Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Cold shock domain-containing protein E1

Gene

CSDE1

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

Functioni

RNA-binding protein. Required for internal initiation of translation of human rhinovirus RNA. May be involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain.2 Publications

GO - Molecular functioni

  • DNA binding Source: InterPro
  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  • male gonad development Source: ProtInc
  • nuclear-transcribed mRNA catabolic process, no-go decay Source: UniProtKB
  • regulation of transcription, DNA-templated Source: InterPro
Complete GO annotation...

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Cold shock domain-containing protein E1
Alternative name(s):
N-ras upstream gene protein
Protein UNR
Gene namesi
Name:CSDE1
Synonyms:D1S155E, KIAA0885, NRU, UNR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:29905. CSDE1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142672072.

Polymorphism and mutation databases

BioMutaiCSDE1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 798798Cold shock domain-containing protein E1PRO_0000100348Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei81 – 811N6-acetyllysineCombined sources
Cross-linki91 – 91Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei123 – 1231PhosphoserineCombined sources
Modified residuei276 – 2761PhosphoserineCombined sources
Modified residuei514 – 5141PhosphoserineCombined sources
Modified residuei584 – 5841PhosphoserineCombined sources
Modified residuei761 – 7611PhosphothreonineCombined sources

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiO75534.
MaxQBiO75534.
PaxDbiO75534.
PeptideAtlasiO75534.
PRIDEiO75534.

PTM databases

iPTMnetiO75534.
PhosphoSiteiO75534.

Expressioni

Gene expression databases

BgeeiO75534.
CleanExiHS_CSDE1.
ExpressionAtlasiO75534. baseline and differential.
GenevisibleiO75534. HS.

Organism-specific databases

HPAiHPA018846.
HPA052221.

Interactioni

Subunit structurei

Component of a multi subunit autoregulatory ribonucleoprotein complex (ARC), at least composed of IGF2BP1, PABPC1 and CSDE1. Interacts with STRAP. Part of a complex associated with the FOS mCRD domain and consisting of PABPC1, PAIP1, HNRPD and SYNCRIP. The interaction with PABPC1 is direct and RNA-independent.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
FAM9BQ8IZU03EBI-719186,EBI-10175124
HID1Q8IV363EBI-719186,EBI-743438

Protein-protein interaction databases

BioGridi113583. 43 interactions.
IntActiO75534. 23 interactions.
STRINGi9606.ENSP00000407724.

Structurei

Secondary structure

1
798
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi19 – 213Combined sources
Beta strandi25 – 339Combined sources
Beta strandi35 – 428Combined sources
Turni43 – 464Combined sources
Beta strandi47 – 526Combined sources
Turni53 – 553Combined sources
Turni60 – 623Combined sources
Beta strandi69 – 757Combined sources
Beta strandi77 – 793Combined sources
Beta strandi82 – 909Combined sources
Beta strandi186 – 1905Combined sources
Beta strandi195 – 2017Combined sources
Beta strandi203 – 2053Combined sources
Beta strandi209 – 2124Combined sources
Turni213 – 2153Combined sources
Beta strandi228 – 2336Combined sources
Beta strandi237 – 2393Combined sources
Beta strandi241 – 2477Combined sources
Beta strandi349 – 3557Combined sources
Beta strandi362 – 3709Combined sources
Helixi378 – 3814Combined sources
Beta strandi391 – 3933Combined sources
Beta strandi399 – 4013Combined sources
Beta strandi519 – 5268Combined sources
Beta strandi528 – 5347Combined sources
Beta strandi536 – 5394Combined sources
Beta strandi541 – 5455Combined sources
Turni546 – 5483Combined sources
Turni553 – 5553Combined sources
Beta strandi561 – 5644Combined sources
Beta strandi676 – 6805Combined sources
Beta strandi683 – 6897Combined sources
Beta strandi693 – 7019Combined sources
Turni702 – 7043Combined sources
Beta strandi716 – 7183Combined sources
Beta strandi725 – 7273Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WFQNMR-A15-90[»]
1X65NMR-A348-423[»]
2YTVNMR-A673-738[»]
2YTXNMR-A175-258[»]
2YTYNMR-A508-582[»]
ProteinModelPortaliO75534.
SMRiO75534. Positions 16-90, 172-259, 345-424, 457-582, 673-744.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO75534.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 8762CSD 1Add
BLAST
Domaini136 – 17944CSD 2; truncatedAdd
BLAST
Domaini186 – 24560CSD 3Add
BLAST
Domaini297 – 33741CSD 4; truncatedAdd
BLAST
Domaini349 – 41062CSD 5Add
BLAST
Domaini447 – 50761CSD 6Add
BLAST
Domaini519 – 57961CSD 7Add
BLAST
Domaini610 – 67061CSD 8Add
BLAST
Domaini674 – 73562CSD 9Add
BLAST

