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Q14493

- SLBP_HUMAN

UniProt

Q14493 - SLBP_HUMAN

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Protein

Histone RNA hairpin-binding protein

Gene

SLBP

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

Functioni

RNA-binding protein involved in the histone pre-mRNA processing. Binds the stem-loop structure of replication-dependent histone pre-mRNAs and contributes to efficient 3'-end processing by stabilizing the complex between histone pre-mRNA and U7 small nuclear ribonucleoprotein (snRNP), via the histone downstream element (HDE). Plays an important role in targeting mature histone mRNA from the nucleus to the cytoplasm and to the translation machinery. Stabilizes mature histone mRNA and could be involved in cell-cycle regulation of histone gene expression. Involved in the mechanism by which growing oocytes accumulate histone proteins that support early embryogenesis. Binds to the 5' side of the stem-loop structure of histone pre-mRNAs.2 Publications

GO - Molecular functioni

  1. histone pre-mRNA DCP binding Source: UniProtKB
  2. histone pre-mRNA stem-loop binding Source: UniProtKB
  3. mRNA binding Source: UniProtKB
  4. poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  1. gene expression Source: Reactome
  2. histone mRNA 3'-end processing Source: UniProtKB
  3. histone mRNA metabolic process Source: Reactome
  4. mRNA 3'-end processing Source: Reactome
  5. mRNA export from nucleus Source: Reactome
  6. mRNA transport Source: UniProtKB
  7. nuclear cell cycle DNA replication Source: UniProtKB
  8. termination of RNA polymerase II transcription Source: Reactome
  9. transcription from RNA polymerase II promoter Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Biological processi

mRNA processing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_1364. SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs.
REACT_405. Transport of the SLBP Dependant Mature mRNA.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone RNA hairpin-binding protein
Alternative name(s):
Histone stem-loop-binding protein
Gene namesi
Name:SLBP
Synonyms:HBP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:10904. SLBP.

Subcellular locationi

Cytoplasm. Nucleus
Note: Polyribosome-associated. Localizes predominantly in the nucleus at the G1/G2 phases and the beginning of S phase. Through the S phase, partially redistributes to the cytoplasm. Binding to histone mRNA is necessary for cytoplasmic localization. Shuttles between the nucleus and the cytoplasm. Imported in the nucleus by the Importin alpha/Importin beta receptor.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. histone pre-mRNA 3'end processing complex Source: UniProtKB
  4. nucleoplasm Source: Reactome
  5. nucleus Source: UniProtKB
  6. ribonucleoprotein complex Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi31 – 344RKRR → AAAA: Reduces interaction with the importin alpha/importin beta receptor. Abolishes interaction with the importin alpha/importin beta receptor; when associated with A-96; A-97; A-98 and A-99 or with A-241; A-242; A-243 and A-244. 1 Publication
Mutagenesisi59 – 635SFTTP → AAAA: Does not increase its stability at the end of the S phase and through G2 and mitosis. 1 Publication
Mutagenesisi59 – 591S → A: Does not increase its stability at the end of the S phase and through G2 and mitosis. 1 Publication
Mutagenesisi61 – 611T → A: Increases its stability at the end of the S phase and through G2 and mitosis. Active in histone pre-mRNA processing during the G2 phase. 2 Publications
Mutagenesisi62 – 621T → A: Increases its stability at the end of the S phase and through G2 and mitosis. 2 Publications
Mutagenesisi63 – 631P → A: Increases its stability at the end of the S phase and through G2 and mitosis. 1 Publication
Mutagenesisi96 – 994KRKL → AAAA: Increases its stability at the end of the S phase and through G2 and mitosis. Inhibits phosphorylation of T-62. Localizes in the nucleus. Reduces interaction with the importin alpha/importin beta receptor. Abolishes interaction with the importin alpha/importin beta receptor; when associated with A-31; A-32; A-33 and A-34 or with A-241; A-242; A-243 and A-244. 3 Publications
Mutagenesisi137 – 1371R → A: Inhibits histone RNA-binding and localization to the cytoplasm. 1 Publication
Mutagenesisi138 – 1381R → A: Inhibits histone RNA-binding and localization to the cytoplasm. 1 Publication
Mutagenesisi230 – 27041Missing: Decrease in 3'-end processing efficiency. 1 PublicationAdd
BLAST
Mutagenesisi241 – 2444KVRH → AAAA: Reduces interaction with the importin alpha/importin beta receptor. Abolishes interaction with the importin alpha/importin beta receptor; when associated with A-31; A-32; A-33 and A-34 or with A-96; A-97; A-98 and A-99. 1 Publication

