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Protein

Golgi resident protein GCP60

Gene

ACBD3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the maintenance of Golgi structure by interacting with giantin, affecting protein transport between the endoplasmic reticulum and Golgi. Involved in hormone-induced steroid biosynthesis in testicular Leydig cells (By similarity).By similarity

GO - Molecular functioni

  1. fatty-acyl-CoA binding Source: InterPro

GO - Biological processi

  1. steroid biosynthetic process Source: UniProtKB-KW
  2. transport Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis

Names & Taxonomyi

Protein namesi
Recommended name:
Golgi resident protein GCP60
Alternative name(s):
Acyl-CoA-binding domain-containing protein 3
Golgi complex-associated protein 1
Short name:
GOCAP1
Golgi phosphoprotein 1
Short name:
GOLPH1
PBR- and PKA-associated protein 7
Peripheral benzodiazepine receptor-associated protein PAP7
Gene namesi
Name:ACBD3
Synonyms:GCP60, GOCAP1, GOLPH1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:15453. ACBD3.

Subcellular locationi

Golgi apparatus membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Mitochondrion By similarity
Note: Also mitochondrial (via its interaction with PBR).By similarity

GO - Cellular componenti

  1. Golgi apparatus Source: HPA
  2. Golgi membrane Source: UniProtKB-SubCell
  3. integral component of membrane Source: InterPro
  4. membrane Source: UniProtKB
  5. mitochondrion Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane, Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28803.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 528527Golgi resident protein GCP60PRO_0000214029Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei13 – 131Phosphoserine1 Publication
Modified residuei18 – 181Phosphothreonine1 Publication
Modified residuei20 – 201Phosphoserine1 Publication
Modified residuei43 – 431Phosphoserine2 Publications
Modified residuei47 – 471Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9H3P7.
PaxDbiQ9H3P7.
PeptideAtlasiQ9H3P7.
PRIDEiQ9H3P7.

PTM databases

PhosphoSiteiQ9H3P7.

Expressioni

Tissue specificityi

Ubiquitous, with highest expression in testis and ovary.1 Publication

Gene expression databases

BgeeiQ9H3P7.
CleanExiHS_ACBD3.
ExpressionAtlasiQ9H3P7. baseline and differential.
GenevestigatoriQ9H3P7.

Organism-specific databases

HPAiHPA015594.

Interactioni

Subunit structurei

Interacts with the C-terminal cytoplasmic domain of giantin/GOLGB1. Interacts with PBR and PKA regulatory subunit RI-alpha. Does not interact with PKA regulatory subunit RI-beta nor PKA regulatory subunit RII-alpha (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
O9146421EBI-1791792,EBI-7587528From a different organism.
PI4KBQ9UBF84EBI-1791792,EBI-1053214
Ppm1lQ8BHN03EBI-1791792,EBI-7970002From a different organism.

Protein-protein interaction databases

BioGridi122262. 22 interactions.
DIPiDIP-40673N.
IntActiQ9H3P7. 12 interactions.
MINTiMINT-5003562.
STRINGi9606.ENSP00000355777.

Structurei

3D structure databases

ProteinModelPortaliQ9H3P7.
SMRiQ9H3P7. Positions 101-162, 385-524.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini83 – 17492ACBPROSITE-ProRule annotationAdd
BLAST
Domaini384 – 526143GOLDPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili174 – 25784Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi21 – 6040Pro-richAdd
BLAST
Compositional biasi182 – 24059Glu-richAdd
BLAST
Compositional biasi196 – 23843Arg-richAdd
BLAST
Compositional biasi241 – 30868Gln-richAdd
BLAST

Domaini

The GOLD domain is essential for giantin binding.

Sequence similaritiesi

Contains 1 ACB (acyl-CoA-binding) domain.PROSITE-ProRule annotation
Contains 1 GOLD domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG287879.
GeneTreeiENSGT00530000063651.
HOVERGENiHBG051712.
InParanoidiQ9H3P7.
OMAiFGVFFEW.
OrthoDBiEOG7KDFB4.
PhylomeDBiQ9H3P7.
TreeFamiTF321667.

