wanglab/gogpt-training-data huggingface dataset:
Protein: Transporter (Q9DGN5)
Organism: Gallus gallus (Chicken)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MGQRHPQCYLARMNKQIQPDRKVSVVAPLPERPGPSPPRKDVELILVKEHNGVQYTSSNLLPAAPAPRYGPQDRETWGKKIDFLLSVIGFAVDLANVWRFPYLCYKNGGGAFLIPYILFLIIAGMPLFYMELALGQYNREGAATVWKICPVFKGVGYAVILIALYVGFYYNVIIAWSLYYLFSSFTFELPWTNCDNSWNSPNCTDPKLFNASVLGNGTKYSKYKLTPAAEFYERGVLHLHESRGIHDLGLPRWQLSLCLLVVVIILFFSLWKGVKTSGKVVWITATLPYVVLFVLLIHGITLPGAYNGINAYLHIDFRRLKEATVWIDAATQIFYSLGAGFGVLIAFASYNKFDNNCYRDALLTSTINCVTSFISGFAIFSILGYMAHEHKVKIEDVATEGAGLVFILYPEAISTLSGSTFWAVVFFIMLLTLGIDSSMGGMEAVITGLADDFHILKQHRKLFTFGVSFGTFLLALFCITNGGIYVLTLLDTFAAGTSILFAVLMEAIGVSWFYGVDRFSEDIQQMMGFKPGLYWRLCWKFVSPAFLLFVVIVSIINFKPLTYDDYTFPFWANRIGWGIALSSMILVPAYVIYKFMNVRGTFKERLAYCITPENEHQLVAQGNVRQFKLQHWLTI
Protein: [histone H4]-lysine(20) N-methyltransferase (EC 2.1.1.361) (C9JKQ0)
Organism: Homo sapiens (Human)
Subcellular location: Chromosome {ECO:0000256|ARBA:ARBA00004286}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MRWLWLLLFPDSPVTLREVLPSQPWRLRGCSDLRGENVFTGQSKIYSYMSPNKCSGMRFPLQEENSVTHHEVKCQGKPLAGIYRKREEKRNAGNAVRSAMKSEEQKIKDARKGPLVPFPNQKSEAAEPPKTPPSSCDSTNAAIAKQALKKPIKGKQAPRKKAQGKTQQNRKLTDFYPVRRSSRKSKAELQSEERKRIDELIESGKEEGMKIDLIDGKGRGVIATKQFSRGDFVVEYHGDLIEITDAKKREALYAQDPSTGCYMYYFQYLSKTYCVDATRETNRLGRLINHSKCGNCQTK
Protein: Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha (EC 2.5.1.58) (EC 2.5.1.59) (CAAX farnesyltransferase subunit alpha) (FTase-alpha) (Ras proteins prenyltransferase subunit alpha) (Type I protein geranyl-geranyltransferase subunit alpha) (GGTase-I-alpha) (Q04631)
Organism: Rattus norvegicus (Rat)
Function: Essential subunit of both the farnesyltransferase and the geranylgeranyltransferase complex. Contributes to the transfer of a farnesyl or geranylgeranyl moiety from farnesyl or geranylgeranyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X. May positively regulate neuromuscular junction development downstream of MUSK via its function in RAC1 prenylation and activation.
