Q9H0F6 (SHRPN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Sharpin

Alternative name(s):
Shank-associated RH domain-interacting protein
Shank-interacting protein-like 1
Short name=hSIPL1

Gene names

Name:	SHARPIN
Synonyms:	SIPL1
ORF Names:	PSEC0216

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	387 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of the LUBAC complex which conjugates linear polyubiquitin chains in a head-to-tail manner to substrates and plays a key role in NF-kappa-B activation and regulation of inflammation. LUBAC conjugates linear polyubiquitin to IKBKG and RIPK1 and is involved in activation of the canonical NF-kappa-B and the JNK signaling pathways. Linear ubiquitination mediated by the LUBAC complex interferes with TNF-induced cell death and thereby prevents inflammation. LUBAC is proposed to be recruited to the TNF-R1 signaling complex (TNF-RSC) following polyubiquitination of TNF-RSC components by BIRC2 and/or BIRC3 and to conjugate linear polyubiquitin to IKBKG and possibly other components contributing to the stability of the complex. Ref.10 Ref.11 Ref.12
Subunit structure	Monomer and homodimer. Interacts with SHANK1, EYA1 and EYA2 By similarity. Component of the LUBAC complex (linear ubiquitin chain assembly complex) which consists of SHARPIN, RBCK1 and RNF31. LUBAC has a MW of approximative 600 kDa suggesting a heteromultimeric assembly of its subunits. Associates with the TNF-R1 signaling complex (TNF-RSC) in a stimulation-dependent manner. Ref.10 Ref.11 Ref.12 Ref.13
Subcellular location	Cytoplasm › cytosol Ref.2.
Tissue specificity	Highly expressed in skeletal muscle and placenta and at lower levels in brain, heart, colon without mucosa, thymus, spleen, kidney, liver, small intestine, lung and peripheral blood leukocytes. Up-regulated in various tumor tissues such as kidney, liver, ovary and pancreas tumors. Ref.2
Domain	The Ubiquitin-like domain is required for the interaction with RNF31. Ref.10 Ref.11 Ref.12 The RanBP2-type zinc fingers mediate the specific interaction with ubiquitin. Binds preferentially linear polyubiquitin chains and 'Lys-63'-linked polyubiquitin chains over 'Lys-48'-linked polyubiquitin chains. Also binds monoubiquitin. Ref.10 Ref.11 Ref.12
Sequence similarities	Contains 1 RanBP2-type zinc finger. Contains 1 ubiquitin-like domain.
Sequence caution	The sequence BAC11666.1 differs from that shown. Reason: Frameshift at position 334. The sequence BAC53797.1 differs from that shown. Reason: Frameshift at position 218. The sequence BAC53798.1 differs from that shown. Reason: Aberrant splicing.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Zinc-finger
Ligand	Metal-binding Zinc
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic nuclear changes Inferred from electronic annotation. Source: Compara brain development Inferred from electronic annotation. Source: Compara keratinization Inferred from electronic annotation. Source: Compara mitochondrion organization Inferred from electronic annotation. Source: Compara negative regulation of inflammatory response Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of I-kappaB kinase/NF-kappaB cascade Inferred from direct assay Ref.10. Source: UniProtKB protein homooligomerization Inferred from electronic annotation. Source: Compara protein linear polyubiquitination Inferred from direct assay Ref.10Ref.11Ref.12. Source: UniProtKB regulation of CD40 signaling pathway Inferred from direct assay Ref.10. Source: UniProtKB regulation of tumor necrosis factor-mediated signaling pathway Inferred from direct assay Ref.10. Source: UniProtKB
Cellular_component	LUBAC complex Inferred from direct assay Ref.10Ref.11Ref.12. Source: UniProtKB cytosol Inferred from direct assay Ref.2. Source: UniProtKB postsynaptic density Inferred from electronic annotation. Source: Compara
Molecular_function	polyubiquitin binding Inferred from direct assay Ref.10Ref.12. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ITGA2	P17301	5	EBI-3942966,EBI-702960
ITGA5	P08648	4	EBI-3942966,EBI-1382311

