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Protein

All-trans retinoic acid-induced differentiation factor

Gene

ATRAID

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

Functioni

Promotes osteoblast cell differentiation and terminal mineralization. Plays a role in inducing the cell cycle arrest via inhibiting CCND1 expression in all-trans-retinoic acid (ATRA) signal pathway.1 Publication

GO - Biological processi

  • cell differentiation Source: UniProtKB-KW
  • negative regulation of cyclin catabolic process Source: UniProtKB
  • negative regulation of osteoblast proliferation Source: UniProtKB
  • positive regulation of bone mineralization Source: UniProtKB
  • positive regulation of osteoblast differentiation Source: UniProtKB
  • regulation of gene expression Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Differentiation

Names & Taxonomyi

Protein namesi
Recommended name:
All-trans retinoic acid-induced differentiation factor
Alternative name(s):
Apoptosis-related protein 3
Short name:
APR-3
p18
Gene namesi
Name:ATRAID
Synonyms:APR3, C2orf28
ORF Names:HSPC013, UNQ214/PRO240
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:24090. ATRAID.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini31 – 199169ExtracellularSequence analysisAdd
BLAST
Transmembranei200 – 22021HelicalSequence analysisAdd
BLAST
Topological domaini221 – 2299CytoplasmicSequence analysis

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • lysosomal membrane Source: Ensembl
  • nuclear envelope Source: UniProtKB
  • perinuclear region of cytoplasm Source: UniProtKB
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134964154.

Polymorphism and mutation databases

BioMutaiATRAID.
DMDMi239938597.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 30301 PublicationAdd
BLAST
Chaini31 – 229199All-trans retinoic acid-induced differentiation factorPRO_0000020752Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi44 – 441N-linked (GlcNAc...)Sequence analysis
Glycosylationi79 – 791N-linked (GlcNAc...)Sequence analysis
Disulfide bondi156 ↔ 171PROSITE-ProRule annotation
Glycosylationi157 – 1571N-linked (GlcNAc...)Sequence analysis
Disulfide bondi165 ↔ 181PROSITE-ProRule annotation
Glycosylationi168 – 1681N-linked (GlcNAc...)Sequence analysis
Disulfide bondi183 ↔ 192PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ6UW56.
PaxDbiQ6UW56.
PRIDEiQ6UW56.

PTM databases

iPTMnetiQ6UW56.
PhosphoSiteiQ6UW56.

Expressioni

Tissue specificityi

Weakly expressed in hematopoietic cell lines.1 Publication

Inductioni

Up-regulated by all-trans-retinoic acid (ATRA) in several tumor cell lines.1 Publication

Gene expression databases

BgeeiQ6UW56.
CleanExiHS_C2orf28.
ExpressionAtlasiQ6UW56. baseline and differential.
GenevisibleiQ6UW56. HS.

Organism-specific databases

HPAiHPA051353.

Interactioni

Subunit structurei

Interacts with NELL1; the interaction promotes osteoblastic differentiation and mineralization.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
NELL1Q928324EBI-723802,EBI-947754
SNX9Q9Y5X12EBI-723802,EBI-77848

Protein-protein interaction databases

BioGridi119507. 3 interactions.
IntActiQ6UW56. 4 interactions.
MINTiMINT-1370379.
STRINGi9606.ENSP00000369518.

Structurei

3D structure databases

ProteinModelPortaliQ6UW56.
SMRiQ6UW56. Positions 75-124.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini152 – 19342EGF-likePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 EGF-like domain.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IYNU. Eukaryota.
ENOG4111PJW. LUCA.
GeneTreeiENSGT00390000017252.
HOVERGENiHBG054041.
InParanoidiQ6UW56.
OMAiGINAWNT.
OrthoDBiEOG7XWPQ5.
PhylomeDBiQ6UW56.
TreeFamiTF335766.

Family and domain databases

Gene3Di3.80.10.10. 1 hit.
InterProiIPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR032675. L_dom-like.
[Graphical view]
PROSITEiPS00022. EGF_1. 1 hit.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 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 promoter usage and alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q6UW56-1) [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
MAPHDPGSLT TLVPWAAALL LALGVERALA LPEICTQCPG SVQNLSKVAF
60 70 80 90 100
YCKTTRELML HARCCLNQKG TILGLDLQNC SLEDPGPNFH QAHTTVIIDL
110 120 130 140 150
QANPLKGDLA NTFRGFTQLQ TLILPQHVNC PGGINAWNTI TSYIDNQICQ
160 170 180 190 200
GQKNLCNNTG DPEMCPENGS CVPDGPGLLQ CVCADGFHGY KCMRQGSFSL
210 220
LMFFGILGAT TLSVSILLWA TQRRKAKTS
Length:229
Mass (Da):24,747
Last modified:June 16, 2009 - v2
Checksum:iCF051C5E886BCFF1
GO
Isoform 2 (identifier: Q6UW56-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-58: Missing.