Interaction partners:
- Geranylgeranyl transferase type-1 subunit beta
- Protein farnesyltransferase subunit beta
- Geranylgeranyl pyrophosphate synthase
- CAAX prenyl protease 2
- CAAX prenyl protease
- Alkyl transferase
- All trans-polyprenyl-diphosphate synthase PDSS1
- Dehydrodolichyl diphosphate synthase complex subunit NUS1
- All trans-polyprenyl-diphosphate synthase PDSS2
- Squalene synthase
Sequence:
MAATEGVGESAPGGEPGQPEQPPPPPPPPPAQQPQEEEMAAEAGEAAASPMDDGFLSLDSPTYVLYRDRAEWADIDPVPQNDGPSPVVQIIYSEKFRDVYDYFRAVLQRDERSERAFKLTRDAIELNAANYTVWHFRRVLLRSLQKDLQEEMNYIIAIIEEQPKNYQVWHHRRVLVEWLKDPSQELEFIADILNQDAKNYHAWQHRQWVIQEFRLWDNELQYVDQLLKEDVRNNSVWNQRHFVISNTTGYSDRAVLEREVQYTLEMIKLVPHNESAWNYLKGILQDRGLSRYPNLLNQLLDLQPSHSSPYLIAFLVDIYEDMLENQCDNKEDILNKALELCEILAKEKDTIRKEYWRYIGRSLQSKHSRESDIPASV
Protein: Zgc:171802 protein (A8E4T2)
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:
MWNDTDLLRNDSFSCASPSVEGYRYFGVLLGSAVTIVGTIGNILTVLAFVTDANLRTRFNVLIVNLAFADLLYCTILQPVSVDSYLHLHWRGGATWCRMFGLLLFLSNSVSIITLCLIAMSRYLVVAHRTSSCARLLLSQRGVAALLISSWVLGLASFAPLWPVYVFAPQVCTCSFHRTKGRPYATVLLFLYFFLGLGFVGLFYFLIYRKVSVAAKAFLKYRPSRRSSKRKQAEAEGTTDDSGISAGASTTQSCEISSDGAVAEKHGKQAQEGQTTTQNATQNASSETTSKASPVVIQNTPAAANSGEDNEFKRVTRMCFTVFLCFVGCFAPFLLLNVADKKNRAPQVIHMICANLTWLNSCINPLLYAAMNRQFNQAYKDLLSKAAHPLRWIGRTHWFTSR
Protein: cDNA FLJ45002 fis, clone BRAWH3011577, moderately similar to Zinc finger protein 175 (Q6ZT36)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPANEDAPQPGEHGSACEVSVSFEDVTVDFSREEWQQLDSTQRRLYQDVMLENYSHLLSVGFEVPKPEVIFKLEQGEGPWTLEGEAPHQSCSDGKFGIKPSQRRISGKSTFHSEMEGEDTLC
Protein: Protein NRT1/ PTR FAMILY 2.13 (AtNPF2.13) (Nitrate transporter 1.7) (Q8RX77)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Low-affinity proton-dependent nitrate transporter. Not involved in dipeptides transport, but has a weak glucosinolate transport activity. Involved in phloem loading and nitrate remobilization from the older leaves to other tissues.
Subcellular location: Cell membrane {ECO:0000269|PubMed:19734434, ECO:0000269|PubMed:28032637}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes at the plasma membrane, where it interacts with NLA. {ECO:0000269|PubMed:28032637}.
Interaction partners:
- High affinity nitrate transporter 2.7
- High affinity nitrate transporter 2.4
- High-affinity nitrate transporter 2.1
- High affinity nitrate transporter 2.5
- Chloride channel protein CLC-a
- High-affinity nitrate transporter 3.1
- E3 ubiquitin-protein ligase NLA
- High-affinity nitrate transporter 2.2
Sequence:
MVLEDRKDGSSLPGRSGSFSKSSPSELDVVDPYKRISSPGSILDAEKVEKKPGGWRAVSFILGNETLERLGSIGLLANFMVYLTKVFHLEQVDAANVINIWSGFTNLTPLVGAYISDTYVGRFKTIAFASFATLLGLITITLTASFPQLHPASCNSQDPLSCGGPNKLQIGVLLLGLCFLSVGSGGIRPCSIPFGVDQFDQRTEEGVKGVASFFNWYYMTFTVVLIITQTVVVYIQDQVSWIIGFSIPTGLMALAVVMFFAGMKRYVYVKPEGSIFSGIAQVIVAARKKRKLKLPAEDDGTVTYYDPAIKSSVLSKLHRSNQFRCLDKAAVVIEGDLTPEGPPADKWRLCSVQEVEEVKCLIRIVPIWSAGIISLAAMTTQGTFTVSQALKMDRNLGPKFEIPAGSLSVISLLTIGIFLPFYDRVFVPFMRRITGHKSGITLLQRIGTGIVFAIFSMIVAGIVERMRRIRSINAGDPTGMTPMSVFWLSPQLILMGLCEAFNIIGQIEFFNSQFPEHMRSIANSLFSLSFAGSSYLSSFLVTVVHKFSGGHDRPDWLNKNLNAGKLDYFYYLIAVLGVVNLVYFWYCARGYRYKVGLPIEDFEEDKSSDDVEMTSKKSMK