Organism-specific databases

PharmGKBiPA35804.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 270270Histone RNA hairpin-binding proteinPRO_0000100356Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei20 – 201Phosphoserine1 Publication
Modified residuei23 – 231Phosphoserine1 Publication
Modified residuei61 – 611Phosphothreonine; by CK22 Publications
Modified residuei62 – 621Phosphothreonine; by CDK12 Publications
Modified residuei171 – 1711Phosphothreonine1 Publication
Modified residuei182 – 1821Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated on Thr-61 and Thr-62 in the S-phase. Phosphorylation of Thr-62 by CDK1 primes phosphorylation of Thr-61 by CK2. Phosphorylation of Thr-62 is required for its degradation by the proteasome at the end of the S phase. Its degradation is not required for histone mRNA degradation at the end of the S phase. All the phosphorylated forms detected are present in the cytoplasm. Both unphosphorylated and phosphorylated forms bind the stem-loop structure of histone mRNAs. Phosphorylation at Thr-171 increases affinity for histone mRNAs.5 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ14493.
PaxDbiQ14493.
PeptideAtlasiQ14493.
PRIDEiQ14493.

PTM databases

PhosphoSiteiQ14493.

Expressioni

Tissue specificityi

Widely expressed.

Developmental stagei

Regulated during the cell cycle: protein levels increase 10 to 20 fold in the late G1 and decrease at the S/G2 border.

Gene expression databases

BgeeiQ14493.
CleanExiHS_SLBP.
ExpressionAtlasiQ14493. baseline and differential.
GenevestigatoriQ14493.

Organism-specific databases

HPAiHPA019254.

Interactioni

Subunit structurei

Monomer. SLBP/pre-mRNA complex interacts with ZNF473. Interacts with the Importin alpha/Importin beta receptor, LSM1, MIF4GD, TNPO3 and UPF1. Interaction with LSM1 occurs when histone mRNA is being rapidly degraded during the S phase. Found in a ternary complex with ERI1 and the stem-loop structure of the 3' end of histone mRNA. Associates with polyribosomes. Identified in a histone pre-mRNA complex, at least composed of ERI1, LSM11, SLBP, SNRPB, SYNCRIP and YBX1 (By similarity). Binds in a cooperative manner with ERI1 to the mature 3'-end of histone mRNAs (By similarity).By similarity

Protein-protein interaction databases

BioGridi113627. 7 interactions.
DIPiDIP-57045N.
IntActiQ14493. 3 interactions.
STRINGi9606.ENSP00000417686.

Structurei

Secondary structure

1
270
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi132 – 14615
Helixi149 – 1579
Helixi180 – 19415
Helixi195 – 1973

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KJMNMR-A129-158[»]
4L8RX-ray2.60C125-223[»]
4QOZX-ray2.30C125-223[»]
ProteinModelPortaliQ14493.
SMRiQ14493. Positions 127-199.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ14493.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni129 – 19870RNA-bindingAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi31 – 344Nuclear localization signal NLS1
Motifi96 – 994Nuclear localization signal NLS2

Domaini

Amino acids 31-34, 96-99 and 241-244 are necessary for interaction with the Importin alpha/Importin beta receptor. The first 18 amino acids, amino acids 69-76 and 179-182 are necessary for interaction with TNPO3. Amino acids 31-34, 96-99 and 241-244 are necessary for nuclear localization.

Sequence similaritiesi

Belongs to the SLBP family.Curated

Phylogenomic databases

eggNOGiNOG278381.
GeneTreeiENSGT00390000008738.
HOGENOMiHOG000065710.
HOVERGENiHBG017805.
InParanoidiQ14493.
OrthoDBiEOG789CF1.
PhylomeDBiQ14493.
TreeFamiTF316521.

Family and domain databases

InterProiIPR026502. SLBP1/SLBP2.
IPR029344. SLBP_RNA_bind.
[Graphical view]
PANTHERiPTHR17408. PTHR17408. 1 hit.
PfamiPF15247. SLBP_RNA_bind. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q14493-1) [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
MACRPRSPPR HQSRCDGDAS PPSPARWSLG RKRRADGRRW RPEDAEEAEH
60 70 80 90 100
RGAERRPESF TTPEGPKPRS RCSDWASAVE EDEMRTRVNK EMARYKRKLL
110 120 130 140 150
INDFGRERKS SSGSSDSKES MSTVPADFET DESVLMRRQK QINYGKNTIA
160 170 180 190 200
YDRYIKEVPR HLRQPGIHPK TPNKFKKYSR RSWDQQIKLW KVALHFWDPP
210 220 230 240 250
AEEGCDLQEI HPVDLESAES SSEPQTSSQD DFDVYSGTPT KVRHMDSQVE
260 270
DEFDLEACLT EPLRDFSAMS
Length:270
Mass (Da):31,286
Last modified:November 1, 1996 - v1
Checksum:i4E84E502393D1BF7
GO
Isoform 2 (identifier: Q14493-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     20-58: Missing.