Note: Produced by alternative splicing of isoform 1. No experimental confirmation available.
Show »
Length:171
Mass (Da):18,597
Checksum:i91A42CD2B2CB0883
GO
Isoform 3 (identifier: Q6UW56-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MKTSAELHEQEKPPSSPRATGPGRLGHARGRGPDALRGGAAGPGRASSGAPRERKM

Note: Produced by alternative promoter usage.
Show »
Length:284
Mass (Da):30,342
Checksum:iF7F1A5CEC82ABB39
GO

Sequence cautioni

The sequence AAD27770.1 differs from that shown. Reason: Frameshift at position 19. Curated
The sequence AAD31317.2 differs from that shown. Reason: Frameshift at position 189. Curated
The sequence AAD31317.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAH02846.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAH11006.3 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAH35850.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAX93173.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51D → G in BAF80618 (Ref. 1) Curated
Sequence conflicti5 – 51D → G in AAD27770 (PubMed:11042152).Curated
Sequence conflicti5 – 51D → G in AAQ89327 (PubMed:12975309).Curated
Sequence conflicti5 – 51D → G in AAH02846 (PubMed:15489334).Curated
Sequence conflicti5 – 51D → G in AAH11006 (PubMed:15489334).Curated
Sequence conflicti5 – 51D → G in AAH35850 (PubMed:15489334).Curated
Sequence conflicti33 – 331E → EP in AAK69412 (Ref. 3) Curated
Sequence conflicti219 – 2191W → S in BAF80618 (Ref. 1) Curated
Sequence conflicti221 – 2211T → A in AAK69412 (Ref. 3) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti209 – 2091A → S.1 Publication
Corresponds to variant rs7437 [ dbSNP | Ensembl ].
VAR_057991

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5858Missing in isoform 2. 4 PublicationsVSP_014108Add
BLAST
Alternative sequencei1 – 11M → MKTSAELHEQEKPPSSPRAT GPGRLGHARGRGPDALRGGA AGPGRASSGAPRERKM in isoform 3. 1 PublicationVSP_037521

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB009017 mRNA. Translation: BAF80618.1.
AF144055 mRNA. Translation: AAD31317.2. Sequence problems.
AF275744 mRNA. Translation: AAK69412.1.
AF077037 mRNA. Translation: AAD27770.1. Frameshift.
AY358968 mRNA. Translation: AAQ89327.1.
AK291894 mRNA. Translation: BAF84583.1.
CR600041 mRNA. No translation available.
AC013403 Genomic DNA. Translation: AAX93173.1. Sequence problems.
CH471053 Genomic DNA. Translation: EAX00617.1.
BC002846 mRNA. Translation: AAH02846.2. Different initiation.
BC011006 mRNA. Translation: AAH11006.3. Different initiation.
BC021237 mRNA. Translation: AAH21237.1.
BC035850 mRNA. Translation: AAH35850.1. Different initiation.
CCDSiCCDS1741.1. [Q6UW56-3]
CCDS46243.1. [Q6UW56-2]
CCDS62877.1. [Q6UW56-1]
RefSeqiNP_001164266.1. NM_001170795.1. [Q6UW56-1]
NP_057169.2. NM_016085.4. [Q6UW56-2]
NP_542159.3. NM_080592.3. [Q6UW56-3]
UniGeneiHs.9527.

Genome annotation databases

EnsembliENST00000380171; ENSP00000369518; ENSG00000138085. [Q6UW56-3]
ENST00000405489; ENSP00000384033; ENSG00000138085. [Q6UW56-2]
ENST00000606999; ENSP00000476080; ENSG00000138085. [Q6UW56-1]
ENST00000611786; ENSP00000484228; ENSG00000138085. [Q6UW56-3]
GeneIDi51374.
KEGGihsa:51374.
UCSCiuc002rjf.5. human. [Q6UW56-1]

Keywords - Coding sequence diversityi

Alternative promoter usage, Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB009017 mRNA. Translation: BAF80618.1.
AF144055 mRNA. Translation: AAD31317.2. Sequence problems.
AF275744 mRNA. Translation: AAK69412.1.
AF077037 mRNA. Translation: AAD27770.1. Frameshift.
AY358968 mRNA. Translation: AAQ89327.1.
AK291894 mRNA. Translation: BAF84583.1.
CR600041 mRNA. No translation available.
AC013403 Genomic DNA. Translation: AAX93173.1. Sequence problems.
CH471053 Genomic DNA. Translation: EAX00617.1.
BC002846 mRNA. Translation: AAH02846.2. Different initiation.
BC011006 mRNA. Translation: AAH11006.3. Different initiation.
BC021237 mRNA. Translation: AAH21237.1.
BC035850 mRNA. Translation: AAH35850.1. Different initiation.
CCDSiCCDS1741.1. [Q6UW56-3]
CCDS46243.1. [Q6UW56-2]
CCDS62877.1. [Q6UW56-1]
RefSeqiNP_001164266.1. NM_001170795.1. [Q6UW56-1]
NP_057169.2. NM_016085.4. [Q6UW56-2]
NP_542159.3. NM_080592.3. [Q6UW56-3]
UniGeneiHs.9527.

