wanglab/gogpt-training-data huggingface dataset:
Protein: Semaphorin-6D (Q76KF0)
Organism: Mus musculus (Mouse)
Function: Shows growth cone collapsing activity on dorsal root ganglion (DRG) neurons in vitro. May be a stop signal for the DRG neurons in their target areas, and possibly also for other neurons. May also be involved in the maintenance and remodeling of neuronal connections (By similarity).
Subcellular location: Cell membrane {ECO:0000305|PubMed:16715077}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Plexin-A1
- Plexin-A4
- Plexin-A2
- Triggering receptor expressed on myeloid cells 2
- TYRO protein tyrosine kinase-binding protein
- Neuronal cell adhesion molecule
- Plexin-A3
- Plexin-C1
Sequence:
MGFLLLWFCVLFLLVSRLRAVSFPEDDEPLNTVDYHYSRQYPVFRGRPSGNESQHRLDFQLMLKIRDTLYIAGRDQVYTVNLNEIPQTEVIPSKKLTWRSRQQDRENCAMKGKHKDECHNFIKVFVPRNDEMVFVCGTNAFNPMCRYYRLRTLEYDGEEISGLARCPFDARQTNVALFADGKLYSATVADFLASDAVIYRSMGDGSALRTIKYDSKWIKEPHFLHAIEYGNYVYFFFREIAVEHNNLGKAVYSRVARICKNDMGGSQRVLEKHWTSFLKARLNCSVPGDSFFYFDVLQSITDIIQINGIPTVVGVFTTQLNSIPGSAVCAFSMDDIEKVFKGRFKEQKTPDSVWTAVPEDKVPKPRPGCCAKHGLAEAYKTSIDFPDDTLAFIKSHPLMDSAVPPIADEPWFTKTRVRYRLTAIEVDRSAGPYQNYTVIFVGSEAGVVLKVLAKTSPFSLNDSVLLEEIEAYNPAKCSAESEEDRKVVSLQLDKDHHALYVAFSSCVVRIPLSRCERYGSCKKSCIASRDPYCGWLSQGVCERVTLGMLPGGYEQDTEYGNTAHLGDCHESLPPSTTPDYKIFGGPTSDMEVSSSSVTTVASSPEITSKVIDTWRPKLTSSRKFVVQDDPNTSDFTDTISGIPKGVRWEVQSGESNQMVHMNVLITCVFAAFVLGAFIAGVAVYCYRDMFVRKNRKIHKDAESAQSCTDSSGSFAKLNGLFDSPVKEYQQNIDSPKLYSNLLTSRKELPPNTDTKSMAVDHRGQPPELAALPTPESTPVLHQKTLQAMKSHSEKAHSHGASRKEHPQFFPSSPPPHSPLSHGHIPSAIVLPNATHDYNTSFSNSNAHKAEKKLQSMDHPLTKSSSKREHRRSVDSRNTLNDLLKHLNDPNSNPKAILGEIHMAHQTLMLDPVGPMAEVPPKVPNREASLYSPPSTLPRNSPTKRVDVPTTPGVPMTSLERQRGYHKNSSQRHSISAVPKNLNSPNGVLLSRQPSMNRGGYMPTPTGAKVDYIQGTPVSVHLQPSLSRQSSYTSNGTLPRTGLKRTPSLKPDVPPKPSFVPQTTSVRPLNKYTY
Protein: D-beta-hydroxybutyrate dehydrogenase, mitochondrial (EC 1.1.1.30) (3-hydroxybutyrate dehydrogenase) (A0A384MTY4)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004273}. Mitochondrion matrix {ECO:0000256|ARBA:ARBA00004305}.
Interaction partners:
Sequence:
MLATRLSRPLSRLPGKTLSACDRENGARRPLLLGSTSFIPIGRRTYASAAEPVGSKAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLNSDRLRTVQLNVCSSEEVEKVVEIVRSSLKDPEKGMWGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAKGRVVNISSMLGRMANPARSPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPGNFIAATSLYSPESIQAIAKKMWEELPEVVRKDYGKKYFDEKIAKMETYCSSGSTDTSPVIDAVTHALTATTPYTRYHPMDYYWWLRMQIMTHLPGAISDMIYIR
Protein: 2-methoxy-6-polyprenyl-1,4-benzoquinol methylase, mitochondrial (EC 2.1.1.201) (Ubiquinone biosynthesis methyltransferase COQ5) (P87230)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Methyltransferase required for the conversion of 2-polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2).