Show »
Length:231
Mass (Da):26,695
Checksum:i09C5137F52AC416D
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei20 – 5839Missing in isoform 2. 1 PublicationVSP_042164Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M63544 Genomic DNA. No translation available.
U75679 mRNA. Translation: AAB97091.1.
Z71188 mRNA. Translation: CAA94918.1.
AK091735 mRNA. Translation: BAG52407.1.
AC016773 Genomic DNA. No translation available.
CH471131 Genomic DNA. Translation: EAW82579.1.
BC014908 mRNA. Translation: AAH14908.1.
BC015703 mRNA. Translation: AAH15703.1.
CCDSiCCDS3350.1. [Q14493-1]
RefSeqiNP_006518.1. NM_006527.2. [Q14493-1]
UniGeneiHs.298345.

Genome annotation databases

EnsembliENST00000429429; ENSP00000406322; ENSG00000163950. [Q14493-2]
ENST00000489418; ENSP00000417686; ENSG00000163950. [Q14493-1]
GeneIDi7884.
KEGGihsa:7884.
UCSCiuc003gdi.1. human. [Q14493-1]
uc003gdk.1. human. [Q14493-2]

Polymorphism databases

DMDMi9789785.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M63544 Genomic DNA. No translation available.
U75679 mRNA. Translation: AAB97091.1 .
Z71188 mRNA. Translation: CAA94918.1 .
AK091735 mRNA. Translation: BAG52407.1 .
AC016773 Genomic DNA. No translation available.
CH471131 Genomic DNA. Translation: EAW82579.1 .
BC014908 mRNA. Translation: AAH14908.1 .
BC015703 mRNA. Translation: AAH15703.1 .
CCDSi CCDS3350.1. [Q14493-1 ]
RefSeqi NP_006518.1. NM_006527.2. [Q14493-1 ]
UniGenei Hs.298345.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2KJM NMR - A 129-158 [» ]
4L8R X-ray 2.60 C 125-223 [» ]
4QOZ X-ray 2.30 C 125-223 [» ]
ProteinModelPortali Q14493.
SMRi Q14493. Positions 127-199.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113627. 7 interactions.
DIPi DIP-57045N.
IntActi Q14493. 3 interactions.
STRINGi 9606.ENSP00000417686.

PTM databases

PhosphoSitei Q14493.

Polymorphism databases

DMDMi 9789785.

Proteomic databases

MaxQBi Q14493.
PaxDbi Q14493.
PeptideAtlasi Q14493.
PRIDEi Q14493.

Protocols and materials databases

DNASUi 7884.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000429429 ; ENSP00000406322 ; ENSG00000163950 . [Q14493-2 ]
ENST00000489418 ; ENSP00000417686 ; ENSG00000163950 . [Q14493-1 ]
GeneIDi 7884.
KEGGi hsa:7884.
UCSCi uc003gdi.1. human. [Q14493-1 ]
uc003gdk.1. human. [Q14493-2 ]

Organism-specific databases

CTDi 7884.
GeneCardsi GC04M001694.
HGNCi HGNC:10904. SLBP.
HPAi HPA019254.
MIMi 602422. gene.
neXtProti NX_Q14493.
PharmGKBi PA35804.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG278381.
GeneTreei ENSGT00390000008738.
HOGENOMi HOG000065710.
HOVERGENi HBG017805.
InParanoidi Q14493.
OrthoDBi EOG789CF1.
PhylomeDBi Q14493.
TreeFami TF316521.

Enzyme and pathway databases

Reactomei REACT_1364. SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs.
REACT_405. Transport of the SLBP Dependant Mature mRNA.

Miscellaneous databases

EvolutionaryTracei Q14493.
GeneWikii SLBP.
GenomeRNAii 7884.
NextBioi 30350.
PROi Q14493.
SOURCEi Search...

Gene expression databases

Bgeei Q14493.
CleanExi HS_SLBP.
ExpressionAtlasi Q14493. baseline and differential.
Genevestigatori Q14493.

