Reviewed, UniProtKB/Swiss-Prot O75534 (CSDE1_HUMAN)

Names and origin

Protein names

Recommended name:
    Cold shock domain-containing protein E1
Alternative name(s):
    UNR protein
    N-ras upstream gene protein

Gene names

Name:	CSDE1
Synonyms:	D1S155E, KIAA0885, NRU, UNR

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	798 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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. Ref.12 Ref.13
Subunit structure	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. Ref.13 Ref.11
Subcellular location	Cytoplasm.
Sequence similarities	Contains 9 CSD (cold-shock) domains.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing
Domain	Repeat
Ligand	RNA-binding
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	male gonad development Traceable author statement. Source: ProtInc regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	DNA binding Inferred from electronic annotation. Source: InterPro RNA binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NCK1	P16333	1	EBI-719186,EBI-389883
PIK3R1	P27986	1	EBI-719186,EBI-79464

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform Long (identifier: O75534-1)

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.

Isoform Short (identifier: O75534-2)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 798

798

Cold shock domain-containing protein E1

PRO_0000100348

Regions

Domain

26 – 87

62

CSD 1

Domain

136 – 179

44

CSD 2; truncated

Domain

186 – 245

60

CSD 3

Domain

297 – 337

41

CSD 4; truncated

Domain

349 – 410

62

CSD 5

Domain

447 – 507

61

CSD 6

Domain

519 – 579

61

CSD 7

Domain

610 – 670

61

CSD 8

Domain

674 – 735

62

CSD 9

Amino acid modifications

Modified residue

81

1

N6-acetyllysine Ref.19

Modified residue

116

1

Phosphoserine Ref.17

Modified residue

123

1

Phosphoserine Ref.17

Modified residue

444

1

Phosphothreonine Ref.16

Modified residue

445

1

Phosphoserine Ref.16

Modified residue

514

1

Phosphoserine Ref.15

Natural variations

Alternative sequence

104 – 134

31

Missing in isoform Short.

VSP_001138

Experimental info

Sequence conflict

31

1

E → G in AAD27787. Ref.2

Sequence conflict

92 – 95

4

QEIL → TRNP in AAD27787. Ref.2

Sequence conflict

152

1

L → P in CAH18231. Ref.5

Sequence conflict

243

1

T → P in AAD27787. Ref.2

Sequence conflict

363 – 385

23

IKCVD…DGNQL → HPSVWIRECSVCSFPLPVKF WMGTSS in AAD27787. Ref.2

Secondary structure

1

.

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798

Helix Strand Turn

Details...

