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Q9P035

- HACD3_HUMAN

UniProt

Q9P035 - HACD3_HUMAN

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Protein

Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase 3

Gene

PTPLAD1

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

Functioni

Responsible for the dehydration step in very long-chain fatty acid (VLCFA) synthesis. Involved in Rac1-signaling pathways leading to the modulation of gene expression.2 Publications

Catalytic activityi

A very-long-chain (3R)-3-hydroxyacyl-CoA = a very-long-chain trans-2,3-dehydroacyl-CoA + H2O.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei286 – 2861By similarity
Active sitei293 – 2931By similarity

GO - Molecular functioni

  1. GTPase activator activity Source: ProtInc
  2. lyase activity Source: UniProtKB-KW

GO - Biological processi

  1. activation of JUN kinase activity Source: ProtInc
  2. fatty acid biosynthetic process Source: UniProtKB-KW
  3. I-kappaB kinase/NF-kappaB signaling Source: ProtInc
  4. positive regulation of GTPase activity Source: GOC
  5. Rac protein signal transduction Source: UniProtKB
  6. Rho protein signal transduction Source: Ensembl
  7. small GTPase mediated signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Names & Taxonomyi

Protein namesi
Recommended name:
Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase 3 (EC:4.2.1.134)
Alternative name(s):
3-hydroxyacyl-CoA dehydratase 3
Short name:
HACD3
Butyrate-induced protein 1
Short name:
B-ind1
Short name:
hB-ind1
Protein tyrosine phosphatase-like protein PTPLAD1
Protein-tyrosine phosphatase-like A domain-containing protein 1
Gene namesi
Name:PTPLAD1
Synonyms:BIND1, HACD3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:24175. PTPLAD1.

Subcellular locationi

Endoplasmic reticulum membrane 1 Publication; Multi-pass membrane protein 1 Publication

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB-KW
  2. focal adhesion Source: UniProtKB
  3. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142671113.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 362362Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase 3PRO_0000313724Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei114 – 1141Phosphoserine8 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9P035.
PaxDbiQ9P035.
PRIDEiQ9P035.

PTM databases

PhosphoSiteiQ9P035.

Expressioni

Tissue specificityi

Highly expressed in testis, kidney, brain, liver and weakly in skeletal muscle, spleen and heart. No expression detected in leukocytes.2 Publications

Inductioni

By AKAP12 and histone deacetylase inhibitors such as sodium butyrate.1 Publication

Gene expression databases

BgeeiQ9P035.
CleanExiHS_PTPLAD1.
ExpressionAtlasiQ9P035. baseline and differential.
GenevestigatoriQ9P035.

Organism-specific databases

HPAiHPA014837.

Interactioni

Subunit structurei

Interacts with the condensation enzymes of the ELOVL family. Interacts with RAC1.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Q034632EBI-359013,EBI-8803426From a different organism.
Q99IB82EBI-359013,EBI-6927873From a different organism.
Q9WMX23EBI-359013,EBI-6863748From a different organism.

Protein-protein interaction databases

BioGridi119570. 30 interactions.
IntActiQ9P035. 21 interactions.
MINTiMINT-1135933.

Structurei

3D structure databases

ProteinModelPortaliQ9P035.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 149149CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini171 – 18515LumenalSequence AnalysisAdd
BLAST
Topological domaini208 – 21710CytoplasmicSequence Analysis
Topological domaini236 – 2416LumenalSequence Analysis
Topological domaini257 – 27923CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini299 – 32224LumenalSequence AnalysisAdd
BLAST
Topological domaini344 – 36219CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei150 – 17021HelicalSequence AnalysisAdd
BLAST
Transmembranei186 – 20722HelicalSequence AnalysisAdd
BLAST
Transmembranei218 – 23518HelicalSequence AnalysisAdd
BLAST
Transmembranei242 – 25615HelicalSequence AnalysisAdd
BLAST
Transmembranei280 – 29819HelicalSequence AnalysisAdd
BLAST
Transmembranei323 – 34321HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 9490CSPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili111 – 13626Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi350 – 3534Poly-Arg
Compositional biasi357 – 3604Poly-Lys

Sequence similaritiesi

Contains 1 CS domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG5198.
GeneTreeiENSGT00530000062962.
HOVERGENiHBG108301.
InParanoidiQ9P035.
OrthoDBiEOG7BP82H.
PhylomeDBiQ9P035.
TreeFamiTF313326.