3D structure databases

ProteinModelPortaliQ6UW56.
SMRiQ6UW56. Positions 75-124.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119507. 3 interactions.
IntActiQ6UW56. 4 interactions.
MINTiMINT-1370379.
STRINGi9606.ENSP00000369518.

PTM databases

iPTMnetiQ6UW56.
PhosphoSiteiQ6UW56.

Polymorphism and mutation databases

BioMutaiATRAID.
DMDMi239938597.

Proteomic databases

MaxQBiQ6UW56.
PaxDbiQ6UW56.
PRIDEiQ6UW56.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000380171; ENSP00000369518; ENSG00000138085. [Q6UW56-3]
ENST00000405489; ENSP00000384033; ENSG00000138085. [Q6UW56-2]
ENST00000606999; ENSP00000476080; ENSG00000138085. [Q6UW56-1]
ENST00000611786; ENSP00000484228; ENSG00000138085. [Q6UW56-3]
GeneIDi51374.
KEGGihsa:51374.
UCSCiuc002rjf.5. human. [Q6UW56-1]

Organism-specific databases

CTDi51374.
GeneCardsiATRAID.
HGNCiHGNC:24090. ATRAID.
HPAiHPA051353.
neXtProtiNX_Q6UW56.
PharmGKBiPA134964154.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IYNU. Eukaryota.
ENOG4111PJW. LUCA.
GeneTreeiENSGT00390000017252.
HOVERGENiHBG054041.
InParanoidiQ6UW56.
OMAiGINAWNT.
OrthoDBiEOG7XWPQ5.
PhylomeDBiQ6UW56.
TreeFamiTF335766.

Miscellaneous databases

GeneWikiiC2orf28.
GenomeRNAii51374.
PROiQ6UW56.

Gene expression databases

BgeeiQ6UW56.
CleanExiHS_C2orf28.
ExpressionAtlasiQ6UW56. baseline and differential.
GenevisibleiQ6UW56. HS.

Family and domain databases

Gene3Di3.80.10.10. 1 hit.
InterProiIPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR032675. L_dom-like.
[Graphical view]
PROSITEiPS00022. EGF_1. 1 hit.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of a novel protein with four putative transmembrane domains."
    Mori K., Ogawa Y., Tashiro K., Ozaki S., Mukoyama M., Tanaka I., Nakao K.
    Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT SER-209.
    Tissue: Kidney.
  2. "Improved PCR-based subtractive hybridization strategy for cloning differentially expressed genes."
    Zhu F., Yan W., Zhao Z.L., Chai Y.B., Lu F., Wang Q., Peng W.D., Yang A.G., Wang C.J.
    BioTechniques 29:310-313(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  3. "Cloning and characterization of p18."
    Yang Y.C., Chen S.Y., Chang M.S.
    Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  4. "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 SPECIFICITY.
    Tissue: Umbilical cord blood.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  6. "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: Skeletal muscle.
  7. "Full-length cDNA libraries and normalization."
    Li W.B., Gruber C., Jessee J., Polayes D.
    Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Neuroblastoma.
  8. "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].
  9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. "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 2).
    Tissue: Brain, Placenta and Uterus.
  11. "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
    Zhang Z., Henzel W.J.
    Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 31-45.
  12. "Apoptosis related protein 3, an ATRA-upregulated membrane protein arrests the cell cycle at G1/S phase by decreasing the expression of cyclin D1."
    Yu F., Yang G., Zhao Z., Ji L., Cao Y., Bai L., Lu F., Fu H., Huang B., Li H., Zhang J., Yao L., Lu Z.
    Biochem. Biophys. Res. Commun. 358:1041-1046(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION, SUBCELLULAR LOCATION, POSSIBLE FUNCTION.
  13. "Identification of the distinct promoters for the two transcripts of apoptosis related protein 3 and their transcriptional regulation by NFAT and NFkappaB."
    Yang G., Yu F., Fu H., Lu F., Huang B., Bai L., Zhao Z., Yao L., Lu Z.
    Mol. Cell. Biochem. 302:187-194(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE PROMOTER USAGE.
  14. "NELL-1 binds to APR3 affecting human osteoblast proliferation and differentiation."
    Zou X., Shen J., Chen F., Ting K., Zheng Z., Pang S., Zara J.N., Adams J.S., Soo C., Zhang X.
    FEBS Lett. 585:2410-2418(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN OSTEOBLAST DIFFERENTIATION, INTERACTION WITH NELL1, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiARAID_HUMAN
AccessioniPrimary (citable) accession number: Q6UW56
Secondary accession number(s): A8C1S2
, A8K779, Q96FF6, Q96RT2, Q9Y2R7, Q9Y5L7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: June 16, 2009
Last modified: June 8, 2016
This is version 104 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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

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.