Alternative products

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

Isoform 1 (identifier: Q9H0F6-1)

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: Q9H0F6-2)

Also known as: hSIPL1A;

The sequence of this isoform differs from the canonical sequence as follows:
     309-326: TGPSPQHPQKMDGELGRL → QLVLSFLHLHQCPRPPWL
     327-387: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 387

387

Sharpin

PRO_0000280634

Regions

Domain

219 – 288

70

Ubiquitin-like

Zinc finger

348 – 377

30

RanBP2-type

Region

1 – 180

180

Self-association By similarity

Region

175 – 310

136

Interaction with SHANK1 By similarity

Amino acid modifications

Modified residue

165

1

Phosphoserine Ref.8

Modified residue

312

1

Phosphoserine Ref.9

Natural variations

Alternative sequence

309 – 326

18

TGPSP…ELGRL → QLVLSFLHLHQCPRPPWL in isoform 2.

VSP_023837

Alternative sequence

327 – 387

61

Missing in isoform 2.

VSP_023838

Natural variant

282

1

S → T.
Corresponds to variant rs11541804 [ dbSNP | Ensembl ].

VAR_047799

Natural variant

294

1

P → S.
Corresponds to variant rs34674752 [ dbSNP | Ensembl ].

VAR_047800

Natural variant

311

1

P → R.
Corresponds to variant rs35844464 [ dbSNP | Ensembl ].

VAR_047801

Experimental info

Mutagenesis

114

1

V → D: Abolishes homodimerization. Ref.13

Mutagenesis

272

1

I → A: Abolishes interaction with RNF31 and ability to mediate linear polyubiquitination. Ref.12

Mutagenesis

354

1

C → S: Abolishes binding to ubiquitin without affecting interaction with RNF31; when associated with S-357. Ref.10

Mutagenesis

357

1

C → S: Abolishes binding to ubiquitin without affecting interaction with RNF31; when associated with S-354. Ref.10

Mutagenesis

358 – 359

2

TF → LV: Abolishes binding to ubiquitin and ability to mediate linear polyubiquitination.

Mutagenesis

368

1

C → S: Abolishes binding to ubiquitin without affecting interaction with RNF31; when associated with S-371. Ref.10

Mutagenesis

371

1

C → S: Abolishes binding to ubiquitin without affecting interaction with RNF31; when associated with S-368. Ref.10

Sequence conflict

238

1

A → P in AAH02688. Ref.6

Sequence conflict

243

1

Q → R in BAC11666. Ref.3

Sequence conflict

257

1

V → A in AAH02688. Ref.6

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

387

Helix Strand Turn

Details...