Protein: Uncharacterized protein (EC 1.1.1.300) (A1Z729)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MCIFIDCLLSPLIMWPATIGVGIYFLKEYMQGGKFTKDTDETGKVFIVTGANTGIGKETALEIARRGGTVYLACRDMNRCEKARKDIIKETNNQNIFSRELDLSSLDSIRKFVDGFKKEQPKLHVLINNAGVMRCPKTLTKDGYELQLGVNHIGHFLLTNLLLDVLKNSAPSRIVVVSSLAHARGSINVADLNSEKSYDEGLAYSQSKLANVLFTRELAKRLEGSGVTVNALHPGVVDTELARNWAFFQTNLVKFFLKPMIWPLLKTPKSGAQTSIYAALDPELKNISGLYFSDCKPKPVASGALDDKVAKFLWAESEKWTGLDKLEANN
Protein: Small ribosomal subunit protein uS14c (30S ribosomal protein S14, chloroplastic) (P0C466)
Organism: Oryza sativa subsp. indica (Rice)
Function: Binds 16S rRNA, required for the assembly of 30S particles.
Subcellular location: Plastid, chloroplast.
Interaction partners:
- Small ribosomal subunit protein mS35 mitochondrial conserved domain-containing protein
- Small ribosomal subunit protein uS12cz/uS12cy
- S5 DRBM domain-containing protein
- Small ribosomal subunit protein uS2c
- Uncharacterized protein
- Uncharacterized protein
- Small ribosomal subunit protein uS9c
- Small ribosomal subunit protein mS29
- Small ribosomal subunit protein bS16c
- Small ribosomal subunit protein uS7cz/uS7cy
Sequence:
MAKKSLIQRERKRQKLEQKYHLIRRSSKKKIRSKVYPLSLSEKTKMREKLQSLPRNSAPTRLHRRCFLTGRPRANYRDFGLSGHILREMVYACLLPGATRSSW
Protein: Phloretin 4'-O-glucosyltransferase (MdPh-4'-OGT) (EC 2.4.1.-) (Flavanone 7-O-beta-glucosyltransferase UGT75L17) (EC 2.4.1.185) (UDP-glycosyltransferase 75L17) (A7MAS5)
Organism: Malus domestica (Apple) (Pyrus malus)
Function: Glycosyltransferase that possesses phloretin 4'-O-glycosyltransferase activity. Converts phloretin to trilobatin (phloretin 4'-O-glucoside), a potential antioxidant. Can convert with low efficiency phlorizin and trilobatin to their corresponding di-O-glucosides. Can convert with low efficiency naringenin to naringenin-7-O-glucoside. Can convert with low efficiency quercetin to quercetin-7-O-glucoside.
Interaction partners:
Sequence:
MVQHRFLLVTFPAQGHINPSLQFAKRLINTTGAHVTYVTSLSAHRRIGNGSIPDGLTYAPFSDGYDDGFKPGDNVDDYMSELRRRGVQAITDLVVASANEGHPYTCLVYSLLLPWSAGMAHELHLPSVLLWIQPATVFDIYYYYFNGYKDLIRDNTSSGTNNVLPCSIELPGLPLSFTSRDLPSFMVDTNPYNFALPLFQEQMELLERETNPTILVNTFDALEPEALKAIDKYNLIGVGPLIPSAFLDGKDPSDKSFGGDLFQKSKDSSYLEWLNSKPEGSVIYVSFGSISVLGKAQMEEIAKGLLDCGLPFLWVIRDKVGKKGDDNEAKKEEEMLRCREELEELGMIVPWCSQVEVLSSPSLGCFVTHCGWNSSLESLVSGVPVVAFPQWTDQGTNAKLIEDYWKTGVRVTPNEEGIVTGEELKRCLDLVLGSGEIGEDVRRNAKKWKDLAREAVSEGDSSDKNLRAFLDQIKVLKDARH
Protein: Hemolysin E, chromosomal (Cytotoxin ClyA) (Hemolysis-inducing protein) (Latent pore-forming 34 kDa hemolysin) (Silent hemolysin SheA) (P77335)
Organism: Escherichia coli (strain K12)
Function: Toxin, which has some hemolytic activity towards mammalian cells. Acts by forming a pore-like structure upon contact with mammalian cells.