Sequence similaritiesi

Contains 9 CSD (cold-shock) domains.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410IF27. Eukaryota.
ENOG410ZH8Y. LUCA.
GeneTreeiENSGT00390000016950.
HOGENOMiHOG000013035.
HOVERGENiHBG013042.
InParanoidiO75534.
OMAiLFFHMSE.
OrthoDBiEOG725DGS.
PhylomeDBiO75534.
TreeFamiTF324707.

Family and domain databases

Gene3Di2.40.50.140. 6 hits.
InterProiIPR019844. Cold-shock_CS.
IPR011129. Cold_shock_prot.
IPR002059. CSP_DNA-bd.
IPR012340. NA-bd_OB-fold.
IPR024642. SUZ-C.
[Graphical view]
PfamiPF00313. CSD. 5 hits.
PF12901. SUZ-C. 1 hit.
[Graphical view]
SMARTiSM00357. CSP. 5 hits.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 5 hits.
PROSITEiPS00352. COLD_SHOCK. 4 hits.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O75534-1) [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
MSFDPNLLHN NGHNGYPNGT SAALRETGVI EKLLTSYGFI QCSERQARLF
60 70 80 90 100
FHCSQYNGNL QDLKVGDDVE FEVSSDRRTG KPIAVKLVKI KQEILPEERM
110 120 130 140 150
NGQVVCAVPH NLESKSPAAP GQSPTGSVCY ERNGEVFYLT YTPEDVEGNV
160 170 180 190 200
QLETGDKINF VIDNNKHTGA VSARNIMLLK KKQARCQGVV CAMKEAFGFI
210 220 230 240 250
ERGDVVKEIF FHYSEFKGDL ETLQPGDDVE FTIKDRNGKE VATDVRLLPQ
260 270 280 290 300
GTVIFEDISI EHFEGTVTKV IPKVPSKNQN DPLPGRIKVD FVIPKELPFG
310 320 330 340 350
DKDTKSKVTL LEGDHVRFNI STDRRDKLER ATNIEVLSNT FQFTNEAREM
360 370 380 390 400
GVIAAMRDGF GFIKCVDRDV RMFFHFSEIL DGNQLHIADE VEFTVVPDML
410 420 430 440 450
SAQRNHAIRI KKLPKGTVSF HSHSDHRFLG TVEKEATFSN PKTTSPNKGK
460 470 480 490 500
EKEAEDGIIA YDDCGVKLTI AFQAKDVEGS TSPQIGDKVE FSISDKQRPG
510 520 530 540 550
QQVATCVRLL GRNSNSKRLL GYVATLKDNF GFIETANHDK EIFFHYSEFS
560 570 580 590 600
GDVDSLELGD MVEYSLSKGK GNKVSAEKVN KTHSVNGITE EADPTIYSGK
610 620 630 640 650
VIRPLRSVDP TQTEYQGMIE IVEEGDMKGE VYPFGIVGMA NKGDCLQKGE
660 670 680 690 700
SVKFQLCVLG QNAQTMAYNI TPLRRATVEC VKDQFGFINY EVGDSKKLFF
710 720 730 740 750
HVKEVQDGIE LQAGDEVEFS VILNQRTGKC SACNVWRVCE GPKAVAAPRP
760 770 780 790
DRLVNRLKNI TLDDASAPRL MVLRQPRGPD NSMGFGAERK IRQAGVID
Length:798
Mass (Da):88,885
Last modified:December 1, 2000 - v2
Checksum:i2BD0B32F33D454DA
GO
Isoform 2 (identifier: O75534-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     104-134: Missing.

