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Q9UBP9

- GULP1_HUMAN

UniProt

Q9UBP9 - GULP1_HUMAN

Protein

PTB domain-containing engulfment adapter protein 1

Gene

GULP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 100 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    May function as an adapter protein. Required for efficient phagocytosis of apoptotic cells. Modulates cellular glycosphingolipid and cholesterol transport. May play a role in the internalization and endosomal trafficking of various LRP1 ligands, such as PSAP. Increases cellular levels of GTP-bound ARF6.4 Publications

    GO - Molecular functioni

    1. signal transducer activity Source: ProtInc

    GO - Biological processi

    1. apoptotic process Source: ProtInc
    2. lipid transport Source: UniProtKB-KW
    3. phagocytosis, engulfment Source: MGI
    4. signal transduction Source: GOC

    Keywords - Biological processi

    Apoptosis, Lipid transport, Phagocytosis, Transport

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    PTB domain-containing engulfment adapter protein 1
    Alternative name(s):
    Cell death protein 6 homolog
    PTB domain adapter protein CED-6
    Protein GULP
    Gene namesi
    Name:GULP1
    Synonyms:CED6, GULP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:18649. GULP1.

    Subcellular locationi

    Cytoplasm 1 Publication
    Note: May associate with the cytoplasmic side of the plasma membrane and early endosomes.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi176 – 1761L → P: Loss of dimerization; when associated with P-183. 1 Publication
    Mutagenesisi183 – 1831L → P: Loss of dimerization; when associated with P-176. 1 Publication

    Organism-specific databases

    PharmGKBiPA134993283.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 304304PTB domain-containing engulfment adapter protein 1PRO_0000296679Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei223 – 2231Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9UBP9.
    PaxDbiQ9UBP9.
    PRIDEiQ9UBP9.

    PTM databases

    PhosphoSiteiQ9UBP9.

    Expressioni

    Tissue specificityi

    Widely expressed. Detected in macrophages, pancreas, kidney, skeletal muscle, heart, colon, intestine, lung, placenta and ovary.1 Publication

    Gene expression databases

    ArrayExpressiQ9UBP9.
    BgeeiQ9UBP9.
    CleanExiHS_GULP1.
    GenevestigatoriQ9UBP9.

    Organism-specific databases

    HPAiHPA020587.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with clathrin. Interacts with GDP-bound ARF6, but not with GTP-bound ARF6. Part of a complex composed of GULP1, ACAP1 and ARF6. Interacts with ACAP1, LRP1, MEGF10 and STAB2.5 Publications

    Protein-protein interaction databases

    BioGridi119550. 5 interactions.
    IntActiQ9UBP9. 5 interactions.
    MINTiMINT-259085.
    STRINGi9606.ENSP00000352047.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UBP9.
    SMRiQ9UBP9. Positions 18-150.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini21 – 176156PIDPROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili158 – 20245Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the ced-6 family.Curated
    Contains 1 PID domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG314249.
    HOGENOMiHOG000039986.
    HOVERGENiHBG056801.
    InParanoidiQ9UBP9.
    OMAiPFDPFSC.
    OrthoDBiEOG7RBZ90.
    PhylomeDBiQ9UBP9.
    TreeFamiTF314159.