Subcellular location: Secreted. Periplasm. Host cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Note=Exported from the cell by outer membrane vesicles. Also found in the periplasmic space.
Interaction partners:
- Transcriptional regulator SlyA
- Prophage lipoprotein Bor homolog
- Outer membrane porin G
Sequence:
MTEIVADKTVEVVKNAIETADGALDLYNKYLDQVIPWQTFDETIKELSRFKQEYSQAASVLVGDIKTLLMDSQDKYFEATQTVYEWCGVATQLLAAYILLFDEYNEKKASAQKDILIKVLDDGITKLNEAQKSLLVSSQSFNNASGKLLALDSQLTNDFSEKSSYFQSQVDKIRKEAYAGAAAGVVAGPFGLIISYSIAAGVVEGKLIPELKNKLKSVQNFFTTLSNTVKQANKDIDAAKLKLTTEIAAIGEIKTETETTRFYVDYDDLMLSLLKEAAKKMINTCNEYQKRHGKKTLFEVPEV
Protein: Mitogen-activated protein kinase kinase kinase A (EC 2.7.11.25) (MAPK/ERK kinase 1) (MEK kinase 1) (MEKK 1) (MAPK/ERK kinase A) (MEK kinase A) (MEKK A) (MEKKalpha) (Q54R82)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Regulates cell-type differentiation and spatial patterning, required for the proper induction and maintenance of prespore cell differentiation.
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. Note=Localized predominantly at the periphery of the cells, possibly in the cortex or the plasma membrane. {ECO:0000255, ECO:0000269|PubMed:9832508}.
Interaction partners:
Sequence:
MSWLNNPSQNFVDPFIRIKCILGDDIRIIKFNSNISYGGLMNQLEQDFQCPISIHQYEDYEGDKVTVKSKDDIMEALTMYFELKALNPTKIISTKFFLKQLPPQSQPLSSSLSPTQSLILNNNNNNNNNNNNNNNNNNNNNNNNIIQHTDFPSLIINEHEELISNHNIKWQKGQILGRGGYGSVYLGLNKDTGELFAVKQLEIVDINSDPKLKNMILSFSKEIEVMRSLRHDNIVRYLGTSLDQSFLSVFLEYIPGGSISSLLGKFGAFSENVIKVYTKQILQGLSFLHANSIIHRDIKGANILIDTKGIVKLSDFGCSKSFSGIVSQFKSMQGTPYWMAPEVIKQTGHGRSSDIWSLGCVIVEMATAQPPWSNITELAAVMYHIASSNSIPNIPSHMSQEAFDFLNLCFKRDPKERPDANQLLKHPFIMNLDDNIQLPTISPTTTLSTNTTNTTATTTTTNNATNSNINQQQQQQQQQPPTRTQRVSISAGSSNNKRYTPPISTSTSSSSSSILNNFSINIILPINLIILIFREIKPNFVNTLSRVCKHWKQIIDDDELWNKYCSDRLINKSKFEESITWKSNYIKIYKQQKVWFHNKLNHSTLKGHDKGVFCVKLIDDQGMVLSGGEDKKLKVWDISGNHHHNHHSGIVGSISKKSGLNIINNNNSNNSNSSSNSSSSNSRYLFSLKGHSGCIKSVDYQRQSGSDVSRVFTASADFTCKIFSLKTKKTLFTYTNHQEAVTCINYLGDVENKCITSSLDKTIQLWDAETGSCLSTLRGHTGGIYCVKTDQVATHGNGYNHLVVSASVDKTSNVWDTRSSSKVRSFTQHTEDVLCCYVFDQKVVTGSCDGTIKLWDIGTGKTISTFIPSETRQKNYVWTVQFDQSKIISSGKTGIIRIWDIYNERDSRSIGGHHETIFSLQFNNQKLITGSLDKLVKIWSID
Protein: ADP-ribosylation factor-like protein 13B (ADP-ribosylation factor-like protein 2-like 1) (ARL2-like protein 1) (Q3SXY8)
Organism: Homo sapiens (Human)
Function: Cilium-specific protein required to control the microtubule-based, ciliary axoneme structure. May act by maintaining the association between IFT subcomplexes A and B. Binds GTP but is not able to hydrolyze it; the GTPase activity remains unclear. Required to pattern the neural tube. Involved in cerebral cortex development: required for the initial formation of a polarized radial glial scaffold, the first step in the construction of the cerebral cortex, by regulating ciliary signaling. Regulates the migration and placement of postmitotic interneurons in the developing cerebral cortex. May regulate endocytic recycling traffic; however, additional evidence is required to confirm these data.
