAESEGDSYVSEVLNTLSEVVHCTSTYALSSACLTVWNKYS
Protein: Transcription factor protein (Q4H3J9)
Organism: Ciona intestinalis (Transparent sea squirt) (Ascidia intestinalis)
Interaction partners:
- Transcription factor protein
- Stress-activated protein kinase JNK
Sequence:
MYQELSTVYGEQCPPQSAAFESDIAFAQRADQHLNQSLRAYPYGPASDLGIHQPLYGSSGDLRQIQQPMAGIPPSYGEATHNQSHDLPTVMSRPDLQWLVTTSNVGMRTRTPPNTVSSPHVGRTDESSAITISHHDLPHHRFQQGEQLPPPLQRTNTGNKRVKMEANSAVPPRPKGTPGRKRKFQDHELSPAEATKRHIRRERNKIAAAKCRNRRRELTDRLQGETDHLEDHQSILHQEIMSLQQEKEHLEFLLAAHSPQCKAGIGASEHLLLAHDDRMMQSNMVGGMHEMSLVPPPEVMEEMMPQPHTDSCVPDNTHTHPGYYTEYSNQDTTLPVSLPSTCAPNSTGPTDLSLHSQSYGTPPTRFPNMNLEPLAISEAPLNTPVCTLTTPSISSGVFTFPSSTSGGLNTTTATTDMSYNYQTSSVSTPCPDFFQTPRLPTTPSYTASVTSFPADGQSFPVLSSHLQQQPAQSCSAAHRRSSSSESHNSPDSVKSPKLLSL
Protein: Methylenetetrahydrofolate reductase (Q5AU15)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Methylenetetrahydrofolate reductase
- Methylenetetrahydrofolate dehydrogenase [NAD
- Serine hydroxymethyltransferase
- C-1-tetrahydrofolate synthase, cytoplasmic
- Aminomethyltransferase
- Homocysteine S-methyltransferase
- Patatin-like serine hydrolase, putative
- Thymidylate synthase
- 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase
- Glycine cleavage system P protein
Sequence:
MEKITHKIAALPPGANYFSLEFFPPKTQMGFANLQARLERMAQALRPLFVTVTWGAGGSTAARSLELAEICQRQLQLTTCLHLTCTNMSRALVDQALEEAKVLGIRNILALRGDPPRSEEYNMHGEDDSNKDFTFAVDLVRYIRKKYGDYFCVGVAAYPEGHPADSFQDIQDPKVDLPWLVEKTQAGADFIMTQLTYDIDAYTEFENLLRNHESGTFKTIPIIPGLMPIHSYKILTRVTKLSHVKIPPPILAKLDEVKHDDDAVKRLGVDILAELVDGMKKLPTPGLRGFHFYTLNLEKTVSFILERCKLIPDHDDDAEAVADGVSLLTVDAEIANRRRRASSISSLPHNRVIVDKVSNGSSKDSVTHEATAASAGLPAGPPDRSTTLQISEGLGALGREATWDDFPNGRWGDARSPAFGEIDGYGPSLHVAPSVAHRIWGYPVSTDDISKLFRRHVSGDLHMVPWSEGGAEENTSGLNAETETIRPELLALIDKKGWWTLASQPAVNGVRSDDPIFGWGPPGEGFVFQKPFVEFFCPASDFKTTLKPLLQKHGHEKLAWFATNAAGDFESSLPAETSDTEPVEMNPNNVNAVTWGVFRGKEIVTPTIIEEVSFRAWGDEAYRIWDEWRRIYPKSSATEKFLEKTKNDVWLVCVVGQDFGAGTEVGSKEEDDEKKWMWRLLADC
Protein: Nucleoporin NUP2 (Nuclear pore protein NUP2) (p95) (P32499)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). As one of the FG repeat nucleoporins NUP2 is involved in interactions with and guidance of nuclear transport receptors such as SRP1-KAP95 (importin alpha and beta) through the NPC. Like the closely related NUP1 it also plays an important role in disassembling and recycling SRP1-KAP95 to the cytoplasm after nuclear import. Upon entry of the heterotrimeric SRP1-KAP95-cargo complex in the nucleus, NUP2 binds through its N-terminus to the SRP1 nuclear localization signal (NLS) binding site, thus accelerating the release of the NLS-cargo. SRP1 in turn is released from NUP2 by binding of the GSP1-GTP associated export factor CSE1. NUP2 may also have a chromatin boundary/insulator activity through indirect interaction with genomic DNA via CSE1 and blocking of heterochromatin spreading.