Note: No experimental confirmation available.
Show »
Length:767
Mass (Da):85,747
Checksum:iA18690E29F04023F
GO
Isoform 3 (identifier: O75534-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MENVFTVSSDPHPSPAAPPSLSLPLSSSSTSSGTKKQKRTPTYQRSM
     104-134: Missing.

Note: No experimental confirmation available.
Show »
Length:813
Mass (Da):90,605
Checksum:i676BE7B660D395F5
GO
Isoform 4 (identifier: O75534-4) [UniParc]FASTAAdd to basket

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

Show »
Length:844
Mass (Da):93,742
Checksum:i6038A89D02384C0E
GO

Sequence cautioni

The sequence BAA74908.2 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAH18231.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti31 – 311E → G in AAD27787 (PubMed:10931946).Curated
Sequence conflicti92 – 954QEIL → TRNP in AAD27787 (PubMed:10931946).Curated
Sequence conflicti152 – 1521L → P in CAH18231 (PubMed:17974005).Curated
Sequence conflicti243 – 2431T → P in AAD27787 (PubMed:10931946).Curated
Sequence conflicti276 – 2761S → G in CAH18269 (PubMed:17974005).Curated
Sequence conflicti299 – 2991F → L in CAH18269 (PubMed:17974005).Curated
Sequence conflicti363 – 38523IKCVD…DGNQL → HPSVWIRECSVCSFPLPVKF WMGTSS in AAD27787 (PubMed:10931946).CuratedAdd
BLAST
Sequence conflicti608 – 6081V → I in CAH18269 (PubMed:17974005).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MENVFTVSSDPHPSPAAPPS LSLPLSSSSTSSGTKKQKRT PTYQRSM in isoform 3 and isoform 4. 1 PublicationVSP_045615
Alternative sequencei104 – 13431Missing in isoform 2 and isoform 3. 5 PublicationsVSP_001138Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF077054 mRNA. Translation: AAD27787.1.
AB020692 mRNA. Translation: BAA74908.2. Different initiation.
AK290146 mRNA. Translation: BAF82835.1.
CR749378 mRNA. Translation: CAH18231.1. Different initiation.
CR749431 mRNA. Translation: CAH18269.1.
AL096773 Genomic DNA. Translation: CAI18825.1.
AL096773 Genomic DNA. Translation: CAI18826.1.
CH471122 Genomic DNA. Translation: EAW56612.1.
CH471122 Genomic DNA. Translation: EAW56616.1.
BC032446 mRNA. Translation: AAH32446.1.
AF070542 mRNA. Translation: AAC28634.1.
CCDSiCCDS30811.1. [O75534-2]
CCDS30812.1. [O75534-1]
CCDS44197.1. [O75534-3]
CCDS55626.1. [O75534-4]
PIRiS29815.
RefSeqiNP_001007554.1. NM_001007553.2. [O75534-1]
NP_001123995.1. NM_001130523.2. [O75534-3]
NP_001229820.1. NM_001242891.1. [O75534-4]
NP_001229821.1. NM_001242892.1. [O75534-1]
NP_001229822.1. NM_001242893.1. [O75534-2]
NP_009089.4. NM_007158.5. [O75534-2]
UniGeneiHs.69855.
Hs.731496.