Subcellular location: Cell projection, cilium membrane {ECO:0000269|PubMed:18554500, ECO:0000269|PubMed:24120134}; Lipid-anchor {ECO:0000269|PubMed:18554500, ECO:0000269|PubMed:24120134}. Cell projection, cilium {ECO:0000269|PubMed:25138100, ECO:0000269|PubMed:38219074}. Cell membrane {ECO:0000269|PubMed:23223633}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:23223633}. Note=Associates with the cilium membrane via palmitoylation. Localizes to proximal ciliary membranes, to an inversin-like subciliary membrane compartment, excluding the transition zone (PubMed:25138100, PubMed:38219074). Colocalizes with microtubules (PubMed:23223633). {ECO:0000269|PubMed:23223633, ECO:0000269|PubMed:25138100, ECO:0000269|PubMed:38219074}.
Interaction partners:
- Phosphatidylinositol polyphosphate 5-phosphatase type IV
- Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit delta
- Intraflagellar transport protein 88 homolog
- Coiled-coil and C2 domain-containing protein 2A
- Transmembrane protein 216
- Intraflagellar transport protein 22 homolog
- Jouberin
- Meckelin
- Intraflagellar transport protein 81 homolog
- Centrosomal protein of 290 kDa
Sequence:
MFSLMASCCGWFKRWREPVRKVTLLMVGLDNAGKTATAKGIQGEYPEDVAPTVGFSKINLRQGKFEVTIFDLGGGIRIRGIWKNYYAESYGVIFVVDSSDEERMEETKEAMSEMLRHPRISGKPILVLANKQDKEGALGEADVIECLSLEKLVNEHKCLCQIEPCSAISGYGKKIDKSIKKGLYWLLHVIARDFDALNERIQKETTEQRALEEQEKQERAERVRKLREERKQNEQEQAELDGTSGLAELDPEPTNPFQPIASVIIENEGKLEREKKNQKMEKDSDGCHLKHKMEHEQIETQGQVNHNGQKNNEFGLVENYKEALTQQLKNEDETDRPSLESANGKKKTKKLRMKRNHRVEPLNIDDCAPESPTPPPPPPPVGWGTPKVTRLPKLEPLGETHHNDFYRKPLPPLAVPQRPNSDAHDVIS
Protein: Potassium channel subfamily K member 1b isoform 2 (Potassium channel, subfamily K, member 1b) (A0A0R4IHS3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MLQSLAGNSCVRLIQSNKSAWYFLFLVLGYVLYLIFGAVVFSSVELPYEDDLRQQLREIKRLFLQEHQCLSEERLERFLSKALEASNYGVSILNNASASWNWDFTSSLFFASTVLSTTVGLHSDLENTTTITHRSIKAQLPLDLLEMCELASASKIAVEIYQGRQICNFYINNTDM
Protein: Sideroflexin FSF1 (Fungal sideroflexin-1) (Q12029)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Mitochondrial amino-acid transporter that mediates transport of serine into mitochondria.