Subcellular location: Nucleus, nuclear pore complex {ECO:0000269|PubMed:10684247}. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side.
Interaction partners:
- Nucleoporin NUP49/NSP49
- Nucleoporin NIC96
- Importin subunit alpha
- GTP-binding nuclear protein GSP1/CNR1
- Nucleoporin NSP1
- Nucleoporin NUP57
- Importin subunit beta-1
- Nucleoporin NUP60
- Nucleoporin NUP159
- Protein MLP2
Sequence:
MAKRVADAQIQRETYDSNESDDDVTPSTKVASSAVMNRRKIAMPKRRMAFKPFGSAKSDETKQASSFSFLNRADGTGEAQVDNSPTTESNSRLKALNLQFKAKVDDLVLGKPLADLRPLFTRYELYIKNILEAPVKSIENPTQTKGNDAKPAKVEDVQKSSDSSSEDEVKVEGPKFTIDAKPPISDSVFSFGPKKENRKKDESDSENDIEIKGPEFKFSGTVSSDVFKLNPSTDKNEKKTETNAKPFSFSSATSTTEQTKSKNPLSLTEATKTNVDNNSKAEASFTFGTKHAADSQNNKPSFVFGQAAAKPSLEKSSFTFGSTTIEKKNDENSTSNSKPEKSSDSNDSNPSFSFSIPSKNTPDASKPSFSFGVPNSSKNETSKPVFSFGAATPSAKEASQEDDNNNVEKPSSKPAFNLISNAGTEKEKESKKDSKPAFSFGISNGSESKDSDKPSLPSAVDGENDKKEATKPAFSFGINTNTTKTADTKAPTFTFGSSALADNKEDVKKPFSFGTSQPNNTPSFSFGKTTANLPANSSTSPAPSIPSTGFKFSLPFEQKGSQTTTNDSKEESTTEATGNESQDATKVDATPEESKPINLQNGEEDEVALFSQKAKLMTFNAETKSYDSRGVGEMKLLKKKDDPSKVRLLCRSDGMGNVLLNATVVDSFKYEPLAPGNDNLIKAPTVAADGKLVTYIVKFKQKEEGRSFTKAIEDAKKEMK
Protein: Methionine--tRNA ligase, cytoplasmic (EC 6.1.1.10) (Methionyl-tRNA synthetase) (MetRS) (P56192)
Organism: Homo sapiens (Human)
Function: Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA. Plays a role in the synthesis of ribosomal RNA in the nucleolus.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:10791971, ECO:0000269|PubMed:19289464, ECO:0000305|PubMed:26472928}. Nucleus, nucleolus {ECO:0000269|PubMed:10791971}. Note=Localizes to the nucleolus in proliferative cells but disappears in quiescent cells. {ECO:0000269|PubMed:10791971}.