Family and domain databases

Gene3Di2.60.40.790. 1 hit.
InterProiIPR007052. CS_dom.
IPR008978. HSP20-like_chaperone.
IPR007482. Tyr_Pase-like_PTPLA.
[Graphical view]
PANTHERiPTHR11035. PTHR11035. 1 hit.
PfamiPF04969. CS. 1 hit.
PF04387. PTPLA. 1 hit.
[Graphical view]
SUPFAMiSSF49764. SSF49764. 1 hit.
PROSITEiPS51203. CS. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9P035) [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
MENQVLTPHV YWAQRHRELY LRVELSDVQN PAISITENVL HFKAQGHGAK
60 70 80 90 100
GDNVYEFHLE FLDLVKPEPV YKLTQRQVNI TVQKKVSQWW ERLTKQEKRP
110 120 130 140 150
LFLAPDFDRW LDESDAEMEL RAKEEERLNK LRLESEGSPE TLTNLRKGYL
160 170 180 190 200
FMYNLVQFLG FSWIFVNLTV RFCILGKESF YDTFHTVADM MYFCQMLAVV
210 220 230 240 250
ETINAAIGVT TSPVLPSLIQ LLGRNFILFI IFGTMEEMQN KAVVFFVFYL
260 270 280 290 300
WSAIEIFRYS FYMLTCIDMD WKVLTWLRYT LWIPLYPLGC LAEAVSVIQS
310 320 330 340 350
IPIFNETGRF SFTLPYPVKI KVRFSFFLQI YLIMIFLGLY INFRHLYKQR
360
RRRYGQKKKK IH
Length:362
Mass (Da):43,160
Last modified:January 15, 2008 - v2
Checksum:i1B3591E88DD85D16
GO
Isoform 2 (identifier: Q9P035-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     69-123: Missing.

Note: No experimental confirmation available.

Show »
Length:307
Mass (Da):36,431
Checksum:iB14E762EB96B17F8
GO

Sequence cautioni

The sequence AAF29085.1 differs from that shown. Reason: Frameshift at position 356.
The sequence BAC11249.1 differs from that shown. Reason: Frameshift at position 359.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti60 – 601E → K in BAB55101. (PubMed:14702039)Curated
Sequence conflicti245 – 2451F → I in BAC11277. (PubMed:14702039)Curated
Sequence conflicti282 – 2821W → G in AAH35508. (PubMed:15489334)Curated
Sequence conflicti292 – 2921A → V in AAF29085. (PubMed:11042152)Curated
Sequence conflicti352 – 36211RRYGQKKKKIH → LKMRAGAVAHACDPSALGG in CAB69070. (PubMed:10747961)CuratedAdd
BLAST
Sequence conflicti361 – 3611I → K in AAH35508. (PubMed:15489334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti56 – 561E → K.
Corresponds to variant rs11632737 [ dbSNP | Ensembl ].
VAR_037712
Natural varianti269 – 2691M → L.
Corresponds to variant rs2279854 [ dbSNP | Ensembl ].
VAR_037713

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei69 – 12355Missing in isoform 2. 1 PublicationVSP_056070Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ271091 mRNA. Translation: CAB69070.1.
AF161470 mRNA. Translation: AAF29085.1. Frameshift.
AK027421 mRNA. Translation: BAB55101.1.
AK074857 mRNA. Translation: BAC11249.1. Frameshift.
AK074898 mRNA. Translation: BAC11277.1.
AK299234 mRNA. Translation: BAG61266.1.
AC011846 Genomic DNA. No translation available.
AC027220 Genomic DNA. No translation available.
BC019873 mRNA. Translation: AAH19873.1.
BC035508 mRNA. Translation: AAH35508.1.
BC047685 mRNA. Translation: AAH47685.1.
BC058912 mRNA. Translation: AAH58912.1.
DQ251107 Genomic DNA. Translation: ABB83547.1.
CCDSiCCDS45282.1. [Q9P035-1]
RefSeqiNP_057479.2. NM_016395.2.
UniGeneiHs.512973.

Genome annotation databases

EnsembliENST00000261875; ENSP00000261875; ENSG00000074696. [Q9P035-1]
ENST00000442729; ENSP00000392491; ENSG00000074696. [Q9P035-2]
GeneIDi51495.
KEGGihsa:51495.
UCSCiuc002apc.3. human. [Q9P035-1]

Polymorphism databases

DMDMi166199462.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ271091 mRNA. Translation: CAB69070.1 .
AF161470 mRNA. Translation: AAF29085.1 . Frameshift.
AK027421 mRNA. Translation: BAB55101.1 .
AK074857 mRNA. Translation: BAC11249.1 . Frameshift.
AK074898 mRNA. Translation: BAC11277.1 .
AK299234 mRNA. Translation: BAG61266.1 .
AC011846 Genomic DNA. No translation available.
AC027220 Genomic DNA. No translation available.
BC019873 mRNA. Translation: AAH19873.1 .
BC035508 mRNA. Translation: AAH35508.1 .
BC047685 mRNA. Translation: AAH47685.1 .
BC058912 mRNA. Translation: AAH58912.1 .
DQ251107 Genomic DNA. Translation: ABB83547.1 .
CCDSi CCDS45282.1. [Q9P035-1 ]
RefSeqi NP_057479.2. NM_016395.2.
UniGenei Hs.512973.

