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Protein

Calcineurin B homologous protein 3

Gene

TESC

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

Functioni

Functions as an integral cofactor in cell pH regulation by controlling plasma membrane-type Na+/H+ exchange activity. Promotes the maturation, transport, cell surface stability and exchange activity of SLC9A1/NHE1 at the plasma membrane. Promotes the induction of hematopoietic stem cell differentiation toward megakaryocytic lineage. Essential for the coupling of ERK cascade activation with the expression of ETS family genes in megakaryocytic differentiation. Also involved in granulocytic differentiation in a ERK-dependent manner. Inhibits the phosphatase activity of calcineurin.3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi123 – 13412PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • cell differentiation Source: UniProtKB-KW
  • cellular response to retinoic acid Source: UniProtKB
  • negative regulation of catalytic activity Source: GOC
  • negative regulation of cell proliferation Source: UniProtKB
  • positive regulation of gene expression Source: UniProtKB
  • positive regulation of granulocyte differentiation Source: UniProtKB
  • positive regulation of megakaryocyte differentiation Source: UniProtKB
  • positive regulation of sodium:proton antiporter activity Source: UniProtKB
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • protein maturation Source: UniProtKB
  • protein stabilization Source: UniProtKB
  • protein targeting to plasma membrane Source: UniProtKB
  • regulation of cell adhesion mediated by integrin Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Protein kinase inhibitor

Keywords - Biological processi

Differentiation, Protein transport, Transport

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Calcineurin B homologous protein 3
Alternative name(s):
Tescalcin
Short name:
TSC
Gene namesi
Name:TESC
Synonyms:CHP3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:26065. TESC.

Subcellular locationi

  • Nucleus 1 Publication
  • Cytoplasm 1 Publication
  • Membrane Curated; Lipid-anchor Curated
  • Cell membrane 1 Publication
  • Cell projectionlamellipodium 1 Publication
  • Cell projectionruffle membrane By similarity

  • Note: Colocalizes with SLC9A1 at the plasma membrane.1 Publication

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • lamellipodium Source: UniProtKB
  • nucleus Source: UniProtKB
  • plasma membrane Source: UniProtKB
  • ruffle Source: UniProtKB
  • ruffle membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA143485630.

Polymorphism and mutation databases

BioMutaiTESC.
DMDMi284018160.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved2 Publications
Chaini2 – 214213Calcineurin B homologous protein 3PRO_0000073859Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine3 Publications

Keywords - PTMi

Disulfide bond, Lipoprotein, Myristate

Proteomic databases

EPDiQ96BS2.
MaxQBiQ96BS2.
PaxDbiQ96BS2.
PRIDEiQ96BS2.

PTM databases

iPTMnetiQ96BS2.
PhosphoSiteiQ96BS2.
SwissPalmiQ96BS2.

Expressioni

Tissue specificityi

Expressed in mature megakaryocytes and polymorphonuclear granulocytes (at protein level). Abundantly expressed in heart. Also expressed at a lower level in adult testis and salivary gland, and in the placenta.2 Publications

Developmental stagei

Strongly up-regulated in K562 cells treated by PMA to promote megakaryocytic differentiation, but not when treated by DMSO to promote granulocytic differentiation or by hemin to promote erythroid differentiation (at protein level).1 Publication

Inductioni

Up-regulated during granulocytic differentiation in a ERK-dependent manner (is mediated by activation of ERK) (at protein level). Up-regulated during the differentiation and maturation of primary megakaryocytes. Down-regulated during monocytic-macrophage differentiation in a ERK-dependent manner.2 Publications

Gene expression databases

BgeeiQ96BS2.
CleanExiHS_TESC.
ExpressionAtlasiQ96BS2. baseline and differential.
GenevisibleiQ96BS2. HS.

Organism-specific databases

HPAiHPA053200.

Interactioni

Subunit structurei

Monomer. Homodimer; disulfide-linked (By similarity). Interacts with SLC9A1/NHE1 (via juxtamembrane region of the cytoplasmic C-terminus); the interaction enable an optimal Na+/H+ exchange activity.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HMG20AQ9NP662EBI-740653,EBI-740641
WBP11Q9Y2W23EBI-740653,EBI-714455

GO - Molecular functioni

Protein-protein interaction databases

BioGridi120330. 8 interactions.
IntActiQ96BS2. 5 interactions.
MINTiMINT-1477844.
STRINGi9606.ENSP00000334785.