Interaction partners:
- Aspartate--tRNA ligase, cytoplasmic
- Glutamine--tRNA ligase
- Leucine--tRNA ligase, cytoplasmic
- Lysine--tRNA ligase
- Eukaryotic translation elongation factor 1 epsilon-1
- Isoleucine--tRNA ligase, cytoplasmic
- Bifunctional glutamate/proline--tRNA ligase
- Tyrosine--tRNA ligase, cytoplasmic
- Aminoacyl tRNA synthase complex-interacting multifunctional protein 2
- Arginine--tRNA ligase, cytoplasmic
Sequence:
MRLFVSDGVPGCLPVLAAAGRARGRAEVLISTVGPEDCVVPFLTRPKVPVLQLDSGNYLFSTSAICRYFFLLSGWEQDDLTNQWLEWEATELQPALSAALYYLVVQGKKGEDVLGSVRRALTHIDHSLSRQNCPFLAGETESLADIVLWGALYPLLQDPAYLPEELSALHSWFQTLSTQEPCQRAAETVLKQQGVLALRPYLQKQPQPSPAEGRAVTNEPEEEELATLSEEEIAMAVTAWEKGLESLPPLRPQQNPVLPVAGERNVLITSALPYVNNVPHLGNIIGCVLSADVFARYSRLRQWNTLYLCGTDEYGTATETKALEEGLTPQEICDKYHIIHADIYRWFNISFDIFGRTTTPQQTKITQDIFQQLLKRGFVLQDTVEQLRCEHCARFLADRFVEGVCPFCGYEEARGDQCDKCGKLINAVELKKPQCKVCRSCPVVQSSQHLFLDLPKLEKRLEEWLGRTLPGSDWTPNAQFITRSWLRDGLKPRCITRDLKWGTPVPLEGFEDKVFYVWFDATIGYLSITANYTDQWERWWKNPEQVDLYQFMAKDNVPFHSLVFPCSALGAEDNYTLVSHLIATEYLNYEDGKFSKSRGVGVFGDMAQDTGIPADIWRFYLLYIRPEGQDSAFSWTDLLLKNNSELLNNLGNFINRAGMFVSKFFGGYVPEMVLTPDDQRLLAHVTLELQHYHQLLEKVRIRDALRSILTISRHGNQYIQVNEPWKRIKGSEADRQRAGTVTGLAVNIAALLSVMLQPYMPTVSATIQAQLQLPPPACSILLTNFLCTLPAGHQIGTVSPLFQKLENDQIESLRQRFGGGQAKTSPKPAVVETVTTAKPQQIQALMDEVTKQGNIVRELKAQKADKNEVAAEVAKLLDLKKQLAVAEGKPPEAPKGKKKK
Protein: Sulfotransferase (EC 2.8.2.-) (Q49IK6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- UDP-glucuronosyltransferase
- Y cytochrome P450, family 2, subfamily AA, polypeptide 2
- Cytochrome P450, family 2, subfamily Y, polypeptide 3
- Cytochrome P450, family 2, subfamily Y, polypeptide 3.
Sequence:
MSRRTSETIRQIQGVPFPERIVKYWTRVEQFQASEEDLLIATYPKSGTTWIQEVVDLILNDGDVDKCKRAPTQVRMPFLEMTAADGSNAGITKLETMDPPRVIKTHLPIQLLPRSFENAGCKVIYVARNPKDSVVSFYHFDRMNLRQPEPGPWKQYLERFMKGQLVWGSWFDHVKGYWRERHKRKIHYMFFEDMKEDPAREVTRTAQFLGRQLSESTIDHIVQMTTFSVMRENPMANYSTLPDTIFDRTASQFMRKGEVGDWKNHFSAEENAAFDEHYQKKMEDCPLPIRFTI
Protein: ATP synthase gamma chain (ATP synthase F1 sector gamma subunit) (F-ATPase gamma subunit) (P09222)
Organism: Bacillus sp. (strain PS3)
Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex.
Subcellular location: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MKPLASLRDIKTRINATKKTSQITKAMEMVLTSKLNRAEKREIVRPYMEKIQEVVANVALAARASHPMLVSRPVKKTGYLVITSDRGLAGAYNSNVLRLVYQTIQKRHASPDEYAIIVIGRVGLSFFRKRNMPVILDITRLPDQPSFADIKEIARKTVGLFADGTFDELYMYYNHYVSAIQQEVTERKLLPLTDLAENKQRTVYEFEPSQEEILDVLLPQYAESLIYGALLDAKASEHAARMTAMKNATDNANELIRTLTLSYNRARQAAITQEITEIVAGANALQ
Protein: Glycosylation-dependent cell adhesion molecule 1 (GlyCAM-1) (28 kDa milk glycoprotein PP3) (Lactophorin) (Proteose-peptone component 3) (PP3) (P80195)
Organism: Bos taurus (Bovine)
Subcellular location: Membrane; Peripheral membrane protein.