Family and domain databases

Gene3Di1.20.80.10. 1 hit.
InterProiIPR022408. Acyl-CoA-binding_prot_CS.
IPR000582. Acyl-CoA-binding_protein.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
IPR009038. GOLD.
[Graphical view]
PfamiPF00887. ACBP. 1 hit.
PF13897. GOLD_2. 1 hit.
[Graphical view]
SUPFAMiSSF101576. SSF101576. 2 hits.
SSF47027. SSF47027. 1 hit.
PROSITEiPS00880. ACB_1. 1 hit.
PS51228. ACB_2. 1 hit.
PS50866. GOLD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9H3P7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAVLNAERL EVSVDGLTLS PDPEERPGAE GAPLLPPPLP PPSPPGSGRG
60 70 80 90 100
PGASGEQPEP GEAAAGGAAE EARRLEQRWG FGLEELYGLA LRFFKEKDGK
110 120 130 140 150
AFHPTYEEKL KLVALHKQVL MGPYNPDTCP EVGFFDVLGN DRRREWAALG
160 170 180 190 200
NMSKEDAMVE FVKLLNRCCH LFSTYVASHK IEKEEQEKKR KEEEERRRRE
210 220 230 240 250
EEERERLQKE EEKRRREEEE RLRREEEERR RIEEERLRLE QQKQQIMAAL
260 270 280 290 300
NSQTAVQFQQ YAAQQYPGNY EQQQILIRQL QEQHYQQYMQ QLYQVQLAQQ
310 320 330 340 350
QAALQKQQEV VVAGSSLPTS SKVNATVPSN MMSVNGQAKT HTDSSEKELE
360 370 380 390 400
PEAAEEALEN GPKESLPVIA APSMWTRPQI KDFKEKIQQD ADSVITVGRG
410 420 430 440 450
EVVTVRVPTH EEGSYLFWEF ATDNYDIGFG VYFEWTDSPN TAVSVHVSES
460 470 480 490 500
SDDDEEEEEN IGCEEKAKKN ANKPLLDEIV PVYRRDCHEE VYAGSHQYPG
510 520
RGVYLLKFDN SYSLWRSKSV YYRVYYTR
Length:528
Mass (Da):60,593
Last modified:January 22, 2007 - v4
Checksum:iB36EC550F8268FC2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti93 – 931F → L in AAN60219 (Ref. 2) Curated
Sequence conflicti230 – 2301R → I in AAN60219 (Ref. 2) Curated
Sequence conflicti265 – 2651Q → R in AAN60219 (Ref. 2) Curated
Sequence conflicti333 – 3331S → P in AAN60219 (Ref. 2) Curated
Sequence conflicti384 – 39714KEKIQ…SVITV → QREDSAGCRFRDYS (Ref. 2) CuratedAdd
BLAST
Sequence conflicti425 – 4251Y → C in AAN60219 (Ref. 2) Curated
Sequence conflicti473 – 4731K → R in AAH60792 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti187 – 1871E → D.2 Publications
Corresponds to variant rs2306120 [ dbSNP | Ensembl ].
VAR_019615

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB043587 mRNA. Translation: BAB20592.2.
AY150218 mRNA. Translation: AAN60219.1.
AK025520 mRNA. Translation: BAB15159.1.
AK314468 mRNA. Translation: BAG37076.1.
AL592045 Genomic DNA. Translation: CAH71922.1.
CH471098 Genomic DNA. Translation: EAW69775.1.
BC034563 mRNA. Translation: AAH34563.2.
BC045533 mRNA. Translation: AAH45533.1.
BC060792 mRNA. Translation: AAH60792.1.
CCDSiCCDS1551.1.
RefSeqiNP_073572.2. NM_022735.3.
UniGeneiHs.520207.

Genome annotation databases

EnsembliENST00000366812; ENSP00000355777; ENSG00000182827.
GeneIDi64746.
KEGGihsa:64746.
UCSCiuc001hpy.3. human.

Polymorphism databases

DMDMi51316096.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB043587 mRNA. Translation: BAB20592.2.
AY150218 mRNA. Translation: AAN60219.1.
AK025520 mRNA. Translation: BAB15159.1.
AK314468 mRNA. Translation: BAG37076.1.
AL592045 Genomic DNA. Translation: CAH71922.1.
CH471098 Genomic DNA. Translation: EAW69775.1.
BC034563 mRNA. Translation: AAH34563.2.
BC045533 mRNA. Translation: AAH45533.1.
BC060792 mRNA. Translation: AAH60792.1.
CCDSiCCDS1551.1.
RefSeqiNP_073572.2. NM_022735.3.
UniGeneiHs.520207.

3D structure databases

ProteinModelPortaliQ9H3P7.
SMRiQ9H3P7. Positions 101-162, 385-524.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122262. 22 interactions.
DIPiDIP-40673N.
IntActiQ9H3P7. 12 interactions.
MINTiMINT-5003562.
STRINGi9606.ENSP00000355777.

Chemistry

BindingDBiQ9H3P7.

PTM databases

PhosphoSiteiQ9H3P7.

Polymorphism databases

DMDMi51316096.

Proteomic databases

MaxQBiQ9H3P7.
PaxDbiQ9H3P7.
PeptideAtlasiQ9H3P7.
PRIDEiQ9H3P7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000366812; ENSP00000355777; ENSG00000182827.
GeneIDi64746.
KEGGihsa:64746.
UCSCiuc001hpy.3. human.

Organism-specific databases

CTDi64746.
GeneCardsiGC01M226332.
H-InvDBHIX0159664.
HGNCiHGNC:15453. ACBD3.
HPAiHPA015594.
MIMi606809. gene.
neXtProtiNX_Q9H3P7.
PharmGKBiPA28803.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG287879.
GeneTreeiENSGT00530000063651.
HOVERGENiHBG051712.
InParanoidiQ9H3P7.
OMAiFGVFFEW.
OrthoDBiEOG7KDFB4.
PhylomeDBiQ9H3P7.
TreeFamiTF321667.

Miscellaneous databases

ChiTaRSiACBD3. human.
GeneWikiiACBD3.
GenomeRNAii64746.
NextBioi66697.
PROiQ9H3P7.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H3P7.
CleanExiHS_ACBD3.
ExpressionAtlasiQ9H3P7. baseline and differential.
GenevestigatoriQ9H3P7.

Family and domain databases

Gene3Di1.20.80.10. 1 hit.
InterProiIPR022408. Acyl-CoA-binding_prot_CS.
IPR000582. Acyl-CoA-binding_protein.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
IPR009038. GOLD.
[Graphical view]
PfamiPF00887. ACBP. 1 hit.
PF13897. GOLD_2. 1 hit.
[Graphical view]
SUPFAMiSSF101576. SSF101576. 2 hits.
SSF47027. SSF47027. 1 hit.
PROSITEiPS00880. ACB_1. 1 hit.
PS51228. ACB_2. 1 hit.
PS50866. GOLD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and characterization of a novel Golgi protein, GCP60, that interacts with the integral membrane protein giantin."
    Sohda M., Misumi Y., Yamamoto A., Yano A., Nakamura N., Ikehara Y.
    J. Biol. Chem. 276:45298-45306(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH GOLGB1, TISSUE SPECIFICITY.
    Tissue: Cervix carcinoma.
  2. Liu J., Tobin D., Tasken K., Papadopoulos V.
    Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ASP-187.
    Tissue: Placenta.
  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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ASP-187.
    Tissue: Trachea.
  4. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain and Ovary.
  7. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-9.
    Tissue: Platelet.
  8. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  10. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13 AND SER-20, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  14. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-18; SER-43 AND SER-47, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiGCP60_HUMAN
AccessioniPrimary (citable) accession number: Q9H3P7
Secondary accession number(s): B2RB29
, Q5VTJ0, Q6P9F1, Q8IZC5, Q8N4D6, Q9H6U3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 15, 2004
Last sequence update: January 22, 2007
Last modified: March 3, 2015
This is version 120 of the entry and version 4 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.