Beta strand

19 – 21

3

Beta strand

25 – 33

9

Beta strand

35 – 42

8

Turn

43 – 46

4

Beta strand

47 – 52

6

Turn

53 – 55

3

Turn

60 – 62

3

Beta strand

69 – 75

7

Beta strand

77 – 79

3

Beta strand

82 – 90

9

Beta strand

349 – 355

7

Beta strand

362 – 370

9

Helix

378 – 381

4

Beta strand

391 – 393

3

Beta strand

399 – 401

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform Long [UniParc]. Last modified December 1, 2000. Version 2. Checksum: 2BD0B32F33D454DA	FASTA	798	88,885
	10 20 30 40 50 60 MSFDPNLLHN NGHNGYPNGT SAALRETGVI EKLLTSYGFI QCSERQARLF FHCSQYNGNL 70 80 90 100 110 120 QDLKVGDDVE FEVSSDRRTG KPIAVKLVKI KQEILPEERM NGQVVCAVPH NLESKSPAAP 130 140 150 160 170 180 GQSPTGSVCY ERNGEVFYLT YTPEDVEGNV QLETGDKINF VIDNNKHTGA VSARNIMLLK 190 200 210 220 230 240 KKQARCQGVV CAMKEAFGFI ERGDVVKEIF FHYSEFKGDL ETLQPGDDVE FTIKDRNGKE 250 260 270 280 290 300 VATDVRLLPQ GTVIFEDISI EHFEGTVTKV IPKVPSKNQN DPLPGRIKVD FVIPKELPFG 310 320 330 340 350 360 DKDTKSKVTL LEGDHVRFNI STDRRDKLER ATNIEVLSNT FQFTNEAREM GVIAAMRDGF 370 380 390 400 410 420 GFIKCVDRDV RMFFHFSEIL DGNQLHIADE VEFTVVPDML SAQRNHAIRI KKLPKGTVSF 430 440 450 460 470 480 HSHSDHRFLG TVEKEATFSN PKTTSPNKGK EKEAEDGIIA YDDCGVKLTI AFQAKDVEGS 490 500 510 520 530 540 TSPQIGDKVE FSISDKQRPG QQVATCVRLL GRNSNSKRLL GYVATLKDNF GFIETANHDK 550 560 570 580 590 600 EIFFHYSEFS GDVDSLELGD MVEYSLSKGK GNKVSAEKVN KTHSVNGITE EADPTIYSGK 610 620 630 640 650 660 VIRPLRSVDP TQTEYQGMIE IVEEGDMKGE VYPFGIVGMA NKGDCLQKGE SVKFQLCVLG 670 680 690 700 710 720 QNAQTMAYNI TPLRRATVEC VKDQFGFINY EVGDSKKLFF HVKEVQDGIE LQAGDEVEFS 730 740 750 760 770 780 VILNQRTGKC SACNVWRVCE GPKAVAAPRP DRLVNRLKNI TLDDASAPRL MVLRQPRGPD 790 NSMGFGAERK IRQAGVID
	Isoform Short. Checksum: A18690E29F04023F	FASTA	767	85,747
	10 20 30 40 50 60 MSFDPNLLHN NGHNGYPNGT SAALRETGVI EKLLTSYGFI QCSERQARLF FHCSQYNGNL 70 80 90 100 110 120 QDLKVGDDVE FEVSSDRRTG KPIAVKLVKI KQEILPEERM NGQEVFYLTY TPEDVEGNVQ 130 140 150 160 170 180 LETGDKINFV IDNNKHTGAV SARNIMLLKK KQARCQGVVC AMKEAFGFIE RGDVVKEIFF 190 200 210 220 230 240 HYSEFKGDLE TLQPGDDVEF TIKDRNGKEV ATDVRLLPQG TVIFEDISIE HFEGTVTKVI 250 260 270 280 290 300 PKVPSKNQND PLPGRIKVDF VIPKELPFGD KDTKSKVTLL EGDHVRFNIS TDRRDKLERA 310 320 330 340 350 360 TNIEVLSNTF QFTNEAREMG VIAAMRDGFG FIKCVDRDVR MFFHFSEILD GNQLHIADEV 370 380 390 400 410 420 EFTVVPDMLS AQRNHAIRIK KLPKGTVSFH SHSDHRFLGT VEKEATFSNP KTTSPNKGKE 430 440 450 460 470 480 KEAEDGIIAY DDCGVKLTIA FQAKDVEGST SPQIGDKVEF SISDKQRPGQ QVATCVRLLG 490 500 510 520 530 540 RNSNSKRLLG YVATLKDNFG FIETANHDKE IFFHYSEFSG DVDSLELGDM VEYSLSKGKG 550 560 570 580 590 600 NKVSAEKVNK THSVNGITEE ADPTIYSGKV IRPLRSVDPT QTEYQGMIEI VEEGDMKGEV 610 620 630 640 650 660 YPFGIVGMAN KGDCLQKGES VKFQLCVLGQ NAQTMAYNIT PLRRATVECV KDQFGFINYE 670 680 690 700 710 720 VGDSKKLFFH VKEVQDGIEL QAGDEVEFSV ILNQRTGKCS ACNVWRVCEG PKAVAAPRPD 730 740 750 760 RLVNRLKNIT LDDASAPRLM VLRQPRGPDN SMGFGAERKI RQAGVID