Subcellular location: Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03191, ECO:0000269|PubMed:24911838}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03191}; Matrix side {ECO:0000255|HAMAP-Rule:MF_03191}.
Interaction partners:
- 5-demethoxyubiquinone hydroxylase, mitochondrial
- Ubiquinone biosynthesis monooxygenase COQ6, mitochondrial
- Ubiquinone biosynthesis O-methyltransferase, mitochondrial
- Ubiquinone biosynthesis protein coq9
- Atypical kinase COQ8, mitochondrial
- 4-hydroxybenzoate polyprenyltransferase, mitochondrial
- Ubiquinone biosynthesis protein coq4, mitochondrial
- Ubiquinone biosynthesis protein coq11
- Decaprenyl-diphosphate synthase subunit 2
- Thiol-specific monooxygenase
Sequence:
MSRLRAPVAKFLADGLKGIRSTALAGSRLSNCRYTSTSSKDTDTSSHMTHFGFKDVPEDEKEHLVKNVFSSVAKKYDEMNDAMSLGIHRLWKNIFVSRLNPGNSTVPMKILDVAGGTGDIAFRILNHATNHNGDRNTRVIVADINPDMLSVGLRRSKKTPYYDSGRVEFIEQNAEILDKIPDNSIDMYTIAFGIRNCTHIPKVLEQAYRVLKPGGVFSCLEFSKVYPAPLAELYRQYSFKILPLLGTIIAGDSQSYEYLVESIERFPDAKTFAKMIEDAGFTLAGETGYETLSFGIAAIHTGIKL
Protein: Interleukin-13 (IL-13) (T-cell activation protein P600) (P20109)
Organism: Mus musculus (Mouse)
Function: Cytokine that plays important roles in allergic inflammation and immune response to parasite infection. Synergizes with IL2 in regulating interferon-gamma synthesis. Stimulates B-cell proliferation, and activation of eosinophils, basophils, and mast cells (By similarity). Plays an important role in controlling IL33 activity by modulating the production of transmembrane and soluble forms of interleukin-1 receptor-like 1/IL1RL1. Displays the capacity to antagonize Th1-driven proinflammatory immune response and downregulates synthesis of many proinflammatory cytokines including IL1, IL6, IL10, IL12 and TNF-alpha through a mechanism that partially involves suppression of NF-kappa-B (By similarity). Functions also on nonhematopoietic cells, including endothelial cells where it induces vascular cell adhesion protein 1/VCAM1, which is important in the recruitment of eosinophils. Exerts its biological effects through its receptors which comprises the IL4R chain and the IL13RA1 chain, to activate JAK1 and TYK2, leading to the activation of STAT6. Aside from IL13RA1, another receptor IL13RA2 acts as a high affinity decoy for IL13 and mediates internalization and depletion of extracellular IL13.
Subcellular location: Secreted.
Interaction partners:
- Interleukin-4 receptor subunit alpha
- Interleukin-13 receptor subunit alpha-1
- Interleukin-13 receptor subunit alpha-2
- Interleukin-4
- Interleukin-5
- Interferon gamma
- Interleukin-10
- Cytokine receptor common subunit gamma
- Interleukin-17A
- Interleukin-9
Sequence:
MALWVTAVLALACLGGLAAPGPVPRSVSLPLTLKELIEELSNITQDQTPLCNGSMVWSVDLAAGGFCVALDSLTNISNCNAIYRTQRILHGLCNRKAPTTVSSLPDTKIEVAHFITKLLSYTKQLFRHGPF
Protein: MUC1 isoform M9 (A6ZIE3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTPGTQSPFFLLLLLTVLTGSGHASSTPGGEKETSATQRSSVPSSTEKNAVSMTSSVLSSHSPGSGSSTTQGQDVTLAPATEPASGSAATWGQDVTSVPVTRPALGSTTPPAGVPGWGIALLVLVCVLVALAIVYLIALAVCQCRRKNYGQLDIFPARDTYHPMSEYPTYHTHGRYVPPSSTDRSPYEKVSAGNGGSSLSYTNPAVAATSANL
Protein: Glycine betaine uptake system ATP-binding protein YehX (EC 7.4.2.-) (P33360)
Organism: Escherichia coli (strain K12)
Function: Part of an ABC transporter complex involved in low-affinity glycine betaine uptake. Probably responsible for energy coupling to the transport system.