Subcellular location: Mitochondrion membrane {ECO:0000269|PubMed:16823961, ECO:0000269|PubMed:30442778}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- 5-formyltetrahydrofolate cyclo-ligase
Sequence:
MASSVPGPIDLPESRYDLSTYWGRIRHCAEISDPTMLLTTEKDLAHAREIISAYRHGELKETTPEFWRAKKQLDSTVHPDTGKTVLLPFRMSSNVLSNLVVTVGMLTPGLGTAGTVFWQWANQSLNVAVNSANANKSHPMSTSQLLTNYAAAVTASCGVALGLNNLVPRLKNISPHSKLILGRLVPFAAVVSAGIVNVFLMRGNEIRKGISVFDSNGDEVGKSKKAAFMAVGETALSRVINATPTMVIPPLILVRLQRGVLKGKSLGVQTLANLGLISVTMFSALPFALGIFPQRQAIHLNKLEPELHGKKDKDGKPIEKVYFNRGI
Protein: Phospholipid phosphatase 1 (EC 3.1.3.-) (EC 3.1.3.106) (EC 3.1.3.4) (EC 3.6.1.75) (Lipid phosphate phosphohydrolase 1) (PAP2-alpha) (Phosphatidate phosphohydrolase type 2a) (Phosphatidic acid phosphatase 2a) (PAP-2a) (PAP2a) (O88956)
Organism: Cavia porcellus (Guinea pig)
Function: Magnesium-independent phospholipid phosphatase of the plasma membrane that catalyzes the dephosphorylation of a variety of glycerolipid and sphingolipid phosphate esters including phosphatidate/PA, lysophosphatidate/LPA, diacylglycerol pyrophosphate/DGPP, sphingosine 1-phosphate/S1P and ceramide 1-phosphate/C1P. Also acts on N-oleoyl ethanolamine phosphate/N-(9Z-octadecenoyl)-ethanolamine phosphate, a potential physiological compound (By similarity). Through its extracellular phosphatase activity allows both the hydrolysis and the cellular uptake of these bioactive lipid mediators from the milieu, regulating signal transduction in different cellular processes (By similarity). It is for instance essential for the extracellular hydrolysis of S1P and subsequent conversion into intracellular S1P (By similarity). Involved in the regulation of inflammation, platelets activation, cell proliferation and migration among other processes (By similarity). May also have an intracellular activity to regulate phospholipid-mediated signaling pathways (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:O14494}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:O14494}; Multi-pass membrane protein {ECO:0000255}. Membrane raft {ECO:0000250|UniProtKB:O14494}; Multi-pass membrane protein {ECO:0000255}. Membrane, caveola {ECO:0000250|UniProtKB:Q61469}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- phosphatidate phosphatase
- phosphatidate phosphatase
- Hepatic triacylglycerol lipase
- phosphatidate phosphatase
- Acylglycerol transacylase
- 3-ketodihydrosphingosine reductase
- Sphingosine-1-phosphate lyase 1
- Diacylglycerol kinase
- sphingosine kinase
- Phospholipid phosphatase 2
Sequence:
MFDKARLPYVALDVLCVVLAGLPFAILTSRHTPFQRGIFCNDESIKYPYKEDTIPYALLGGIMIPFSIVVMIIGETLSVYCNLLHSNSFIRNNYIATIYKSIGTFLFGAAASQSLTDIAKYSIGRLRPHFLSVCDPDWSKVNCSDGYIEYYVCRGNAEKVKEGRLSFYSGHSSFSMYCMVFVALYLQARMKGDWARLLRPTLQFGLVAASIYVGLSRISDYKHHWSDVLTGLIQGAIVAILVAVYVSDFFKARNSPFQERKEEDSHTTLHETPTAGNHYRSNHQP
Protein: Procollagen-lysine,2-oxoglutarate 5-dioxygenase (Procollagen lysyl hydroxylase) (EC 1.14.11.4) (Q9VTH0)
Organism: Drosophila melanogaster (Fruit fly)
Function: Forms hydroxylysine residues in collagen type IV (By similarity). Required for the secretion of collagen type IV (vkg) from haemocytes, fat body and follicle cells.
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:20888931}. Secreted, extracellular space {ECO:0000269|PubMed:20888931}. Note=Detected in the ER of fat body cells and haemocytes. Also detected in small puncta in the extracellular space, particularly in the region surrounding the haemocytes. {ECO:0000269|PubMed:20888931}.