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 2052355] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
[2]	Song H., Peng Y., Zhou J., Huang Q., Dai M., Mao Y., Yu Y., Xu X., Luo M., Hu R., Chen J. Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT). 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: 10048485] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG). 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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG). Tissue: Thalamus.
[5]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG). 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: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT). 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 SHORT). 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: 8439573] [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: 10049359] [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: 11051545] [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: 15314026] [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: 16356927] [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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-514, MASS SPECTROMETRY. Tissue: Epithelium.
[16]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-444 AND SER-445, MASS SPECTROMETRY.
[17]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116 AND SER-123, MASS SPECTROMETRY.
[18]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[19]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-81, MASS SPECTROMETRY.
[20]	"Solution structure of the first and third cold-shock domains of the human KIAA0885 protein (UNR protein)." RIKEN structural genomics initiative (RSGI) Submitted (NOV-2005) to the PDB data bank Cited for: STRUCTURE BY NMR OF 15-90 AND 348-424.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AF077054 mRNA. Translation: AAD27787.1.
AB020692 mRNA. Translation: BAA74908.2. Different initiation.
AK290146 mRNA. Translation: BAF82835.1.
CR749378 mRNA. Translation: CAH18231.1. Different initiation.
AL096773 Genomic DNA. Translation: CAI18825.1.
AL096773 Genomic DNA. Translation: CAI18826.1.
CH471122 Genomic DNA. Translation: EAW56612.1.
BC032446 mRNA. Translation: AAH32446.1.
AF070542 mRNA. Translation: AAC28634.1.

IPI

IPI00470891.
IPI00873244.

PIR

S29815.

RefSeq

NP_001007554.1.
NP_001123995.1.
NP_009089.4.

UniGene

Hs.486502
Hs.713562

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1WFQ	NMR	-	A	15-90	[»]
1X65	NMR	-	A	348-423	[»]
2YTV	NMR	-	A	673-738	[»]
2YTX	NMR	-	A	175-259	[»]
2YTY	NMR	-	A	508-582	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

O75534. 10 interactions.

STRING

O75534.

PTM databases

PhosphoSite

O75534.

Proteomic databases

PRIDE

O75534.

Genome annotation databases

Ensembl

ENST00000261443; ENSP00000261443; ENSG00000009307; Homo sapiens. [Genome view]
ENST00000339438; ENSP00000342408; ENSG00000009307; Homo sapiens. [Genome view]
ENST00000358528; ENSP00000351329; ENSG00000009307; Homo sapiens. [Genome view]
ENST00000369530; ENSP00000358543; ENSG00000009307; Homo sapiens. [Genome view]
ENST00000369533; ENSP00000358546; ENSG00000009307; Homo sapiens. [Genome view]
ENST00000438362; ENSP00000407724; ENSG00000009307; Homo sapiens. [Genome view]

GeneID

7812.

KEGG

hsa:7812.

UCSC

uc001efk.1. human.
uc001efl.1. human.

Organism-specific databases

CTD

7812.

GeneCards

GC01M115049.

H-InvDB

HIX0000915.

HGNC

HGNC:29905. CSDE1.

HPA

HPA018846.

MIM

191510. gene.

PharmGKB

PA142672072.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

O75534.

Gene expression databases

ArrayExpress

O75534.

Bgee

O75534.

CleanEx

HS_CSDE1.

Genevestigator

O75534.

GermOnline

ENSG00000009307. Homo sapiens.

Family and domain databases

InterPro

IPR019844. Cold-shock_CS.
IPR011129. Cold_shock_prot.
IPR002059. CSP_DNA_bd.
[Graphical view]

Pfam

PF00313. CSD. 5 hits.
[Graphical view]

SMART

SM00357. CSP. 5 hits.
[Graphical view]

PROSITE

PS00352. COLD_SHOCK. 4 hits.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

30207.

SOURCE

Search...

Entry information

Entry name

CSDE1_HUMAN

Accession

Primary (citable) accession number: O75534
Secondary accession number(s): A8K281 , O94961, Q5TF04, Q5TF05, Q68DI9, Q9Y2S4

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	December 1, 2000
Last modified:	October 13, 2009
This is version 103 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.