Interaction partners:
- L-selectin
- Alpha-S2-casein
- Beta-casein
- Alpha-lactalbumin
- Alpha-S1-casein
- Kappa-casein
- Beta-lactoglobulin
- Butyrophilin subfamily 1 member A1
- Tyrosine-protein kinase
- Mucosal vascular addressin cell adhesion molecule 1.
Sequence:
MKFLCVLLLASLAATSLAILNKPEDETHLEAQPTDASAQFIRNLQISNEDLSKEPSISREDLISKEQIVIRSSRQPQSQNPKLPLSILKEKHLRNATLGSEETTEHTPSDASTTEGKLMELGHKIMRNLENTVKETIKYLKSLFSHAFEVVKT
Protein: Disheveled-associated activator of morphogenesis 2 (Q86T65)
Organism: Homo sapiens (Human)
Function: Key regulator of the Wnt signaling pathway, which is required for various processes during development, such as dorsal patterning, determination of left/right symmetry or myelination in the central nervous system. Acts downstream of Wnt ligands and upstream of beta-catenin (CTNNB1). Required for canonical Wnt signaling pathway during patterning in the dorsal spinal cord by promoting the aggregation of Disheveled (Dvl) complexes, thereby clustering and formation of Wnt receptor signalosomes and potentiating Wnt activity. During dorsal patterning of the spinal cord, inhibits oligodendrocytes differentiation via interaction with PIP5K1A. Also regulates non-canonical Wnt signaling pathway. Acts downstream of PITX2 in the developing gut and is required for left/right asymmetry within dorsal mesentery: affects mesenchymal condensation by lengthening cadherin-based junctions through WNT5A and non-canonical Wnt signaling, inducing polarized condensation in the left dorsal mesentery necessary to initiate gut rotation. Together with DAAM1, required for myocardial maturation and sarcomere assembly. Is a regulator of actin nucleation and elongation, filopodia formation and podocyte migration.
Interaction partners:
- Segment polarity protein dishevelled homolog DVL-1
- Transforming protein RhoA
- Segment polarity protein dishevelled homolog DVL-2
- Segment polarity protein dishevelled homolog DVL-3
- Disheveled-associated activator of morphogenesis 1
- Profilin-4
Sequence:
MAPRKRSHHGLGFLCCFGGSDIPEINLRDNHPLQFMEFSSPIPNAEELNIRFAELVDELDLTDKNREAMFALPPEKKWQIYCSKKKEQEDPNKLATSWPDYYIDRINSMAAMQSLYAFDEEETEMRNQVVEDLKTALRTQPMRFVTRFIELEGLTCLLNFLRSMDHATCESRIHTSLIGCIKALMNNSQGRAHVLAQPEAISTIAQSLRTENSKTKVAVLEILGAVCLVPGGHKKVLQAMLHYQVYAAERTRFQTLLNELDRSLGRYRDEVNLKTAIMSFINAVLNAGAGEDNLEFRLHLRYEFLMLGIQPVIDKLRQHENAILDKHLDFFEMVRNEDDLELARRFDMVHIDTKSASQMFELIHKKLKYTEAYPCLLSVLHHCLQMPYKRNGGYFQQWQLLDRILQQIVLQDERGVDPDLAPLENFNVKNIVNMLINENEVKQWRDQAEKFRKEHMELVSRLERKERECETKTLEKEEMMRTLNKMKDKLARESQELRQARGQVAELVAQLSELSTGPVSSPPPPGGPLTLSSSMTTNDLPPPPPPLPFACCPPPPPPPLPPGGPPTPPGAPPCLGMGLPLPQDPYPSSDVPLRKKRVPQPSHPLKSFNWVKLNEERVPGTVWNEIDDMQVFRILDLEDFEKMFSAYQRHQKELGSTEDIYLASRKVKELSVIDGRRAQNCIILLSKLKLSNEEIRQAILKMDEQEDLAKDMLEQLLKFIPEKSDIDLLEEHKHEIERMARADRFLYEMSRIDHYQQRLQALFFKKKFQERLAEAKPKVEAILLASRELVRSKRLRQMLEVILAIGNFMNKGQRGGAYGFRVASLNKIADTKSSIDRNISLLHYLIMILEKHFPDILNMPSELQHLPEAAKVNLAELEKEVGNLRRGLRAVEVELEYQRRQVREPSDKFVPVMSDFITVSSFSFSELEDQLNEARDKFAKALMHFGEHDSKMQPDEFFGIFDTFLQAFSEARQDLEAMRRRKEEEERRARMEAMLKEQRERERWQRQRKVLAAGSSLEEGGEFDDLVSALRSGEVFDKDLCKLKRSRKRSGSQALEVTRERAINRLNY
Protein: Exportin 1 (CRM1 homolog, yeast) a (Exportin-1) (E7F0E8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Nucleoporin 214.
- GTP-binding nuclear protein Ran
- Nucleoporin 88
- Snurportin-1
- Si:ch1073-55a19.2.
- Nucleoporin NUP42
- FinTRIM family, member 52, pseudogene.
- Phosphorylated adaptor for RNA export.
- Exportin 1
- Adhesion G protein-coupled receptor D1
Sequence:
MPADMTMLADHTARQLLDFSQKLDINLLDNVVNSMYYDVGSQQRLAQEVLTNLKDHPDAWTRVDTILEFSQNMKTKYYALQILETVIKTRWKILPRNQCEGIKKYVVGLIIKTSSDANSVEKEQVYISKLNMILVQILKQEWPKHWPTFISDIVGASRTSESLCQNNMIILKLLSEEVFDFSSGQMTQVKAKHLKDSMCNEFSQIFQLCQFVMENSQNAPLVHATLETLLRFLNWIPLGYIFETKLISTLVYKFLNVPMFRNVTLKCLTEIAGVSVSQYEEQFVNLFTLTMMQLKQMLPLNTNIRLAYSNGKDDEQNFIQNLSLFLCTFLKEHGQLIEKRLNLRETLMEALHYMLLVSEVEETEIFKICLEYWNHLAAELYRESPFSTSTSPLLSTSQHFDVPPRRHLYLPVLSKVRLLMVSRMAKPEEVLVVENDQGEVVREFMKDTDSINLYKNMRETLVYLTHLDYADTERIMTEKLHNQVNGTEWSWRNLNTLCWAIGSISGAMHEEDEKRFLVTVIKDLLGLCEQKRGKDNKAIIASNIMYIVGQYPRFLRAHWKFLKTVVNKLFEFMHETHDGVQDMACDTFIKIAQKCRRHFVQVQVGEVMPFIDEILNNINTIICDLQPQQVHTFYEAVGYMIGAQTDQAVQERLIEKYMLLPNQVWDSIIQQATKNVDILKDPETVRQLGSILKTNVRACKAVGHPFVLQLGRIYLDMLNVYKCLSENISSAIQSNGEMVTKQPLIRSMRTVKRETLKLISGWVSRSNDPQMVGENFVPPLLEAVLIDYQRNVPAAREPEVLSTMATIVNKLGSHITGEIPKIFDAVFECTLEMINKNFEEFPEHRTHFFYLLQAVNSQCFPAFLSIPPAQFKLVLDSIIWAFKHTMRNVADTGLQILFTMLQNIAQEEAAAQSFYQTYFFDILQHIFSVVTDTSHTAGLTMHASILAYMFNLVEEGKISVALNAGTAGNNQGYVQDYVANLLKTAFPHLQDAQVKVFVTGLFSLNQDIPAFKEHLRDFLVQIKEFAGEDSTDLFLEEREASLRQAQEEKHKIQLSVPGILNPHELPEEMCE
Protein: NAD(P)H-quinone oxidoreductase subunit H, chloroplastic (EC 7.1.1.-) (NAD(P)H dehydrogenase subunit H) (NADH-plastoquinone oxidoreductase 49 kDa subunit) (NADH-plastoquinone oxidoreductase subunit H) (P56753)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01358}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01358}; Stromal side {ECO:0000255|HAMAP-Rule:MF_01358}.