Family and domain databases

InterProi IPR026502. SLBP1/SLBP2.
IPR029344. SLBP_RNA_bind.
[Graphical view ]
PANTHERi PTHR17408. PTHR17408. 1 hit.
Pfami PF15247. SLBP_RNA_bind. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
  2. "The protein that binds the 3' end of histone mRNA: a novel RNA-binding protein required for histone pre-mRNA processing."
    Wang Z.-F., Whitfield M.L., Ingledue T.C. III, Dominski Z., Marzluff W.F.
    Genes Dev. 10:3028-3040(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Cervix adenocarcinoma.
  3. "The gene for histone RNA hairpin binding protein is located on human chromosome 4 and encodes a novel type of RNA binding protein."
    Martin F., Schaller A., Eglite S., Schuemperli D., Mueller B.
    EMBO J. 16:769-778(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Lymphocyte.
  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 2).
    Tissue: Heart.
  5. "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].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Uterus.
  8. "A novel zinc finger protein is associated with U7 snRNP and interacts with the stem-loop binding protein in the histone pre-mRNP to stimulate 3'-end processing."
    Dominski Z., Erkmann J.A., Yang X., Sanchez R., Marzluff W.F.
    Genes Dev. 16:58-71(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF 230-ASP--SER-270, INTERACTION WITH ZNF473.
  9. "Phosphorylation of stem-loop binding protein (SLBP) on two threonines triggers degradation of SLBP, the sole cell cycle-regulated factor required for regulation of histone mRNA processing, at the end of S phase."
    Zheng L., Dominski Z., Yang X.-C., Elms P., Raska C.S., Borchers C.H., Marzluff W.F.
    Mol. Cell. Biol. 23:1590-1601(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ASSOCIATION WITH POLYRIBOSOMES, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-61 AND THR-62, RNA-BINDING, MUTAGENESIS OF SER-59; THR-61; THR-62; PRO-63 AND 96-LYS--LEU-99, IDENTIFICATION BY MASS SPECTROMETRY.
  10. "Nuclear import of the stem-loop binding protein and localization during the cell cycle."
    Erkmann J.A., Wagner E.J., Dong J., Zhang Y., Kutay U., Marzluff W.F.
    Mol. Biol. Cell 16:2960-2971(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TNPO3 AND THE IMPORTIN ALPHA/IMPORTIN BETA RECEPTOR, SUBCELLULAR LOCATION, MUTAGENESIS OF 31-ARG--ARG-34; 96-LYS--LYS-99; ARG-137; ARG-138 AND 241-LYS--HIS-244.
  11. "Regulated degradation of replication-dependent histone mRNAs requires both ATR and Upf1."
    Kaygun H., Marzluff W.F.
    Nat. Struct. Mol. Biol. 12:794-800(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH UPF1.
  12. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20 AND SER-23, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "Characterization of 3'hExo, a 3' exonuclease specifically interacting with the 3' end of histone mRNA."
    Yang X.-C., Purdy M., Marzluff W.F., Dominski Z.
    J. Biol. Chem. 281:30447-30454(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A TERNARY COMPLEX, RNA-BINDING.
  14. "Degradation of histone mRNA requires oligouridylation followed by decapping and simultaneous degradation of the mRNA both 5' to 3' and 3' to 5'."
    Mullen T.E., Marzluff W.F.
    Genes Dev. 22:50-65(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LSM1.
  15. "SLIP1, a factor required for activation of histone mRNA translation by the stem-loop binding protein."
    Cakmakci N.G., Lerner R.S., Wagner E.J., Zheng L., Marzluff W.F.
    Mol. Cell. Biol. 28:1182-1194(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MIF4GD.
  16. "Phosphorylation of threonine 61 by cyclin a/Cdk1 triggers degradation of stem-loop binding protein at the end of S phase."
    Koseoglu M.M., Graves L.M., Marzluff W.F.
    Mol. Cell. Biol. 28:4469-4479(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-61 AND THR-62, MUTAGENESIS OF THR-61; THR-62; 59-SER--PRO-63 AND 96-LYS--LEU-99, IDENTIFICATION BY MASS SPECTROMETRY.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. "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].
  19. "Knockdown of SLBP results in nuclear retention of histone mRNA."
    Sullivan K.D., Mullen T.E., Marzluff W.F., Wagner E.J.
    RNA 15:459-472(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN HISTONE MRNA EXPORT.
  20. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "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-182, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "Interaction of the histone mRNA hairpin with stem-loop binding protein (SLBP) and regulation of the SLBP-RNA complex by phosphorylation and proline isomerization."
    Zhang M., Lam T.T., Tonelli M., Marzluff W.F., Thapar R.
    Biochemistry 51:3215-3231(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 129-158, PHOSPHORYLATION AT THR-171.

Entry informationi

Entry nameiSLBP_HUMAN
AccessioniPrimary (citable) accession number: Q14493
Secondary accession number(s): B3KRJ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1996
Last modified: October 29, 2014
This is version 133 of the entry and version 1 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 4
    Human chromosome 4: 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

External Data

Dasty 3