Structurei

3D structure databases

ProteinModelPortaliQ96BS2.
SMRiQ96BS2. Positions 9-214.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini110 – 14536EF-handPROSITE-ProRule annotationAdd
BLAST

Domaini

Binds calcium via its EF-hands. Calcium-binding mediates a conformational change. Can also bind magnesium (By similarity).By similarity

Sequence similaritiesi

Contains 1 EF-hand domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0034. Eukaryota.
COG5126. LUCA.
GeneTreeiENSGT00730000111113.
HOGENOMiHOG000233019.
HOVERGENiHBG105313.
InParanoidiQ96BS2.
KOiK17612.
OMAiPDLEFNP.
OrthoDBiEOG7NSB38.
PhylomeDBiQ96BS2.
TreeFamiTF354284.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]
SMARTiSM00054. EFh. 1 hit.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q96BS2-1) [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
MGAAHSASEE VRELEGKTGF SSDQIEQLHR RFKQLSGDQP TIRKENFNNV
60 70 80 90 100
PDLELNPIRS KIVRAFFDNR NLRKGPSGLA DEINFEDFLT IMSYFRPIDT
110 120 130 140 150
TMDEEQVELS RKEKLRFLFH MYDSDSDGRI TLEEYRNVVE ELLSGNPHIE
160 170 180 190 200
KESARSIADG AMMEAASVCM GQMEPDQVYE GITFEDFLKI WQGIDIETKM
210
HVRFLNMETM ALCH
Length:214
Mass (Da):24,750
Last modified:January 19, 2010 - v3
Checksum:iAB3DBE6EA3EB5E60
GO
Isoform 2 (identifier: Q96BS2-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     139-163: VEELLSGNPHIEKESARSIADGAMM → KWSRSCCRETLTSRRSPLAPSPTGP
     164-214: Missing.

Show »
Length:163
Mass (Da):18,919
Checksum:i62F6297230869579
GO
Isoform 3 (identifier: Q96BS2-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     43-69: Missing.

Note: No experimental confirmation available.
Show »
Length:187
Mass (Da):21,521
Checksum:iD0DA826BC7A293AC
GO

Sequence cautioni

The sequence BAA91288.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence EAW98101.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti209 – 2113TMA → NMG in BQ949772 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei43 – 6927Missing in isoform 3. 1 PublicationVSP_045287Add
BLAST
Alternative sequencei139 – 16325VEELL…DGAMM → KWSRSCCRETLTSRRSPLAP SPTGP in isoform 2. 1 PublicationVSP_035518Add
BLAST
Alternative sequencei164 – 21451Missing in isoform 2. 1 PublicationVSP_035519Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF443207 mRNA. Translation: AAL35615.1.
AK000614 mRNA. Translation: BAA91288.1. Different initiation.
AC026368 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW98101.1. Different initiation.
BC015221 mRNA. Translation: AAH15221.1.
BQ949772 mRNA. No translation available.
CCDSiCCDS53835.1. [Q96BS2-3]
CCDS9183.3. [Q96BS2-1]
RefSeqiNP_001161797.1. NM_001168325.1. [Q96BS2-3]
NP_060369.3. NM_017899.3. [Q96BS2-1]
UniGeneiHs.525709.

Genome annotation databases

EnsembliENST00000335209; ENSP00000334785; ENSG00000088992. [Q96BS2-1]
ENST00000470612; ENSP00000432716; ENSG00000088992. [Q96BS2-2]
ENST00000541210; ENSP00000445689; ENSG00000088992. [Q96BS2-3]
GeneIDi54997.
KEGGihsa:54997.
UCSCiuc001twh.4. human. [Q96BS2-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF443207 mRNA. Translation: AAL35615.1.
AK000614 mRNA. Translation: BAA91288.1. Different initiation.
AC026368 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW98101.1. Different initiation.
BC015221 mRNA. Translation: AAH15221.1.
BQ949772 mRNA. No translation available.
CCDSiCCDS53835.1. [Q96BS2-3]
CCDS9183.3. [Q96BS2-1]
RefSeqiNP_001161797.1. NM_001168325.1. [Q96BS2-3]
NP_060369.3. NM_017899.3. [Q96BS2-1]
UniGeneiHs.525709.

3D structure databases

ProteinModelPortaliQ96BS2.
SMRiQ96BS2. Positions 9-214.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120330. 8 interactions.
IntActiQ96BS2. 5 interactions.
MINTiMINT-1477844.
STRINGi9606.ENSP00000334785.

PTM databases

iPTMnetiQ96BS2.
PhosphoSiteiQ96BS2.
SwissPalmiQ96BS2.

Polymorphism and mutation databases

BioMutaiTESC.
DMDMi284018160.

Proteomic databases

EPDiQ96BS2.
MaxQBiQ96BS2.
PaxDbiQ96BS2.
PRIDEiQ96BS2.

