Q14493 (SLBP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone RNA hairpin-binding protein

Alternative name(s):
Histone stem-loop-binding protein

Gene names

Name:	SLBP
Synonyms:	HBP

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	270 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.9 Ref.18
Subunit structure	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. Ref.8 Ref.10 Ref.11 Ref.13 Ref.14 Ref.15
Subcellular location	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. Ref.9 Ref.10
Tissue specificity	Widely expressed.
Developmental stage	Regulated during the cell cycle: protein levels increase 10 to 20 fold in the late G1 and decrease at the S/G2 border.
Domain	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.
Post-translational modification	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. Ref.9 Ref.16
Sequence similarities	Belongs to the SLBP family.

Ontologies

Keywords
Biological process	mRNA processing
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Ligand	RNA-binding
Molecular function	Ribonucleoprotein
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA replication involved in S phase Inferred from mutant phenotype Ref.18. Source: UniProtKB histone mRNA 3'-end processing Inferred from sequence or structural similarity. Source: UniProtKB mRNA export from nucleus Traceable author statement. Source: Reactome regulation of S phase Inferred from mutant phenotype Ref.18. Source: UniProtKB termination of RNA polymerase II transcription Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome histone pre-mRNA 3'end processing complex Inferred from sequence or structural similarity. Source: UniProtKB nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	histone pre-mRNA DCP binding Inferred from sequence or structural similarity. Source: UniProtKB histone pre-mRNA stem-loop binding Inferred from sequence or structural similarity. Source: UniProtKB mRNA binding Inferred from direct assay Ref.13. Source: UniProtKB
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: Q14493-1)

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 2 (identifier: Q14493-2)

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 270

270

Histone RNA hairpin-binding protein

PRO_0000100356

Regions

Region

129 – 198

70

RNA-binding

Motif

31 – 34

4

Nuclear localization signal NLS1

Motif

96 – 99

4

Nuclear localization signal NLS2

Amino acid modifications

Modified residue

20

1

Phosphoserine Ref.12

Modified residue

23

1

Phosphoserine Ref.12

Modified residue

61

1

Phosphothreonine; by CK2 Ref.9 Ref.16

Modified residue

62

1

Phosphothreonine; by CDK1 Ref.9 Ref.16

Modified residue

182

1

Phosphoserine Ref.21

Natural variations

Alternative sequence

20 – 58

39

Missing in isoform 2.

VSP_042164

Experimental info

Mutagenesis

31 – 34

4

RKRR → 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. Ref.10

Mutagenesis

59 – 63

5

SFTTP → AAAA: Does not increase its stability at the end of the S phase and through G2 and mitosis. Ref.9 Ref.16

Mutagenesis

59

1

S → A: Does not increase its stability at the end of the S phase and through G2 and mitosis. Ref.9

Mutagenesis

61

1

T → 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. Ref.9 Ref.16

Mutagenesis

62

1

T → A: Increases its stability at the end of the S phase and through G2 and mitosis. Ref.9 Ref.16

Mutagenesis

63

1

P → A: Increases its stability at the end of the S phase and through G2 and mitosis. Ref.9

Mutagenesis

96 – 99

4

KRKL → 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. Ref.9 Ref.10 Ref.16

Mutagenesis

137

1

R → A: Inhibits histone RNA-binding and localization to the cytoplasm. Ref.10

Mutagenesis

138

1

R → A: Inhibits histone RNA-binding and localization to the cytoplasm. Ref.10

Mutagenesis

230 – 270

41

Missing: Decrease in 3'-end processing efficiency. Ref.8

Mutagenesis

241 – 244

4

KVRH → 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. Ref.10

Secondary structure

1

.

.

.

.

.

.

.

270

Helix Strand Turn

Details...