Interaction partners:
- NAD
- NAD
- NAD
- NAD
- NAD
- NAD
- NAD
- NAD
- NAD
- Photosystem I iron-sulfur center
Sequence:
MKRPVTGKDLMIVNMGPHHPSMHGVLRLIVTLDGEDVVDCEPILGYLHRGMEKIAENRAIIQYLPYVTRWDYLATMFTEAITVNGPEQLGNIQVPKRASYIRVIMLELSRIASHLLWLGPFMADIGAQTPFFYIFREREFVYDLFEAATGMRMMHNFFRIGGIAADLPYGWIDKCLDFCDYFLTEVVEYQKLITRNPIFLERVEGVGIIGGEEAINWGLSGPMLRASGIPWDLRKIDRYESYDEFEWEIQWQKQGDSLARYLVRLSEMTESIKIIQQALEGLPGGPYENLESRGFDRKRNPEWNDFEYRFISKKPSPTFELSKQELYVRVEAPKGELGIFLIGDQSGFPWRWKIRPPGFINLQILPELVKRMKLADIMTILGSIDIIMGEVDR
Protein: Adenylyl-sulfate kinase 1, chloroplastic (EC 2.7.1.25) (ATP adenosine-5'-phosphosulfate 3'-phosphotransferase 1) (Adenosine-5'-phosphosulfate kinase 1) (APS kinase 1) (Q43295)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the synthesis of activated sulfate. Essential for plant reproduction and viability. Required for the production of glucosinolates.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:19304933}.
Interaction partners:
- ATP sulfurylase 4, chloroplastic
- ATP-sulfurylase 3, chloroplastic
- ATP sulfurylase 2
- ATP sulfurylase 1, chloroplastic
- 5'-adenylylsulfate reductase 1, chloroplastic
- 5'-adenylylsulfate reductase 2, chloroplastic
- 5'-adenylylsulfate reductase 3, chloroplastic
- Assimilatory sulfite reductase
- Adenylyl-sulfate kinase 2, chloroplastic
- 3'
Sequence:
MIAAGAKSLLGLSMASPKGIFDSNSMSNSRSVVVVRACVSMDGSQTLSHNKNGSIPEVKSINGHTGQKQGPLSTVGNSTNIKWHECSVEKVDRQRLLDQKGCVIWVTGLSGSGKSTLACALNQMLYQKGKLCYILDGDNVRHGLNRDLSFKAEDRAENIRRVGEVAKLFADAGIICIASLISPYRTDRDACRSLLPEGDFVEVFMDVPLSVCEARDPKGLYKLARAGKIKGFTGIDDPYEPPLNCEISLGREGGTSPIEMAEKVVGYLDNKGYLQA
Protein: Antifungal protein J (AFP-J) (P84794)
Organism: Solanum tuberosum (Potato)
Function: Inhibitor of serine proteases chymotrypsin, pepsin and trypsin. Has strong antifungal activity against the human pathogenic fungi C.albicans TIMM 1768, S.cerevisiae KCTC 7296 and T.beigelli KCTC 7707, but lacks antifungal activity against the plant pathogenic fungi C.gloeosporioides KACC 40003, C.coccodes KACC 40803 and D.bryoniae KACC 40669. Lacks hemolytic activity against human erythrocytes.
Subcellular location: Vacuole {ECO:0000250|UniProtKB:P30941}.
Interaction partners:
- Potamin-1
Sequence:
LPSDATLVLDQTGKELDARL