Protocols and materials databases

DNASUi54997.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000335209; ENSP00000334785; ENSG00000088992. [Q96BS2-1]
ENST00000470612; ENSP00000432716; ENSG00000088992. [Q96BS2-2]
ENST00000541210; ENSP00000445689; ENSG00000088992. [Q96BS2-3]
GeneIDi54997.
KEGGihsa:54997.
UCSCiuc001twh.4. human. [Q96BS2-1]

Organism-specific databases

CTDi54997.
GeneCardsiTESC.
HGNCiHGNC:26065. TESC.
HPAiHPA053200.
MIMi611585. gene.
neXtProtiNX_Q96BS2.
PharmGKBiPA143485630.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0034. Eukaryota.
COG5126. LUCA.
GeneTreeiENSGT00730000111113.
HOGENOMiHOG000233019.
HOVERGENiHBG105313.
InParanoidiQ96BS2.
KOiK17612.
OMAiPDLEFNP.
OrthoDBiEOG7NSB38.
PhylomeDBiQ96BS2.
TreeFamiTF354284.

Miscellaneous databases

ChiTaRSiTESC. human.
GenomeRNAii54997.
PROiQ96BS2.
SOURCEiSearch...

Gene expression databases

BgeeiQ96BS2.
CleanExiHS_TESC.
ExpressionAtlasiQ96BS2. baseline and differential.
GenevisibleiQ96BS2. HS.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]
SMARTiSM00054. EFh. 1 hit.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Human homolog of mouse tescalcin associates with Na(+)/H(+) exchanger type-1."
    Mailaender J., Mueller-Esterl W., Dedio J.
    FEBS Lett. 507:331-335(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH SLC9A1, CALCIUM-BINDING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  2. "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 2).
    Tissue: Signet-ring cell carcinoma.
  3. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] (ISOFORMS 1 AND 3).
  6. "The Na+/H+ exchanger cytoplasmic tail: structure, function, and interactions with tescalcin."
    Li X., Liu Y., Kay C.M., Muller-Esterl W., Fliegel L.
    Biochemistry 42:7448-7456(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SLC9A1.
  7. "Characterization of tescalcin, a novel EF-hand protein with a single Ca2+-binding site: metal-binding properties, localization in tissues and cells, and effect on calcineurin."
    Gutierrez-Ford C., Levay K., Gomes A.V., Perera E.M., Som T., Kim Y.M., Benovic J.L., Berkovitz G.D., Slepak V.Z.
    Biochemistry 42:14553-14565(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: MYRISTOYLATION AT GLY-2.
  8. "Tescalcin is an essential factor in megakaryocytic differentiation associated with Ets family gene expression."
    Levay K., Slepak V.Z.
    J. Clin. Invest. 117:2672-2683(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MEGAKARYOCYTIC DIFFERENTIATION, INDUCTION, DEVELOPMENTAL STAGE.
  9. "Calcineurin B homologous protein 3 promotes the biosynthetic maturation, cell surface stability, and optimal transport of the Na+/H+ exchanger NHE1 isoform."
    Zaun H.C., Shrier A., Orlowski J.
    J. Biol. Chem. 283:12456-12467(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SLC9A1, SUBCELLULAR LOCATION.
  10. "Up- or downregulation of tescalcin in HL-60 cells is associated with their differentiation to either granulocytic or macrophage-like lineage."
    Levay K., Slepak V.Z.
    Exp. Cell Res. 316:1254-1262(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN GRANULOCYTIC DIFFERENTIATION, INDUCTION, TISSUE SPECIFICITY.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Global profiling of co- and post-translationally N-myristoylated proteomes in human cells."
    Thinon E., Serwa R.A., Broncel M., Brannigan J.A., Brassat U., Wright M.H., Heal W.P., Wilkinson A.J., Mann D.J., Tate E.W.
    Nat. Commun. 5:4919-4919(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, IDENTIFICATION BY MASS SPECTROMETRY.
  13. "Multifunctional reagents for quantitative proteome-wide analysis of protein modification in human cells and dynamic profiling of protein lipidation during vertebrate development."
    Broncel M., Serwa R.A., Ciepla P., Krause E., Dallman M.J., Magee A.I., Tate E.W.
    Angew. Chem. Int. Ed. 54:5948-5951(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, IDENTIFICATION BY MASS SPECTROMETRY.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCHP3_HUMAN
AccessioniPrimary (citable) accession number: Q96BS2
Secondary accession number(s): F5H1Y5, Q9NWT9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: January 19, 2010
Last modified: June 8, 2016
This is version 125 of the entry and version 3 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

Caution

Although PubMed:12809501 reports that TESC results in a decrease in transporter activity of human SLC9A1, studies with rat SLC9A1 show that TESC-binding results in the maturation and accumulation of SLC9A1 at the cell surface.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: 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.