3D structure databases

ProteinModelPortali Q9P035.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 119570. 30 interactions.
IntActi Q9P035. 21 interactions.
MINTi MINT-1135933.

PTM databases

PhosphoSitei Q9P035.

Polymorphism databases

DMDMi 166199462.

Proteomic databases

MaxQBi Q9P035.
PaxDbi Q9P035.
PRIDEi Q9P035.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000261875 ; ENSP00000261875 ; ENSG00000074696 . [Q9P035-1 ]
ENST00000442729 ; ENSP00000392491 ; ENSG00000074696 . [Q9P035-2 ]
GeneIDi 51495.
KEGGi hsa:51495.
UCSCi uc002apc.3. human. [Q9P035-1 ]

Organism-specific databases

CTDi 51495.
GeneCardsi GC15P065822.
H-InvDB HIX0012353.
HGNCi HGNC:24175. PTPLAD1.
HPAi HPA014837.
neXtProti NX_Q9P035.
PharmGKBi PA142671113.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5198.
GeneTreei ENSGT00530000062962.
HOVERGENi HBG108301.
InParanoidi Q9P035.
OrthoDBi EOG7BP82H.
PhylomeDBi Q9P035.
TreeFami TF313326.

Miscellaneous databases

ChiTaRSi PTPLAD1. human.
GeneWikii PTPLAD1.
GenomeRNAii 51495.
NextBioi 35474375.
PROi Q9P035.

Gene expression databases

Bgeei Q9P035.
CleanExi HS_PTPLAD1.
ExpressionAtlasi Q9P035. baseline and differential.
Genevestigatori Q9P035.

Family and domain databases

Gene3Di 2.60.40.790. 1 hit.
InterProi IPR007052. CS_dom.
IPR008978. HSP20-like_chaperone.
IPR007482. Tyr_Pase-like_PTPLA.
[Graphical view ]
PANTHERi PTHR11035. PTHR11035. 1 hit.
Pfami PF04969. CS. 1 hit.
PF04387. PTPLA. 1 hit.
[Graphical view ]
SUPFAMi SSF49764. SSF49764. 1 hit.
PROSITEi PS51203. CS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "B-ind1, a novel mediator of Rac1 signaling cloned from sodium butyrate-treated fibroblasts."
    Courilleau D., Chastre E., Sabbah M., Redeuilh G., Atfi A., Mester J.
    J. Biol. Chem. 275:17344-17348(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH RAC1, TISSUE SPECIFICITY.
  2. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
    Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
    , Gu J., Chen S.-J., Chen Z.
    Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Umbilical cord blood.
  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 AND 2).
  4. "Analysis of the DNA sequence and duplication history of human chromosome 15."
    Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
    , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
    Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
    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 1).
    Tissue: B-cell, Duodenum, Eye and Urinary bladder.
  6. "Human B-ind1 gene promoter: cloning and regulation by histone deacetylase inhibitors."
    Sabbah M., Saucier C., Redeuilh G.
    Gene 374:128-133(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
  7. "SSeCKS/Gravin/AKAP12 attenuates expression of proliferative and angiogenic genes during suppression of v-Src-induced oncogenesis."
    Liu Y., Gao L., Gelman I.H.
    BMC Cancer 6:105-105(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY AKAP12.
  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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Characterization of four mammalian 3-hydroxyacyl-CoA dehydratases involved in very long-chain fatty acid synthesis."
    Ikeda M., Kanao Y., Yamanaka M., Sakuraba H., Mizutani Y., Igarashi Y., Kihara A.
    FEBS Lett. 582:2435-2440(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, INTERACTION WITH ELOVL FAMILY.
  10. "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-114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "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-114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
    Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
    Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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-114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  16. "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-114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "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-114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiHACD3_HUMAN
AccessioniPrimary (citable) accession number: Q9P035
Secondary accession number(s): A0PJA1
, B4DRF4, Q280Z3, Q6PD63, Q8IUI5, Q8NC86, Q8NCB1, Q96T12, Q9NQA7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 15, 2008
Last modified: October 29, 2014
This is version 99 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 15
    Human chromosome 15: 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. SIMILARITY comments
    Index of protein domains and families

External Data

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