Interaction partners:
- Glycine betaine uptake system permease protein YehW
- Glycine betaine-binding protein YehZ
- Glycine betaine uptake system permease protein YehY
- Nickel import ATP-binding protein NikD
- Putrescine export system ATP-binding protein SapD
- Glutathione/L-cysteine transport system ATP-binding/permease protein CydD
- Probable multidrug ABC transporter permease YbhS
- L-cystine transport system permease protein TcyL
- Uncharacterized transporter YeaV
- Glycine betaine/proline betaine transport system permease protein ProW
Sequence:
MIEFSHVSKLFGAQKAVNDLNLNFQEGSFSVLIGTSGSGKSTTLKMINRLVEHDSGEIRFAGEEIRSLPVLELRRRMGYAIQSIGLFPHWSVAQNIATVPQLQKWSRARIDDRIDELMALLGLESNLRERYPHQLSGGQQQRVGVARALAADPQVLLMDEPFGALDPVTRGALQQEMTRIHRLLGRTIVLVTHDIDEALRLAEHLVLMDHGEVVQQGNPLTMLTRPANDFVRQFFGRSELGVRLLSLRSVADYVRREERADGEALAEEMTLRDALSLFVARGCEVLPVVNMQGQPCGTLHFQDLLVEA
Protein: MIP24941p (Q9I7V4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Uncharacterized protein, isoform A
Sequence:
MCNFHLLLILATALGDLACATPSLRSASDPEKILNNLAQLRQSSFLDWIQSILGPEVPAEWSSPAKRECAECSCGNINTRHRIVGGQETEVHEYPWMIMLMWFGNFYCGASLVNDQYALTAAHCVNGFYHRLITVRLLEHNRQDSHVKIVDRRVSRVLIHPKYSTRNFDSDIALIRFNEPVRLGIDMHPVCMPTPSENYAGQTAVVTGWGALSEGGPISDTLQEVEVPILSQEECRNSNYGESKITDNMICAGYVEQGGKDSCQGDSGGPMHVLGSGDAYQLAGIVSWGEGCAKPNAPGVYTRVGSFNDWIAENTRDACSCAQPEAAGEPASPMETTEQGDQENTTANGAAEADPEVEEANKLI
Protein: Protein-lysine myristoyltransferase HlyC (EC 2.3.1.-) (Hemolysin C) (Hemolysin-activating lysine-acyltransferase HlyC) (Toxin-activating protein C, PHLY152) (P06736)
Organism: Escherichia coli
Function: Protein-lysine myristoyltransferase that catalyzes myristoylation of the protoxin (HlyA) at two internal lysine residues, thereby converting it to the active toxin.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
Sequence:
MNINKPLEILGHVSWLWASSPLHRNWPVSLFAINVLPAIQANQYVLLTRDDYPVAYCSWANLSLENEIKYLNDVTSLVAEDWTSGDRKWFIDWIAPFGDNGALYKYMRKKFPDELFRAIRVDPKTHVGKVSEFHGGKIDKQLANKIFKQYHHELITEVKRKSDFNFSLTG
Protein: Prolyl 4-hydroxylase subunit alpha-3 (4-PH alpha-3) (EC 1.14.11.2) (Procollagen-proline,2-oxoglutarate-4-dioxygenase subunit alpha-3) (Q6W3E9)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000250}.
Interaction partners:
- Protein disulfide-isomerase
- Prolyl 4-hydroxylase subunit alpha 2
- Prolyl 4-hydroxylase subunit alpha-1
- Pyrroline-5-carboxylate reductase 3
- Proline dehydrogenase
- Pyrroline-5-carboxylate reductase
- Pyrroline-5-carboxylate reductase 2
- Cytosol aminopeptidase
- Egl nine homolog 1
- Prolyl hydroxylase EGLN3
Sequence:
MGPGARLAALLVLLKLGVGDPAAAAGREDTFSALTSVARALAPERRLLGTLRRYLRGEEARLRDLTRFYDKVLSLHEDLKIPVVNPLLVFTLIKRLPSDWRNVVHSLEATENIRAPKDGYEKVEQDLPAFEDLEGAARALMRLQDAYMLNVKGLAQGVFQRVTGSSITDLYSPRQLFSLTADDCFQVGKVAYDTGDYYHAIPWLEEAVSLFRRSYGEWKTEDEASLEDALDYLAFACYQVGNVSCALSLSREFLVYSPDNKRMARNVLKYERLLAENGHLMAAETAIQRPNVPHLQTRDTYEGLCQTLGSQPTHYQIPSLYCSYETNSSPYLLLQPARKEVIHLRPLVALYHDFVSDEEAQKIRELAEPWLQRSVVASGEKQLQVEYRISKSAWLKDTVDPVLVTLDRRIAALTGLDIQPPYAEYLQVVNYGIGGHYEPHFDHATSPSSPLYKMKSGNRAATLMIYLSSVEAGGATAFIYGNFSVPVVKNAALFWWNLHRSGEGDDDTLHAGCPVLVGDKWVANKWIHEYGQEFRRPCDTNPED
Protein: Uncharacterized HTH-type transcriptional regulator PA4778 (Q9HV30)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Copper resistance protein B