Beta strand

20 – 30

11

Helix

31 – 33

3

Beta strand

40 – 48

9

Beta strand

56 – 60

5

Beta strand

70 – 73

4

Helix

74 – 76

3

Beta strand

77 – 83

7

Beta strand

86 – 90

5

Beta strand

99 – 105

7

Helix

106 – 119

14

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 33EE4BF66936AB60	FASTA	387	39,949
	10 20 30 40 50 60 MAPPAGGAAA AASDLGSAAV LLAVHAAVRP LGAGPDAEAQ LRRLQLSADP ERPGRFRLEL 70 80 90 100 110 120 LGAGPGAVNL EWPLESVSYT IRGPTQHELQ PPPGGPGTLS LHFLNPQEAQ RWAVLVRGAT 130 140 150 160 170 180 VEGQNGSKSN SPPALGPEAC PVSLPSPPEA STLKGPPPEA DLPRSPGNLT EREELAGSLA 190 200 210 220 230 240 RAIAGGDEKG AAQVAAVLAQ HRVALSVQLQ EACFPPGPIR LQVTLEDAAS AASAASSAHV 250 260 270 280 290 300 ALQVHPHCTV AALQEQVFSE LGFPPAVQRW VIGRCLCVPE RSLASYGVRQ DGDPAFLYLL 310 320 330 340 350 360 SAPREAPATG PSPQHPQKMD GELGRLFPPS LGLPPGPQPA ASSLPSPLQP SWSCPSCTFI 370 380 NAPDRPGCEM CSTQRPCTWD PLAAAST
	Isoform 2 (hSIPL1A) [UniParc]. Checksum: C92FE8845FD1EC3E	FASTA	326	33,878
	10 20 30 40 50 60 MAPPAGGAAA AASDLGSAAV LLAVHAAVRP LGAGPDAEAQ LRRLQLSADP ERPGRFRLEL 70 80 90 100 110 120 LGAGPGAVNL EWPLESVSYT IRGPTQHELQ PPPGGPGTLS LHFLNPQEAQ RWAVLVRGAT 130 140 150 160 170 180 VEGQNGSKSN SPPALGPEAC PVSLPSPPEA STLKGPPPEA DLPRSPGNLT EREELAGSLA 190 200 210 220 230 240 RAIAGGDEKG AAQVAAVLAQ HRVALSVQLQ EACFPPGPIR LQVTLEDAAS AASAASSAHV 250 260 270 280 290 300 ALQVHPHCTV AALQEQVFSE LGFPPAVQRW VIGRCLCVPE RSLASYGVRQ DGDPAFLYLL 310 320 SAPREAPAQL VLSFLHLHQC PRPPWL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Novel human and mouse genes encoding a shank-interacting protein and its upregulation in gastric fundus of W/WV mouse." Daigo Y., Takayama I., Ward S.M., Sanders K.M., Fujino M.A. J. Gastroenterol. Hepatol. 18:712-718(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[2]	"Newly identified tumor-associated role of human Sharpin." Jung J., Kim J.M., Park B., Cheon Y., Lee B., Choo S.H., Koh S.S., Lee S.J. Mol. Cell. Biochem. 340:161-167(2010) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[3]	"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs." Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A. Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Testis.
[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: Embryo.
[5]	"DNA sequence and analysis of human chromosome 8." Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T. , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S. Nature 439:331-335(2006) [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] (ISOFORMS 1 AND 2). Tissue: Pancreas, Prostate and Uterus.
[8]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"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-312, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Linear ubiquitination prevents inflammation and regulates immune signalling." Gerlach B., Cordier S.M., Schmukle A.C., Emmerich C.H., Rieser E., Haas T.L., Webb A.I., Rickard J.A., Anderton H., Wong W.W., Nachbur U., Gangoda L., Warnken U., Purcell A.W., Silke J., Walczak H. Nature 471:591-596(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE LUBAC COMPLEX, FUNCTION, DOMAIN RANBP2-TYPE, DOMAIN UBIQUITIN-LIKE, UBIQUITIN-BINDING, MUTAGENESIS OF CYS-354; CYS-357; CYS-368 AND CYS-371.
[11]	"SHARPIN is a component of the NF-kappaB-activating linear ubiquitin chain assembly complex." Tokunaga F., Nakagawa T., Nakahara M., Saeki Y., Taniguchi M., Sakata S., Tanaka K., Nakano H., Iwai K. Nature 471:633-636(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE LUBAC COMPLEX, FUNCTION, DOMAIN UBIQUITIN-LIKE.
[12]	"SHARPIN forms a linear ubiquitin ligase complex regulating NF-kappaB activity and apoptosis." Ikeda F., Deribe Y.L., Skanland S.S., Stieglitz B., Grabbe C., Franz-Wachtel M., van Wijk S.J., Goswami P., Nagy V., Terzic J., Tokunaga F., Androulidaki A., Nakagawa T., Pasparakis M., Iwai K., Sundberg J.P., Schaefer L., Rittinger K., Macek B., Dikic I. Nature 471:637-641(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE LUBAC COMPLEX, FUNCTION, DOMAIN RANBP2-TYPE, DOMAIN UBIQUITIN-LIKE, UBIQUITIN-BINDING, MUTAGENESIS OF ILE-272 AND 358-THR-PHE-359.
[13]	"Structural analysis of SHARPIN, a subunit of a large multi-protein E3 ubiquitin ligase, reveals a novel dimerization function for the pleckstrin homology superfold." Stieglitz B., Haire L.F., