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Protein

Palmitoyltransferase ZDHHC5

Gene

ZDHHC5

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

Functioni

Palmitoyl acyltransferase for the G-protein coupled receptor SSTR5. Also palmitoylates FLOT2 (By similarity).By similarity1 Publication

Catalytic activityi

Palmitoyl-CoA + [protein]-L-cysteine = [protein]-S-palmitoyl-L-cysteine + CoA.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei134 – 1341S-palmitoyl cysteine intermediateBy similarity

GO - Molecular functioni

GO - Biological processi

  • protein palmitoylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Names & Taxonomyi

Protein namesi
Recommended name:
Palmitoyltransferase ZDHHC5 (EC:2.3.1.225)
Alternative name(s):
Zinc finger DHHC domain-containing protein 5
Short name:
DHHC-5
Zinc finger protein 375
Gene namesi
Name:ZDHHC5
Synonyms:KIAA1748, ZNF375
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:18472. ZDHHC5.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1313CytoplasmicSequence analysisAdd
BLAST
Transmembranei14 – 3421HelicalSequence analysisAdd
BLAST
Topological domaini35 – 384ExtracellularSequence analysis
Transmembranei39 – 5921HelicalSequence analysisAdd
BLAST
Topological domaini60 – 14889CytoplasmicSequence analysisAdd
BLAST
Transmembranei149 – 16921HelicalSequence analysisAdd
BLAST
Topological domaini170 – 19122ExtracellularSequence analysisAdd
BLAST
Transmembranei192 – 21221HelicalSequence analysisAdd
BLAST
Topological domaini213 – 715503CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • cytoplasm Source: GO_Central
  • dendrite Source: Ensembl
  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: UniProtKB
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA38338.

Polymorphism and mutation databases

BioMutaiZDHHC5.
DMDMi28202103.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 715715Palmitoyltransferase ZDHHC5PRO_0000212868Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei91 – 911PhosphotyrosineBy similarity
Modified residuei247 – 2471PhosphoserineCombined sources
Modified residuei294 – 2941PhosphothreonineBy similarity
Modified residuei296 – 2961PhosphoserineCombined sources
Modified residuei299 – 2991PhosphoserineCombined sources
Modified residuei303 – 3031PhosphothreonineBy similarity
Modified residuei345 – 3451PhosphoserineCombined sources
Modified residuei348 – 3481PhosphothreonineCombined sources
Modified residuei350 – 3501PhosphothreonineBy similarity
Modified residuei380 – 3801PhosphoserineCombined sources
Modified residuei398 – 3981PhosphoserineCombined sources
Modified residuei406 – 4061PhosphoserineCombined sources
Modified residuei409 – 4091PhosphoserineCombined sources
Modified residuei411 – 4111PhosphothreonineCombined sources
Modified residuei415 – 4151PhosphoserineCombined sources
Modified residuei425 – 4251PhosphoserineCombined sources
Modified residuei429 – 4291PhosphoserineBy similarity
Modified residuei432 – 4321PhosphoserineCombined sources
Modified residuei436 – 4361PhosphothreonineCombined sources
Modified residuei529 – 5291PhosphoserineCombined sources
Modified residuei554 – 5541PhosphoserineCombined sources
Modified residuei621 – 6211PhosphoserineCombined sources
Modified residuei659 – 6591PhosphothreonineCombined sources
Modified residuei684 – 6841PhosphoserineCombined sources
Modified residuei694 – 6941PhosphoserineCombined sources

Keywords - PTMi

Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

EPDiQ9C0B5.
MaxQBiQ9C0B5.
PaxDbiQ9C0B5.
PeptideAtlasiQ9C0B5.
PRIDEiQ9C0B5.

PTM databases

iPTMnetiQ9C0B5.
PhosphoSiteiQ9C0B5.
SwissPalmiQ9C0B5.

Expressioni

Gene expression databases

BgeeiQ9C0B5.
CleanExiHS_ZDHHC5.
ExpressionAtlasiQ9C0B5. baseline and differential.
GenevisibleiQ9C0B5. HS.

Organism-specific databases

HPAiHPA014670.

Interactioni

Protein-protein interaction databases

BioGridi117422. 22 interactions.
IntActiQ9C0B5. 16 interactions.
STRINGi9606.ENSP00000287169.

Structurei

3D structure databases

ProteinModelPortaliQ9C0B5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini104 – 15451DHHCPROSITE-ProRule annotationAdd
BLAST

Domaini

The DHHC domain is required for palmitoyltransferase activity.By similarity

Sequence similaritiesi

Contains 1 DHHC domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1311. Eukaryota.
COG5273. LUCA.
GeneTreeiENSGT00550000074293.
HOGENOMiHOG000234346.
HOVERGENiHBG057186.
InParanoidiQ9C0B5.
KOiK20030.
OMAiSRHIVAS.
OrthoDBiEOG7WHH9B.
PhylomeDBiQ9C0B5.
TreeFamiTF354263.

Family and domain databases

InterProiIPR001594. Znf_DHHC_palmitoyltrfase.
[Graphical view]
PfamiPF01529. zf-DHHC. 1 hit.
[Graphical view]
PROSITEiPS50216. DHHC. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9C0B5-1) [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

        10         20         30         40         50
MPAESGKRFK PSKYVPVSAA AIFLVGATTL FFAFTCPGLS LYVSPAVPIY
60 70 80 90 100
NAIMFLFVLA NFSMATFMDP GIFPRAEEDE DKEDDFRAPL YKTVEIKGIQ
110 120 130 140 150
VRMKWCATCR FYRPPRCSHC SVCDNCVEEF DHHCPWVNNC IGRRNYRYFF
160 170 180 190 200
LFLLSLTAHI MGVFGFGLLY VLYHIEELSG VRTAVTMAVM CVAGLFFIPV
210 220 230 240 250
AGLTGFHVVL VARGRTTNEQ VTGKFRGGVN PFTNGCCNNV SRVLCSSPAP
260 270 280 290 300
RYLGRPKKEK TIVIRPPFLR PEVSDGQITV KIMDNGIQGE LRRTKSKGSL
310 320 330 340 350
EITESQSADA EPPPPPKPDL SRYTGLRTHL GLATNEDSSL LAKDSPPTPT
360 370 380 390 400
MYKYRPGYSS SSTSAAMPHS SSAKLSRGDS LKEPTSIAES SRHPSYRSEP
410 420 430 440 450
SLEPESFRSP TFGKSFHFDP LSSGSRSSSL KSAQGTGFEL GQLQSIRSEG
460 470 480 490 500
TTSTSYKSLA NQTRNGSLSY DSLLTPSDSP DFESVQAGPE PDPPLGYTSP
510 520 530 540 550
FLSARLAQQR EAERHPRLVP TGPTHREPSP VRYDNLSRHI VASLQEREKL
560 570 580 590 600
LRQSPPLPGR EEEPGLGDSG IQSTPGSGHA PRTSSSSDDS KRSPLGKTPL
610 620 630 640 650
GRPAVPRFGK PDGLRGRGVG SPEPGPTAPY LGRSMSYSSQ KAQPGVSETE
660 670 680 690 700
EVALQPLLTP KDEVQLKTTY SKSNGQPKSL GSASPGPGQP PLSSPTRGGV
710
KKVSGVGGTT YEISV
Length:715
Mass (Da):77,545
Last modified:February 1, 2003 - v2
Checksum:i9E4FB0C9AC8EFE28
GO
Isoform 2 (identifier: Q9C0B5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-53: Missing.

Note: No experimental confirmation available.
Show »
Length:662
Mass (Da):71,952
Checksum:i9BC8E828B718A32E
GO

Sequence cautioni

The sequence BAB21839.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAD18778.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti508 – 5092QQ → TR in CAB56033 (PubMed:17974005).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5353Missing in isoform 2. 1 PublicationVSP_006935Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB051535 mRNA. Translation: BAB21839.1. Different initiation.
AY894889 mRNA. Translation: AAX73368.1.
AK023130 mRNA. Translation: BAB14420.1.
AK172807 mRNA. Translation: BAD18778.1. Different initiation.
CH471076 Genomic DNA. Translation: EAW73771.1.
BC026967 mRNA. Translation: AAH26967.1.
AL117662 mRNA. Translation: CAB56033.1.
CCDSiCCDS7965.1. [Q9C0B5-1]
PIRiT17343.
RefSeqiNP_056272.2. NM_015457.2. [Q9C0B5-1]
XP_011543201.1. XM_011544899.1. [Q9C0B5-1]
XP_011543202.1. XM_011544900.1. [Q9C0B5-1]
XP_011543203.1. XM_011544901.1. [Q9C0B5-1]
UniGeneiHs.27239.