- Copper resistance protein A
- HMA domain-containing protein
- ArsR protein
- Copper transport outer membrane porin OprC
- Uncharacterized protein
- Four-helix bundle copper-binding protein
Sequence:
MNIGEAAKKSGLTPKMIRYYESIELLRPAGRSASGYRHYNENDLHTLAFIRRSRDLGFSLDEVGKLLTLWQDRQRASADVKALAAQHVRELNRKIEELSTLRDTLQDLVEHCQGDHRPDCPILKDLASGCCH
Protein: Axoneme-associated protein mst101(2) (A1Z9G6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MVFLGRHLSRSLAYHLKQPSWNRLFLKPRTNLHHVSVYLGQPRILSHKSDAYDDLSSKYRMKTNCMINQAIDQSEPQKFYYHHRIYKASQLKDRVFKRNIDQICLNQQRSFCKEADKDSCYCKKLEDENCALQPLPKPEPKKKCSRISRKRKHLLEQKKKAAKSEAPPESQSEPNLDEAVDELKFSCMLASEKKDCERKQYKALCEELRKSKPQGDPKSVDSLVKCMLSGIQKACIVHAEKIVYQKKFAEQIAIEEAKRKEREKKEGKPLDCTKPSEDDETGAKNKAEKKKAKEKAEIKRLLKEIKGKCKKQREEAERKKKEEAELNKKCKEAAAKKKCEELEAKKKCEEAAAKKKCEEAAAKKKCEEAAAKKKCEEAAAKKKCEEAAAKKKCEEAAAKKKCEEAAAKKKCEEAAAKKKCEKSAPKNKCQESAAKNKCKEAAAKKNCAEAEAKKKCEEAAAKKKCEEAAAKKKCEEAAAKKKCEEAAAKKKCEEGAAKKKCEEKAEIKKCVESDRKKNSANDAAMKKCEEDKKKKSQEAEKKTKSEQAALQKKCAEAKKNKAREAEKKKKTAESERKKDCDLAEFKKRCNELKKKIAEANCEEKKGK
Protein: GDP-4-keto-6-deoxy-D-mannose 3-dehydratase (EC 4.2.1.168) (G4WJD4)
Organism: Yersinia pseudotuberculosis
Function: Involved in the biosynthesis of L-colitose, a 3,6-dideoxyhexose present in the O-antigen region of lipopolysaccharides (LPS), where it serves as an antigenic determinant and is vital for bacterial defense and survival. Catalyzes the removal of the C3'-hydroxyl group from GDP-4-keto-6-deoxy-D-mannose via a combined transamination-deoxygenation reaction. The catalysis is initiated by a transamination step in which pyridoxal 5'-phosphate (PLP) is converted to pyridoxamine 5'-phosphate (PMP) in the presence of L-glutamate. This coenzyme then forms a Schiff base with GDP-4-keto-6-deoxy-D-mannose and the resulting adduct undergoes a PMP-mediated beta-dehydration reaction to give a sugar enamine intermediate, which after tautomerization and hydrolysis to release ammonia yields GDP-4-keto-3,6-dideoxy-D-mannose as a product.
Subcellular location: Cell membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MRKIMINFPLASSTWDEKELNAIQRIIDSNMFTMGESVKQYEKDFAEYFGSKYSVMVSSGSTANLLMIAALFFTKKPKFKRGDEVIVPAVSWSTTYFPLQQYGLNVRFVDIDKKTLNIDLDKLKSAITEKTKAILAVNLLGNPNDFDAITKITEGKDIFILEDNCESMGARLNGKQAGTYGLMGTFSSFFSHHIATMEGGCVITDDEELYHILLCIRAHGWTRNLPEFNHITGQKSIDPFEESFKFVLPGYNVRPLEMSGAIGIEQLKKLPSFIEMRRKNATIFKELFSSHPYIDIQQETGESSWFGFALILKESSPITRAELVKKLIEAGIECRPIVTGNFLKNKEVLKFFDYTIAGEVTDAEYIDKHGLFVGNHQIDLSEQIKNLFNILKK
Protein: THO complex subunit 6 (Functional spliceosome-associated protein 35) (fSAP35) (WD repeat-containing protein 58) (Q86W42)
Organism: Homo sapiens (Human)
Function: Acts as component of the THO subcomplex of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and which specifically associates with spliced mRNA and not with unspliced pre-mRNA. TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NFX1 pathway. The TREX complex is essential for the export of Kaposi's sarcoma-associated herpesvirus (KSHV) intronless mRNAs and infectious virus production. Plays a role in apoptosis negative control involved in brain development.