    Family and domain databases

    Gene3Di2.30.29.30. 1 hit.
    InterProiIPR011993. PH_like_dom.
    IPR006020. PTB/PI_dom.
    [Graphical view]
    PfamiPF00640. PID. 1 hit.
    [Graphical view]
    SMARTiSM00462. PTB. 1 hit.
    [Graphical view]
    PROSITEiPS01179. PID. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9UBP9-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MNRAFSRKKD KTWMHTPEAL SKHFIPYNAK FLGSTEVEQP KGTEVVRDAV    50
    RKLKFARHIK KSEGQKIPKV ELQISIYGVK ILEPKTKEVQ HNCQLHRISF 100
    CADDKTDKRI FTFICKDSES NKHLCYVFDS EKCAEEITLT IGQAFDLAYR 150
    KFLESGGKDV ETRKQIAGLQ KRIQDLETEN MELKNKVQDL ENQLRITQVS 200
    APPAGSMTPK SPSTDIFDMI PFSPISHQSS MPTRNGTQPP PVPSRSTEIK 250
    RDLFGAEPFD PFNCGAADFP PDIQSKLDEM QEGFKMGLTL EGTVFCLDPL 300
    DSRC 304
    Length:304
    Mass (Da):34,490
    Last modified:May 1, 2000 - v1
    Checksum:i6FCDE040073DBE8B
    GO
    Isoform 2 (identifier: Q9UBP9-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         134-167: AEEITLTIGQAFDLAYRKFLESGGKDVETRKQIA → VSIPDVVGWFVLFYKPGIVLLLALAKYLKMNNFL
         168-304: Missing.

    Show »
    Length:167
    Mass (Da):19,423
    Checksum:i6A33DC720CB9A2DE
    GO
    Isoform 3 (identifier: Q9UBP9-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         31-133: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:201
    Mass (Da):22,567
    Checksum:i139143B94E5121C4
    GO
    Isoform 4 (identifier: Q9UBP9-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         282-304: EGFKMGLTLEGTVFCLDPLDSRC → RQRWRGSKWD

    Note: No experimental confirmation available.

    Show »
    Length:291
    Mass (Da):33,333
    Checksum:i2736C095A6140AB5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti292 – 2921G → S in BAG60802. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei31 – 133103Missing in isoform 3. 1 PublicationVSP_044703Add
    BLAST
    Alternative sequencei134 – 16734AEEIT…RKQIA → VSIPDVVGWFVLFYKPGIVL LLALAKYLKMNNFL in isoform 2. 1 PublicationVSP_027250Add
    BLAST
    Alternative sequencei168 – 304137Missing in isoform 2. 1 PublicationVSP_027251Add
    BLAST
    Alternative sequencei282 – 30423EGFKM…LDSRC → RQRWRGSKWD in isoform 4. 1 PublicationVSP_045540Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF200715 mRNA. Translation: AAF08006.1.
    AF191771 mRNA. Translation: AAF18975.1.
    AK055718 mRNA. No translation available.
    AK298626 mRNA. Translation: BAG60802.1.
    AK314498 mRNA. Translation: BAG37098.1.
    AC092598 Genomic DNA. Translation: AAX93242.1.
    AC125490 Genomic DNA. Translation: AAY24122.1.
    AC104131 Genomic DNA. No translation available.
    AC108493 Genomic DNA. No translation available.
    AC133606 Genomic DNA. No translation available.
    CH471058 Genomic DNA. Translation: EAX10913.1.
    CH471058 Genomic DNA. Translation: EAX10914.1.
    CH471058 Genomic DNA. Translation: EAX10915.1.
    CH471058 Genomic DNA. Translation: EAX10917.1.
    BC001103 mRNA. Translation: AAH01103.1.
    CCDSiCCDS2295.1. [Q9UBP9-1]
    CCDS58742.1. [Q9UBP9-4]
    CCDS58743.1. [Q9UBP9-3]
    RefSeqiNP_001239597.1. NM_001252668.1. [Q9UBP9-4]
    NP_001239598.1. NM_001252669.1. [Q9UBP9-3]
    NP_057399.1. NM_016315.3. [Q9UBP9-1]
    XP_006712653.1. XM_006712590.1. [Q9UBP9-1]
    UniGeneiHs.470887.
    Hs.712910.

