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Q9UBP9

- GULP1_HUMAN

UniProt

Q9UBP9 - GULP1_HUMAN

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Protein
PTB domain-containing engulfment adapter protein 1
Gene
GULP1, CED6, GULP
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

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 1
PRO_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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 176156PID
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili158 – 20245 Reviewed prediction
Add
BLAST

Sequence similaritiesi

Belongs to the ced-6 family.
Contains 1 PID domain.

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei31 – 133103Missing in isoform 3.
VSP_044703Add
BLAST
Alternative sequencei134 – 16734AEEIT…RKQIA → VSIPDVVGWFVLFYKPGIVL LLALAKYLKMNNFL in isoform 2.
VSP_027250Add
BLAST
Alternative sequencei168 – 304137Missing in isoform 2.
VSP_027251Add
BLAST
Alternative sequencei282 – 30423EGFKM…LDSRC → RQRWRGSKWD in isoform 4.
VSP_045540Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti292 – 2921G → S in BAG60802. 1 Publication

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 99 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

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