Interaction partners:
- Glycosyltransferase 25 family member
- Nuclear receptor binding SET domain protein
- EG:BACR7C10.4 protein
- G9a, isoform B
- Histone-lysine N-methyltransferase E
- Histone-lysine N-methyltransferase Su
- Histone-lysine N-methyltransferase eggless
- Histone-lysine N-methyltransferase trithorax
- Histone-lysine N-methyltransferase SETD1
- Histone-lysine N-methyltransferase ash1
Sequence:
MRIQQSALLLLLLAVTSQGDAESNWNDKIKVFTVATEPTDGYTRYIRSARVYDIEVTTLGLGEEWKGGDMQKPGGGFKLNLLREAIAPYKNEPETIILFTDSYDVIITTTLDEIFEKFKESGAKILFSAEKYCWPDKSLANDYPEVEGKASRFLNSGAFIGYAPQVFALLVDPIEDTADDQLYFTKIFLDETKRAKLGLKLDVQSRLFQNLHGAKNDVKLKVDLESNQGVLQNVDFMTTPSIIHGNGLSKVDLNAYGNYLARTFNGVCLLCQENLLDLEETNLPVISLALMVTQPVPFFDQFLEGIESLNYPKEKLHLLIYSNVAFHDDDIKSFVNKHAKEYATAKFALSTDELDERQGRQLALDKARLHQSDYIFFVDADAHIDDGEVLRELLRLNKQFVAPIFSKHKELWSNFWGALSEGGYYARSHDYVDIVKRELIGMFNVPHVTSIYLVKKTAFDAISFKHKEFDPDMAMCESLRNAGIFMYASNLRIFGHLVNADDFNTTVTRPDFYTLFSNEIDWTEKYIHPNYSLQLNESNKIQQPCPDVYWFQIVSDAFCDDLVAIMEAHNGWSDGSNNDNRLEGGYEAVPTRDIHMKQVGLERLYLKFLQMFVRPLQERAFTGYFHNPPRALMNFMVRYRPDEQPSLRPHHDSSTYTINIAMNRAGIDYQGGGCRFIRYNCSVTDTKKGWMLMHPGRLTHYHEGLLVTNGTRYIMISFIDP
Protein: Cullin-associated NEDD8-dissociated protein 2 (Cullin-associated and neddylation-dissociated protein 2) (TBP-interacting protein of 120 kDa B) (TBP-interacting protein 120B) (p120 CAND2) (Q6ZQ73)
Organism: Mus musculus (Mouse)
Function: Probable assembly factor of SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complexes that promotes the exchange of the substrate-recognition F-box subunit in SCF complexes, thereby playing a key role in the cellular repertoire of SCF complexes.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Cullin-1
- E3 ubiquitin-protein ligase RBX1
- Cullin-3
Sequence:
MSTGAFYISSLLEKMTSSDKDFRFMATSDLMSELQKDSIQLDEDSERKVVRTLLRLLEDRSGEVQNLAVKCLGPLVGKVKEYQVENIVDTLCANMRSDKEQLRDIAGIGLKTVLSELPPAATGSGLAINVCRKITGQLTSAIAQQEDVAVQLEALDILSDMLSRLGAPLGTFHASLLHCLLPQLSSPRLAVRKRTVVALGHLAAACSTDLFVELADHLVDRLPGPRAPASPAAIRTLIQCLGSVGRQAGHRLGAHLDRLVPMVEEFCNLDDDELRESCLQAFEAFLRKCPKEMDPHVPNVTSLCLQYMKHDPNYDHDSDDEEQMETEDSEFSEQESEDEYSDDDDMSWKVRRAAAKCMAALISSRPDLLPDFHCTLAPALIRRFKEREENVKADIFGAYIMLLRHTRPPKGWLEAVEEPTQTGRNLNMLRAQVPLVIKALQRQLKDRNVRTRQGCFNLFTELAGVLPGSLAEHMAVLVSGIVFSLADYSSSSTIRMDALAFLQGLLGTEPAEAFHPHLPTLLPPVMACVADPFYKVAAEALLVLQELVRTLWPLDRPRLLDPEPYVGEMSTATLARLRATDLDQEVKERAISCVGHLVGHLGDRLGDDLEPTLMLLLDRLRNEITRLPAVKALTLVAMSPLRLDLQPILAEALPILASFLRKNQRALRLATLAALDALAQSQGLGLPPPAVRTVLTELPALVSENDMHVAQLAVDFLTTVTQTQPSSLVEVSGPVLGELLQLLHSPLLPAGVLAATEGFLQALVGTRPPCVEYSELISLLTAPVYNQVGDGGPGLHKQVFHSLARCVAALSAACPQEAAGTASRLVCDAKSPHSSTGVKVLAFLSLAEVGQVAGPGPQRELKTVLLEALGSPSEDVRAAAAYALGRVGAGNLPDFLPFLLAQIEAQPRRQYLLLHALREALGAAQPDNLKPYVEDVWALLFQRCESPEEGTRCVVAECIGKLVFVNPPYLLPRFRKQLAAGQPYTRSTVITAVKFLISDQPHSIDPLLKSFIAEFMESLQDPDLNVRRATLTFFNSAVHNKPSLVRDLLDDILPLLYQETKIRRDLIREVEMGPFKHTVDDGLDVRKAAFECMYSLLESCLGQLDMCEFLNHVEDGLKDHYDIRMLTFIMLARLATLCPAPVLQRVDRLIEPLRATCTAKVKAGSVKQELEKQEELKRSAMRAVAALLTNPEVRKSPTVADFSAQIRSNPELTTLFESIQKDTASGPSTDSMELS
Protein: Protein E7 (Q6TY28)
Organism: Human papillomavirus type 96
Subcellular location: Host cytoplasm {ECO:0000256|HAMAP-Rule:MF_04004}. Host nucleus {ECO:0000256|HAMAP-Rule:MF_04004}. Note=Predominantly found in the host nucleus. {ECO:0000256|HAMAP-Rule:MF_04004}.
Interaction partners:
Sequence:
MIGKEATIPDIKLELQDLVLPIDLHCDEELTEEQSENLSESTVAEVEPQRTLYKIVVPCGGCDSRLKIYVSATQFGIRSLEDLLLEEPSLLCPACRNGR
Protein: 1,3-beta-glucanosyltransferase gas5 (O13692)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Splits internally a 1,3-beta-glucan molecule and transfers the newly generated reducing end (the donor) to the non-reducing end of another 1,3-beta-glucan molecule (the acceptor) forming a 1,3-beta linkage, resulting in the elongation of 1,3-beta-glucan chains in the cell wall.
Subcellular location: Secreted, cell wall {ECO:0000269|PubMed:17230583}. Membrane {ECO:0000269|PubMed:17230583}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:17230583}. Note=Covalently-linked GPI-modified cell wall protein (GPI-CWP).
Interaction partners:
- Cell wall protein ecm33
- Alkali-sensitive linkage protein 1
- Uncharacterized WD repeat-containing protein C17D11.16
Sequence:
MNFLHFLTTSLLLLGGSRLALADSASSAIKIKGNAFFNSDTNERFYVRGVDYQPGGSSTLVDPLADTSICKRDLPYLQGLNINTIRVYQVDNSANHDECMSALQDAGIYVILDLATSSNSISRLDAASSYNAVFLQGIFATIDAFKNYTNVLGFFAGNEVANTAENSATTTWVKAALRDAKEYISKNSDRDIPVGYSAADVAEIRVQCADFFACGNSSVRADFYGMNMYEWCGADSSFTISGYDQRMEEFANYSIPLFLSEYGCNDVTKESDGTPDRPFDEVDAIFSSEMSSVFSGGLVYQYSEEGNNYGLVVIDGDNVTISKNYETLKEKYASAANYTGDGDYSSSPATLTCPADDSYFTSFPLPTMPSEAKGFIESGAGQPLGFNAPSNQEFSANATALVSPGPHSVSTTINTNIVQATISQSSTSGSSSGSSSASTTASSSSVSSGSSISSGSSSMSTSYTSASGSSAHSSGSSSGSSSATSSASTFNLSRFYVFAGILAISGLVFA