Genome annotation databases

EnsembliENST00000261443; ENSP00000261443; ENSG00000009307. [O75534-2]
ENST00000339438; ENSP00000342408; ENSG00000009307. [O75534-2]
ENST00000358528; ENSP00000351329; ENSG00000009307. [O75534-1]
ENST00000369530; ENSP00000358543; ENSG00000009307. [O75534-3]
ENST00000438362; ENSP00000407724; ENSG00000009307. [O75534-4]
ENST00000534699; ENSP00000432958; ENSG00000009307. [O75534-1]
ENST00000610726; ENSP00000481762; ENSG00000009307. [O75534-4]
GeneIDi7812.
KEGGihsa:7812.
UCSCiuc001efi.4. human. [O75534-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF077054 mRNA. Translation: AAD27787.1.
AB020692 mRNA. Translation: BAA74908.2. Different initiation.
AK290146 mRNA. Translation: BAF82835.1.
CR749378 mRNA. Translation: CAH18231.1. Different initiation.
CR749431 mRNA. Translation: CAH18269.1.
AL096773 Genomic DNA. Translation: CAI18825.1.
AL096773 Genomic DNA. Translation: CAI18826.1.
CH471122 Genomic DNA. Translation: EAW56612.1.
CH471122 Genomic DNA. Translation: EAW56616.1.
BC032446 mRNA. Translation: AAH32446.1.
AF070542 mRNA. Translation: AAC28634.1.
CCDSiCCDS30811.1. [O75534-2]
CCDS30812.1. [O75534-1]
CCDS44197.1. [O75534-3]
CCDS55626.1. [O75534-4]
PIRiS29815.
RefSeqiNP_001007554.1. NM_001007553.2. [O75534-1]
NP_001123995.1. NM_001130523.2. [O75534-3]
NP_001229820.1. NM_001242891.1. [O75534-4]
NP_001229821.1. NM_001242892.1. [O75534-1]
NP_001229822.1. NM_001242893.1. [O75534-2]
NP_009089.4. NM_007158.5. [O75534-2]
UniGeneiHs.69855.
Hs.731496.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WFQNMR-A15-90[»]
1X65NMR-A348-423[»]
2YTVNMR-A673-738[»]
2YTXNMR-A175-258[»]
2YTYNMR-A508-582[»]
ProteinModelPortaliO75534.
SMRiO75534. Positions 16-90, 172-259, 345-424, 457-582, 673-744.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113583. 43 interactions.
IntActiO75534. 23 interactions.
STRINGi9606.ENSP00000407724.

PTM databases

iPTMnetiO75534.
PhosphoSiteiO75534.

Polymorphism and mutation databases

BioMutaiCSDE1.

Proteomic databases

EPDiO75534.
MaxQBiO75534.
PaxDbiO75534.
PeptideAtlasiO75534.
PRIDEiO75534.

Protocols and materials databases

DNASUi7812.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000261443; ENSP00000261443; ENSG00000009307. [O75534-2]
ENST00000339438; ENSP00000342408; ENSG00000009307. [O75534-2]
ENST00000358528; ENSP00000351329; ENSG00000009307. [O75534-1]
ENST00000369530; ENSP00000358543; ENSG00000009307. [O75534-3]
ENST00000438362; ENSP00000407724; ENSG00000009307. [O75534-4]
ENST00000534699; ENSP00000432958; ENSG00000009307. [O75534-1]
ENST00000610726; ENSP00000481762; ENSG00000009307. [O75534-4]
GeneIDi7812.
KEGGihsa:7812.
UCSCiuc001efi.4. human. [O75534-1]

Organism-specific databases

CTDi7812.
GeneCardsiCSDE1.
HGNCiHGNC:29905. CSDE1.
HPAiHPA018846.
HPA052221.
MIMi191510. gene.
neXtProtiNX_O75534.
PharmGKBiPA142672072.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IF27. Eukaryota.
ENOG410ZH8Y. LUCA.
GeneTreeiENSGT00390000016950.
HOGENOMiHOG000013035.
HOVERGENiHBG013042.
InParanoidiO75534.
OMAiLFFHMSE.
OrthoDBiEOG725DGS.
PhylomeDBiO75534.
TreeFamiTF324707.

Miscellaneous databases

ChiTaRSiCSDE1. human.
EvolutionaryTraceiO75534.
GeneWikiiCSDE1.
GenomeRNAii7812.
PROiO75534.
SOURCEiSearch...

Gene expression databases

BgeeiO75534.
CleanExiHS_CSDE1.
ExpressionAtlasiO75534. baseline and differential.
GenevisibleiO75534. HS.