Subcellular location: Nucleus {ECO:0000269|PubMed:23621916}. Nucleus speckle {ECO:0000305|PubMed:23621916}.
Interaction partners:
- THO complex subunit 5
- THO complex subunit 2
- THO complex subunit 3
- Spliceosome RNA helicase DDX39B
- THO complex subunit 7
- THO complex subunit 1
- THO complex subunit 4
- SAP domain-containing ribonucleoprotein
- Chromatin target of PRMT1 protein
- Nuclear cap-binding protein subunit 3
Sequence:
MERAVPLAVPLGQTEVFQALQRLHMTIFSQSVSPCGKFLAAGNNYGQIAIFSLSSALSSEAKEESKKPVVTFQAHDGPVYSMVSTDRHLLSAGDGEVKAWLWAEMLKKGCKELWRRQPPYRTSLEVPEINALLLVPKENSLILAGGDCQLHTMDLETGTFTRVLRGHTDYIHCLALRERSPEVLSGGEDGAVRLWDLRTAKEVQTIEVYKHEECSRPHNGRWIGCLATDSDWMVCGGGPALTLWHLRSSTPTTIFPIRAPQKHVTFYQDLILSAGQGRCVNQWQLSGELKAQVPGSSPGLLSLSLNQQPAAPECKVLTAAGNSCRVDVFTNLGYRAFSLSF
Protein: GAS2-like protein 3 (Growth arrest-specific protein 2-like 3) (Q3UWW6)
Organism: Mus musculus (Mouse)
Function: Cytoskeletal linker protein. May promote and stabilize the formation of the actin and microtubule network (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q86XJ1}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q86XJ1}. Note=Localizes to microtubule and actin cytoskeletons. {ECO:0000250|UniProtKB:Q86XJ1}.
Interaction partners:
- G2/M phase-specific E3 ubiquitin-protein ligase
- WD repeat-containing protein 76
Sequence:
MTMQPAIQVWFGEDLPLSPRCPLTPRHGPGLADVCQYDEWIAVRHEATLLPMQEDLSIWLSGLLGVDIKAERLLEELDNGVLLCQLINVLQNMVKGCHSDEPGNFPMRKVPCKKDAASGSFFARDNTANFLHWCRHIGVDETYLFESEGLVLHKDPRQVYLCLLEIGRIVSRYGVEPPVLVKLEKEIELEETLLNASGLEESISIPKSCCQQEELHEAVKHIAEDPPCSCSHRFSIEYLSEGRYRLGEKILFIRMLHGKHVMVRVGGGWDTLQGFLLKYDPCRILQFATLEQKILAFQKGVSNESVPDSPARTPKPPEMNPLSAVNMFQKQNLRPGTPVSVPKNKEKQVRLPGARLPASSVKGNLASPSTRAKRPDSPASFPHPKVTSLKDAAKKTTAPSNSVSQSLASPNPGSKPSTAQCASESSRKCVTFPKTAQTKAIPAQNSRDLSKSRLLPSKSPGKMEPKHLKHNHLSSRDESRINLSSKSPKLPKGAMHGRPNPSPFQPPAKVTKPSSKTGAIGLGTQSQPPTRTPRSGAVSAQRLQSTLNLNSPASVCSGSSAKATQGSKGKNTVSVAKKQPQSKGVCRNPGPGSSKSPGRTPLSIVTVPQSATKTETVSKSAKTAMKGQYSAKGPPKSSKPPTSFRDPPSSGKGADSGDKMPTARKKEEDDHYFVMTGNKKLRK
Protein: Clathrin heavy chain (P29742)
Organism: Drosophila melanogaster (Fruit fly)
Function: Clathrin is the major protein of the polyhedral coat of coated pits and vesicles.
Subcellular location: Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Membrane, coated pit; Peripheral membrane protein; Cytoplasmic side. Note=Cytoplasmic face of coated pits and vesicles.