Helix

132 – 146

15

Helix

149 – 157

9

Helix

180 – 194

15

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 4E84E502393D1BF7	FASTA	270	31,286
	10 20 30 40 50 60 MACRPRSPPR HQSRCDGDAS PPSPARWSLG RKRRADGRRW RPEDAEEAEH RGAERRPESF 70 80 90 100 110 120 TTPEGPKPRS RCSDWASAVE EDEMRTRVNK EMARYKRKLL INDFGRERKS SSGSSDSKES 130 140 150 160 170 180 MSTVPADFET DESVLMRRQK QINYGKNTIA YDRYIKEVPR HLRQPGIHPK TPNKFKKYSR 190 200 210 220 230 240 RSWDQQIKLW KVALHFWDPP AEEGCDLQEI HPVDLESAES SSEPQTSSQD DFDVYSGTPT 250 260 270 KVRHMDSQVE DEFDLEACLT EPLRDFSAMS
	Isoform 2 [UniParc]. Checksum: 09C5137F52AC416D	FASTA	231	26,695
	10 20 30 40 50 60 MACRPRSPPR HQSRCDGDAS FTTPEGPKPR SRCSDWASAV EEDEMRTRVN KEMARYKRKL 70 80 90 100 110 120 LINDFGRERK SSSGSSDSKE SMSTVPADFE TDESVLMRRQ KQINYGKNTI AYDRYIKEVP 130 140 150 160 170 180 RHLRQPGIHP KTPNKFKKYS RRSWDQQIKL WKVALHFWDP PAEEGCDLQE IHPVDLESAE 190 200 210 220 230 SSSEPQTSSQ DDFDVYSGTP TKVRHMDSQV EDEFDLEACL TEPLRDFSAM S

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Expressed genes, Alu repeats and polymorphisms in cosmids sequenced from chromosome 4p16.3." McCombie W.R., Martin-Gallardo A., Gocayne J.D., FitzGerald M., Dubnick M., Kelley J.M., Castilla L., Liu L.I., Wallace S., Trapp S., Tagle D., Whaley W.L., Cheng S., Gusella J., Frischauf A.-M., Poustka A., Lehrach H., Collins F.S. , Kerlavage A.R., Fields C., Venter J.C. Nat. Genet. 1:348-353(1992) [PubMed] [Europe PMC] [Abstract] 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]	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 (SEP-2005) to the EMBL/GenBank/DDBJ databases 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, MASS SPECTROMETRY. 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]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[18]	"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.
[19]	"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.
[20]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] 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-182, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00031015.
IPI00947182.

RefSeq

NP_006518.1. NM_006527.2.

UniGene

Hs.298345.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2KJM	NMR	-	A	129-158	[»]
4HXH	X-ray	2.60	C	125-223	[»]

ProteinModelPortal

Q14493.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q14493. 3 interactions.

STRING

9606.ENSP00000417686.

PTM databases

PhosphoSite

Q14493.

Polymorphism databases

DMDM

9789785.

Proteomic databases

PaxDb

Q14493.

PeptideAtlas

Q14493.

PRIDE

Q14493.

Protocols and materials databases

DNASU

7884.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000429429; ENSP00000406322; ENSG00000163950.
ENST00000489418; ENSP00000417686; ENSG00000163950.

GeneID

7884.

KEGG

hsa:7884.

UCSC

uc003gdi.1. human.

Organism-specific databases

CTD

7884.

GeneCards

GC04M001694.

HGNC

HGNC:10904. SLBP.

HPA

HPA019254.

MIM

602422. gene.

neXtProt

NX_Q14493.

PharmGKB

PA35804.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG278381.

HOGENOM

HOG000065710.

HOVERGEN

HBG017805.

InParanoid

Q14493.

OrthoDB

EOG4J1196.

PhylomeDB

Q14493.

Enzyme and pathway databases

Reactome

REACT_1675. mRNA Processing.
REACT_1788. Transcription.
REACT_71. Gene Expression.
REACT_78. Post-Elongation Processing of the Transcript.

Gene expression databases

ArrayExpress

Q14493.

Bgee

Q14493.

CleanEx

HS_SLBP.

Genevestigator

Q14493.

GermOnline

ENSG00000163950. Homo sapiens.

Family and domain databases

InterPro

IPR026502. SLBP1/SLBP2.
[Graphical view]

PANTHER

PTHR17408. PTHR17408. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

Q14493.

GenomeRNAi

7884.

NextBio

30350.

SOURCE

Search...

Entry information

Entry name

SLBP_HUMAN

Accession

Primary (citable) accession number: Q14493
Secondary accession number(s): B3KRJ5

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 116 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.