Genome annotation databases

EnsembliENST00000287169; ENSP00000287169; ENSG00000156599. [Q9C0B5-1]
ENST00000527985; ENSP00000432202; ENSG00000156599. [Q9C0B5-2]
GeneIDi25921.
KEGGihsa:25921.
UCSCiuc001nkx.2. human. [Q9C0B5-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB051535 mRNA. Translation: BAB21839.1. Different initiation.
AY894889 mRNA. Translation: AAX73368.1.
AK023130 mRNA. Translation: BAB14420.1.
AK172807 mRNA. Translation: BAD18778.1. Different initiation.
CH471076 Genomic DNA. Translation: EAW73771.1.
BC026967 mRNA. Translation: AAH26967.1.
AL117662 mRNA. Translation: CAB56033.1.
CCDSiCCDS7965.1. [Q9C0B5-1]
PIRiT17343.
RefSeqiNP_056272.2. NM_015457.2. [Q9C0B5-1]
XP_011543201.1. XM_011544899.1. [Q9C0B5-1]
XP_011543202.1. XM_011544900.1. [Q9C0B5-1]
XP_011543203.1. XM_011544901.1. [Q9C0B5-1]
UniGeneiHs.27239.

3D structure databases

ProteinModelPortaliQ9C0B5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117422. 22 interactions.
IntActiQ9C0B5. 16 interactions.
STRINGi9606.ENSP00000287169.

PTM databases

iPTMnetiQ9C0B5.
PhosphoSiteiQ9C0B5.
SwissPalmiQ9C0B5.

Polymorphism and mutation databases

BioMutaiZDHHC5.
DMDMi28202103.

Proteomic databases

EPDiQ9C0B5.
MaxQBiQ9C0B5.
PaxDbiQ9C0B5.
PeptideAtlasiQ9C0B5.
PRIDEiQ9C0B5.

Protocols and materials databases

DNASUi25921.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000287169; ENSP00000287169; ENSG00000156599. [Q9C0B5-1]
ENST00000527985; ENSP00000432202; ENSG00000156599. [Q9C0B5-2]
GeneIDi25921.
KEGGihsa:25921.
UCSCiuc001nkx.2. human. [Q9C0B5-1]

Organism-specific databases

CTDi25921.
GeneCardsiZDHHC5.
HGNCiHGNC:18472. ZDHHC5.
HPAiHPA014670.
MIMi614586. gene.
neXtProtiNX_Q9C0B5.
PharmGKBiPA38338.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1311. Eukaryota.
COG5273. LUCA.
GeneTreeiENSGT00550000074293.
HOGENOMiHOG000234346.
HOVERGENiHBG057186.
InParanoidiQ9C0B5.
KOiK20030.
OMAiSRHIVAS.
OrthoDBiEOG7WHH9B.
PhylomeDBiQ9C0B5.
TreeFamiTF354263.

Miscellaneous databases

ChiTaRSiZDHHC5. human.
GenomeRNAii25921.
PROiQ9C0B5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9C0B5.
CleanExiHS_ZDHHC5.
ExpressionAtlasiQ9C0B5. baseline and differential.
GenevisibleiQ9C0B5. HS.

Family and domain databases

InterProiIPR001594. Znf_DHHC_palmitoyltrfase.
[Graphical view]
PfamiPF01529. zf-DHHC. 1 hit.
[Graphical view]
PROSITEiPS50216. DHHC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.
    DNA Res. 7:347-355(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  2. "A superfamily of membrane-associated DHHC type zinc finger proteins."
    Huang C.-H., Chen Y., Ye T.
    Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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] (ISOFORM 1).
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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: Uterus.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 508-715 (ISOFORMS 1/2).
    Tissue: Uterus.
  7. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
    Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
    Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-432, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "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-621, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-621, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296; SER-345; THR-348; SER-380; SER-409; SER-432; THR-436; SER-554; SER-621; THR-659 AND SER-694, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-432; THR-436 AND SER-621, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  14. "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(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-380; SER-432; SER-621; SER-684 AND SER-694, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "Somatostatin receptor 5 is palmitoylated by the interacting ZDHHC5 palmitoyltransferase."
    Kokkola T., Kruse C., Roy-Pogodzik E.M., Pekkinen J., Bauch C., Honck H.H., Hennemann H., Kreienkamp H.J.
    FEBS Lett. 585:2665-2670(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  16. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-621, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247; SER-299; SER-380; SER-398; SER-406; SER-409; THR-411; SER-415; SER-425; SER-432; THR-436; SER-529; SER-554; SER-621; SER-684 AND SER-694, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  18. "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(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-380 AND SER-554, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiZDHC5_HUMAN
AccessioniPrimary (citable) accession number: Q9C0B5
Secondary accession number(s): Q2TGF0
, Q6ZMF0, Q8TAK8, Q9H923, Q9UFI7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2003
Last sequence update: February 1, 2003
Last modified: July 6, 2016
This is version 133 of the entry and version 2 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 11
    Human chromosome 11: 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

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 one 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.