Interaction partners:
- Cyclin-G-associated kinase
- Clathrin light chain
- AP complex subunit beta
- AP-1 complex subunit gamma
- AP-2 complex subunit alpha
- Adaptor protein complex 2, mu subunit, isoform A
- FI19443p1
- Amphiphysin
- Huntingtin interacting protein 1
- Dynamin
Sequence:
MTQPLPIRFQEHLQLTNVGINANSFSFSTLTMESDKFICVREKVNDTAQVVIIDMNDATNPTRRPISADSAIMNPASKVIALKAQKTLQIFNIEMKSKMKAHTMNEDVVFWKWISLNTLALVTETSVFHWSMEGDSMPQKMFDRHSSLNGCQIINYRCNASQQWLLLVGISALPSRVAGAMQLYSVERKVSQAIEGHAASFATFKIDANKEPTTLFCFAVRTATGGKLHIIEVGAPPNGNQPFAKKAVDVFFPPEAQNDFPVAMQVSAKYDTIYLITKYGYIHLYDMETATCIYMNRISADTIFVTAPHEASGGIIGVNRKGQVLSVTVDEEQIIPYINTVLQNPDLALRMAVRNNLAGAEDLFVRKFNKLFTAGQYAEAAKVAALAPKAILRTPQTIQRFQQVQTPAGSTTPPLLQYFGILLDQGKLNKFESLELCRPVLLQGKKQLCEKWLKEEKLECSEELGDLVKASDLTLALSIYLRANVPNKVIQCFAETGQFQKIVLYAKKVNYTPDYVFLLRSVMRSNPEQGAGFASMLVAEEEPLADINQIVDIFMEHSMVQQCTAFLLDALKHNRPAEGALQTRLLEMNLMSAPQVADAILGNAMFTHYDRAHIAQLCEKAGLLQRALEHYTDLYDIKRAVVHTHMLNAEWLVSFFGTLSVEDSLECLKAMLTANLRQNLQICVQIATKYHEQLTNKALIDLFEGFKSYDGLFYFLSSIVNFSQDPEVHFKYIQAACKTNQIKEVERICRESNCYNPERVKNFLKEAKLTDQLPLIIVCDRFDFVHDLVLYLYRNNLQKYIEIYVQKVNPSRLPVVVGGLLDVDCSEDIIKNLILVVKGQFSTDELVEEVEKRNRLKLLLPWLESRVHEGCVEPATHNALAKIYIDSNNNPERYLKENQYYDSRVVGRYCEKRDPHLACVAYERGLCDRELIAVCNENSLFKSEARYLVGRRDAELWAEVLSESNPYKRQLIDQVVQTALSETQDPDDISVTVKAFMTADLPNELIELLEKIILDSSVFSDHRNLQNLLILTAIKADRTRVMDYINRLENYDAPDIANIAISNQLYEEAFAIFKKFDVNTSAIQVLIDQVNNLERANEFAERCNEPAVWSQLAKAQLQQGLVKEAIDSYIKADDPSAYVDVVDVASKVESWDDLVRYLQMARKKARESYIESELIYAYARTGRLADLEEFISGPNHADIQKIGNRCFSDGMYDAAKLLYNNVSNFARLAITLVYLKEFQGAVDSARKANSTRTWKEVCFACVDAEEFRLAQMCGLHIVVHADELEDLINYYQNRGYFDELIALLESALGLERAHMGMFTELAILYSKFKPSKMREHLELFWSRVNIPKVLRAAESAHLWSELVFLYDKYEEYDNAVLAMMAHPTEAWREGHFKDIITKVANIELYYKAIEFYLDFKPLLLNDMLLVLAPRMDHTRAVSYFSKTGYLPLVKPYLRSVQSLNNKAINEALNGLLIDEEDYQGLRNSIDGFDNFDNIALAQKLEKHELTEFRRIAAYLYKGNNRWKQSVELCKKDKLYKDAMEYAAESCKQDIAEELLGWFLERDAYDCFAACLYQCYDLLRPDVILELAWKHKIVDFAMPYLIQVLREYTTKVDKLELNEAQREKEDDSTEHKNIIQMEPQLMITAGPAMGIPPQYAQNYPPGAATVTAAGGRNMGYPYL
Protein: Flagellar assembly protein FliH (P15934)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: Needed for flagellar regrowth and assembly.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Flagellar motor switch protein FliM
- Flagellar biosynthesis protein FlhA
- Flagellar motor switch protein FliG
- Flagellar motor switch protein FliN
- Flagellar M-ring protein
- Flagellum-specific ATP synthase
- Flagellar FliJ protein
- Flagellar protein FliO
- Flagellar hook-length control protein
- Flagellar biosynthetic protein FliP
Sequence:
MSNELPWQVWTPDDLAPPPETFVPVEADNVTLTEDTPEPELTAEQQLEQELAQLKIQAHEQGYNAGLAEGRQKGHAQGYQEGLAQGLEQGQAQAQTQQAPIHARMQQLVSEFQNTLDALDSVIASRLMQMALEAARQVIGQTPAVDNSALIKQIQQLLQQEPLFSGKPQLRVHPDDLQRVEEMLGATLSLHGWRLRGDPTLHHGGCKVSADEGDLDASVATRWQELCRLAAPGVL
Protein: Glucosamine kinase GspK (EC 2.7.1.8) (GlcN kinase) (Q9KUA9)
Organism: Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Function: ATP-dependent kinase, which is specific for glucosamine. Does not show kinase activity with any other sugar.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11850417}.