    Genome annotation databases

    EnsembliENST00000359135; ENSP00000352047; ENSG00000144366. [Q9UBP9-1]
    ENST00000409580; ENSP00000386289; ENSG00000144366. [Q9UBP9-1]
    ENST00000409609; ENSP00000386867; ENSG00000144366. [Q9UBP9-1]
    ENST00000409637; ENSP00000386402; ENSG00000144366. [Q9UBP9-2]
    ENST00000409805; ENSP00000387171; ENSG00000144366. [Q9UBP9-3]
    ENST00000409830; ENSP00000386732; ENSG00000144366. [Q9UBP9-1]
    ENST00000409843; ENSP00000387144; ENSG00000144366. [Q9UBP9-4]
    ENST00000410051; ENSP00000387013; ENSG00000144366. [Q9UBP9-2]
    GeneIDi51454.
    KEGGihsa:51454.
    UCSCiuc002uqc.4. human. [Q9UBP9-2]
    uc002uqf.3. human. [Q9UBP9-1]

    Polymorphism databases

    DMDMi74720076.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF200715 mRNA. Translation: AAF08006.1 .
    AF191771 mRNA. Translation: AAF18975.1 .
    AK055718 mRNA. No translation available.
    AK298626 mRNA. Translation: BAG60802.1 .
    AK314498 mRNA. Translation: BAG37098.1 .
    AC092598 Genomic DNA. Translation: AAX93242.1 .
    AC125490 Genomic DNA. Translation: AAY24122.1 .
    AC104131 Genomic DNA. No translation available.
    AC108493 Genomic DNA. No translation available.
    AC133606 Genomic DNA. No translation available.
    CH471058 Genomic DNA. Translation: EAX10913.1 .
    CH471058 Genomic DNA. Translation: EAX10914.1 .
    CH471058 Genomic DNA. Translation: EAX10915.1 .
    CH471058 Genomic DNA. Translation: EAX10917.1 .
    BC001103 mRNA. Translation: AAH01103.1 .
    CCDSi CCDS2295.1. [Q9UBP9-1 ]
    CCDS58742.1. [Q9UBP9-4 ]
    CCDS58743.1. [Q9UBP9-3 ]
    RefSeqi NP_001239597.1. NM_001252668.1. [Q9UBP9-4 ]
    NP_001239598.1. NM_001252669.1. [Q9UBP9-3 ]
    NP_057399.1. NM_016315.3. [Q9UBP9-1 ]
    XP_006712653.1. XM_006712590.1. [Q9UBP9-1 ]
    UniGenei Hs.470887.
    Hs.712910.

    3D structure databases

    ProteinModelPortali Q9UBP9.
    SMRi Q9UBP9. Positions 18-150.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119550. 5 interactions.
    IntActi Q9UBP9. 5 interactions.
    MINTi MINT-259085.
    STRINGi 9606.ENSP00000352047.

    PTM databases

    PhosphoSitei Q9UBP9.

    Polymorphism databases

    DMDMi 74720076.

    Proteomic databases

    MaxQBi Q9UBP9.
    PaxDbi Q9UBP9.
    PRIDEi Q9UBP9.

    Protocols and materials databases

    DNASUi 51454.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000359135 ; ENSP00000352047 ; ENSG00000144366 . [Q9UBP9-1 ]
    ENST00000409580 ; ENSP00000386289 ; ENSG00000144366 . [Q9UBP9-1 ]
    ENST00000409609 ; ENSP00000386867 ; ENSG00000144366 . [Q9UBP9-1 ]
    ENST00000409637 ; ENSP00000386402 ; ENSG00000144366 . [Q9UBP9-2 ]
    ENST00000409805 ; ENSP00000387171 ; ENSG00000144366 . [Q9UBP9-3 ]
    ENST00000409830 ; ENSP00000386732 ; ENSG00000144366 . [Q9UBP9-1 ]
    ENST00000409843 ; ENSP00000387144 ; ENSG00000144366 . [Q9UBP9-4 ]
    ENST00000410051 ; ENSP00000387013 ; ENSG00000144366 . [Q9UBP9-2 ]
    GeneIDi 51454.
    KEGGi hsa:51454.
    UCSCi uc002uqc.4. human. [Q9UBP9-2 ]
    uc002uqf.3. human. [Q9UBP9-1 ]

    Organism-specific databases

    CTDi 51454.
    GeneCardsi GC02P189156.
    H-InvDB HIX0022389.
    HGNCi HGNC:18649. GULP1.
    HPAi HPA020587.
    MIMi 608165. gene.
    neXtProti NX_Q9UBP9.
    PharmGKBi PA134993283.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG314249.
    HOGENOMi HOG000039986.
    HOVERGENi HBG056801.
    InParanoidi Q9UBP9.
    OMAi PFDPFSC.
    OrthoDBi EOG7RBZ90.
    PhylomeDBi Q9UBP9.
    TreeFami TF314159.

    Miscellaneous databases

    ChiTaRSi GULP1. human.
    GenomeRNAii 51454.
    NextBioi 55065.
    PROi Q9UBP9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UBP9.
    Bgeei Q9UBP9.
    CleanExi HS_GULP1.
    Genevestigatori Q9UBP9.

    Family and domain databases

    Gene3Di 2.30.29.30. 1 hit.
    InterProi IPR011993. PH_like_dom.
    IPR006020. PTB/PI_dom.
    [Graphical view ]
    Pfami PF00640. PID. 1 hit.
    [Graphical view ]
    SMARTi SM00462. PTB. 1 hit.
    [Graphical view ]
    PROSITEi PS01179. PID. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human CED-6 encodes a functional homologue of the Caenorhabditis elegans engulfment protein CED-6."
      Liu Q.A., Hengartner M.O.
      Curr. Biol. 9:1347-1350(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
    2. "The human homologue of Caenorhabditis elegans CED-6 specifically promotes phagocytosis of apoptotic cells."
      Smits E., Van Criekinge W., Plaetinck G., Bogaert T.
      Curr. Biol. 9:1351-1354(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
      Tissue: Neuroblastoma and Trachea.
    4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Placenta.
    7. "Identification and characterization of a dimerization domain in CED-6, an adapter protein involved in engulfment of apoptotic cells."
      Su H.P., Brugnera E., Van Criekinge W., Smits E., Hengartner M., Bogaert T., Ravichandran K.S.
      J. Biol. Chem. 275:9542-9549(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, MUTAGENESIS OF LEU-176 AND LEU-183.
    8. "The lipoprotein receptor-related protein-1 (LRP) adapter protein GULP mediates trafficking of the LRP ligand prosaposin, leading to sphingolipid and free cholesterol accumulation in late endosomes and impaired efflux."
      Kiss R.S., Ma Z., Nakada-Tsukui K., Brugnera E., Vassiliou G., McBride H.M., Ravichandran K.S., Marcel Y.L.
      J. Biol. Chem. 281:12081-12092(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    9. "Cooperation between engulfment receptors: the case of ABCA1 and MEGF10."
      Hamon Y., Trompier D., Ma Z., Venegas V., Pophillat M., Mignotte V., Zhou Z., Chimini G.
      PLoS ONE 1:E120-E120(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MEGF10.
    10. "Regulation of Arf6 and ACAP1 signaling by the PTB-domain-containing adaptor protein GULP."
      Ma Z., Nie Z., Luo R., Casanova J.E., Ravichandran K.S.
      Curr. Biol. 17:722-727(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ARF6 AND ACAP1, IDENTIFICATION IN A COMPLEX WITH ACAP1 AND ARF6.
    11. "MEGF10 is a mammalian ortholog of CED-1 that interacts with clathrin assembly protein complex 2 medium chain and induces large vacuole formation."
      Suzuki E., Nakayama M.
      Exp. Cell Res. 313:3729-3742(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MEGF10.
    12. "Requirement of adaptor protein GULP during stabilin-2-mediated cell corpse engulfment."
      Park S.Y., Kang K.B., Thapa N., Kim S.Y., Lee S.J., Kim I.S.
      J. Biol. Chem. 283:10593-10600(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH STAB2.
    13. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-223, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiGULP1_HUMAN
    AccessioniPrimary (citable) accession number: Q9UBP9
    Secondary accession number(s): B2RB51
    , B4DQ40, B8ZZ72, D3DPH1, E9PB86, Q53PC1, Q53RF3, Q9BVL3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 24, 2007
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 100 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3