Family and domain databases

Gene3Di2.40.50.140. 6 hits.
InterProiIPR019844. Cold-shock_CS.
IPR011129. Cold_shock_prot.
IPR002059. CSP_DNA-bd.
IPR012340. NA-bd_OB-fold.
IPR024642. SUZ-C.
[Graphical view]
PfamiPF00313. CSD. 5 hits.
PF12901. SUZ-C. 1 hit.
[Graphical view]
SMARTiSM00357. CSP. 5 hits.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 5 hits.
PROSITEiPS00352. COLD_SHOCK. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Organization of the human N-ras locus: characterization of a gene located immediately upstream of N-ras."
    Nicolaiew N., Triqueneaux G., Dautry F.
    Oncogene 6:721-730(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Pituitary.
  3. "Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 5:355-364(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  4. "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).
    Tissue: Thalamus.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
    Tissue: Liver.
  6. "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(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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: Cervix.
  9. Yu W., Gibbs R.A.
    Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-498 (ISOFORM 2).
    Tissue: Brain.
  10. "Exon skipping in the expression of the gene immediately upstream of N-ras (unr/NRU)."
    Boussadia O., Jacquemin-Sablon H., Dautry F.
    Biochim. Biophys. Acta 1172:64-72(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 67-166, ALTERNATIVE SPLICING.
  11. "unr, a cellular cytoplasmic RNA-binding protein with five cold-shock domains, is required for internal initiation of translation of human rhinovirus RNA."
    Hunt S.L., Hsuan J.J., Totty N., Jackson R.J.
    Genes Dev. 13:437-448(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH STRAP.
  12. "A mechanism for translationally coupled mRNA turnover: interaction between the poly(A) tail and a c-fos RNA coding determinant via a protein complex."
    Grosset C., Chen C.-Y.A., Xu N., Sonenberg N., Jacquemin-Sablon H., Shyu A.-B.
    Cell 103:29-40(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN TRANSLATIONALLY COUPLED MRNA TURNOVER, IDENTIFICATION IN A COMPLEX WITH HNRPD; SYNCRIP; PABPC1 AND PAIP1.
  13. "UNR, a new partner of poly(A)-binding protein, plays a key role in translationally coupled mRNA turnover mediated by the c-fos major coding-region determinant."
    Chang T.-C., Yamashita A., Chen C.-Y.A., Yamashita Y., Zhu W., Durdan S., Kahvejian A., Sonenberg N., Shyu A.-B.
    Genes Dev. 18:2010-2023(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PABPC1.
  14. "The autoregulatory translational control element of poly(A)-binding protein mRNA forms a heteromeric ribonucleoprotein complex."
    Patel G.P., Ma S., Bag J.
    Nucleic Acids Res. 33:7074-7089(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A MRNP COMPLEX WITH IGF2BP1 AND PABPC1.
  15. "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.
  16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. "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].
  18. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-81, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "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-514, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "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-514, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "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-123; SER-276; SER-584 AND THR-761, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  24. "Uncovering global SUMOylation signaling networks in a site-specific manner."
    Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., Vertegaal A.C.
    Nat. Struct. Mol. Biol. 21:927-936(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-91, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. "The NMR solution structures of the five constituent cold-shock domains (CSD) of the human UNR (upstream of N-ras) protein."
    Goroncy A.K., Koshiba S., Tochio N., Tomizawa T., Inoue M., Watanabe S., Harada T., Tanaka A., Ohara O., Kigawa T., Yokoyama S.
    J. Struct. Funct. Genomics 11:181-188(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 15-90; 175-259; 348-424; 508-582 AND 673-738.

Entry informationi

Entry nameiCSDE1_HUMAN
AccessioniPrimary (citable) accession number: O75534
Secondary accession number(s): A8K281
, E9PGZ0, G5E9Q2, O94961, Q5TF04, Q5TF05, Q68DF1, Q68DI9, Q9Y2S4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: December 1, 2000
Last modified: July 6, 2016
This is version 170 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.