Interaction partners:
- beta-N-acetylhexosaminidase
- Endoglucanase-related protein
- N-acetylglucosamine-6-phosphate deacetylase
- N-acetylglucosamine-6-phosphate deacetylase
- beta-N-acetylhexosaminidase
- Chitodextrinase
- Chitinase, putative
- Peptide ABC transporter, ATP-binding protein
- Glutamine--fructose-6-phosphate aminotransferase
- chitinase
Sequence:
MNYYVGIDGGGTSCRARIRNQQGEWVGEAKSGSANIMLGVEVALRSVVDAITQAAEQGGLSPDDFPSMHVGLALAGAEQKEAWHAFMQQAHPFASITLNTDAYGACLGAHLGEEGAIMIAGTGSCGILLKGGKQYVVGGREFPISDQGSGAVMGLRLIQQVLLAQDGIRPHTPLCDVVMNHFNHDIDSIVAWSKTALPRDYGQFSPQIFSHAYCGDPLAIELLKQTAADIEMFLIALHHKGAERICLMGSIAERIQDWLSPPVQQWIVKPQSDAIEGALMFAGKPEHNLYKDGL
Protein: Mating factor M secretion protein mam1 (Multiple drug resistance protein homolog) (P-glycoprotein) (P78966)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required in S.pombe M (minus) cells for production of M-factor pheromone. Involved in the transport of the farnesyl-derivation of the M-factor pheromone.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Pheromone P-factor receptor
- Leptomycin B resistance protein pmd1
- M-factor
- Carboxypeptidase sxa2
- Pro-P-factor
- Pheromone M-factor receptor
Sequence:
MHIHSDLSLPQFEHASIDPPSYSPQKSSFEEKKHNFSITNKSLETLRSQESPCSTTFPVSDRKDALLNIPTVVDDEFQHTEELAGVSSWSDFFYLFHFSDIPLIFGTLIFTCLSAALEPLMTWTTGKVFDALSQYATSQITLGKMISLINFNSLLITIFGLASCVFSFGVRFLWQYLSAIAGKRARSLCFHVLSSKSSTFYSLTESKSGLVNSVDRCIQFYEKSISLPMFHIAENLAISLSCLIISFRYSWSLTLVVLASYPIIILVVGFINSFLSSAYEKDRKSSEKAASILEKSISAIQTVIFHSMQDTEYRYFADACSTSSKSFLRFSFLDAFQGGVSQFFLYSVFFQGLWFGNHLATTKRVNVGQVVTVFGSCLSVASSLQQILPAIPDLIKGKFSSHFIKTLCESHDPIEAAKRSAAKIKSISFERGFRFDNVSFAYPSRDENLFSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGSTITLVCQQPVIFDMTIRENIIMRNENASESDFEEVCRLALVDEFALTFDQSYDTPCKEASLSGGQQQRIALARALLRDTEILILDEPTSALDPITKNLVMDAIRAHRKGKTTLVITHDMSQINNDELVLVIDKGHLIQRCARKELVLFEDFENNVSIDEKVLKEEADNPFILPNEESLLEKYWINYNESFSQLSRESLFTSLESPFTDIESPTIVSRRKIVEQRKLRMEKESFQETNVDQTFHLFDDKEHACSLTLIFKSIWKVKKLRWFFLLGLLTSLIQGASVPIFAYVISKCLNLFMQIDPSIGVAFWSSMVLVVAAGSGASYFFSHYIFSISAKIWCDHYRLLAVKVLFTQDQAWFDQIENYPLVLSKILVNNISDMRNMISSLIEEVFIAFTMAIIGIAWSFATGWRLAAVLVAVSPILCLTSRMFSYIYVSTERMCQDVVISTTSILHKTIVNLDTIKGYSVLSFFRENHKNSLRKSWEAFKRRAFWTSLGFAINNSLLYFVRALLFYCSSIFISKEFYTVEQMVQVLSLATFTLLMASTCIMSLPNVSASRIATSRVLKLSSLKPGNLHKSGYLKFPLVGKIEFDGVSFAYPDSERNHLALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYPSEDIYIDGYPLTNIDTNWLLKKVAIVDQKPHLLGSTILESLLYGVDRDINSVMDALDKTYMTEVIQNLPNGLDTPLLEFSKNFSGGQIQRLAFARALLRNPRLLILDECTSALDSKSSLLLEKTIQNLSCTVLIITHQPSLMKLADRIIVMDSGIVKESGSFDELMNRHTHFWKLIHRGEWIE
Protein: Adiponectin receptor protein (Q9N536)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Immunoglobulin domain and leucine-rich repeat-containing protein 2
- Delta
- Nuclear hormone receptor family member nhr-49
- Sterol regulatory element binding protein sbp-1
- Mediator of RNA polymerase II transcription subunit 15
- Delta
- Delta
- Acyl-CoA dehydrogenase family member 11
- Probable enoyl-CoA hydratase, mitochondrial
Sequence:
MEEDDVESATPAESQKLLQKSVRNSFDERDMVMVLDNDELIMENRNSSNLQSPLRSVTDVLREAENIITDGPLQLADTQENQNVIVDQVDVQFPNSQPSDGQRFEIIVRHSKVVEQPASQQRDESMYVTRQNRLPTLLEGIEIDNGDVPSTSKAAALPFKKGHRRAWSMPNAKGEKMTVAVIHDNHEEGGNQHRRRIVKYKLHPQRRGHEDGKHLRFVTAGHDAEIHLDHSDDDDELEVEINEEEVIIPSETGEGPRAVIKRFWEARWKATNFETLPEWLQDNEYLRTGHRPPLPSFSSCFKSIFALHTETGNIWTHMYGCVAFFGIGIWFLTRPHDQMQWVEKLIYSAFFLGAVICLGMSFLFHTVACHSIEMAKLFSKLDYTGISLLIVGSFVPWIYFAFYCRPQPMIIYNGMIIILGIAAMVVSLWDKFAEPKFRPVRAAVFIAMGLSAVVPAFHLLVVDGVHYMVEESQVHLMIMMGAMYIGGATLYATRVPERCFPGKCDIWFQSHQLFHTFVVLAAFVHYHAISQMGMHKLMKGSCPDQLKTRYGNELNPSFVGTLLGLDEPLNVRDWTPADVGL
Protein: Stromal cell-derived factor 1 (xSDF-1) (C-X-C motif chemokine 12) (Q8UUJ9)
Organism: Xenopus laevis (African clawed frog)
Function: Chemoattractant. Activates the C-X-C chemokine receptor cxcr4 to induce a rapid and transient rise in the level of intracellular calcium ions, and chemotaxis. Signaling with cxcr4 mediates the directional movement of mesodermal cells during gastrulation (Ref.2). Binds to the allosteric site (site 2) of integrins and activates them in a cxcr4-independent manner (By similarity).
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
Sequence:
MDIRTLALLSILLGTLCLTEGKPVSLVYRCPCRYFESNVPKSNIKHLKILSTSNCSLQIVARLKHNGKQICLDPKTKWIQEYLEKALNKKAKKT
Protein: F-actin-capping protein subunit alpha (P34685)
Organism: Caenorhabditis elegans
Function: F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:A0PFK5}.
Interaction partners:
- F-actin-capping protein subunit beta
- Probable dynactin subunit 2
- Actin
- Actin-related protein 10
- Dynactin subunit 1
- Dynactin subunit 5
- Dynactin subunit 4
- Dynactin subunit 6
- CARMIL pleckstrin homology domain-containing protein
- DyNactin Complex component
Sequence:
MSEISDAEKVRIASDFIKHAPPGEFNEVFNSVRMLLENDDLLKNKCVNAIAQYNVGQFVPVKLDGVAKQTLITPYNDLGNGRFYDEVSKKSFKYDHVRKEAADLQPHPAESGITEQWRQALQTQLDIYIDDHYAKSGTGVVFARNGVFTICIESHQFQPKNFCNGRWRSEWNVPVGDGKSGSQEMKGKILSQVHYYEDGNVQLFSEKEPVLKVNVSADFDKTAKEIIHAISEEETIYQNAVQENYANMSDTTFKALRRQLPVTRAKMDWNKAQTYRIGQEMK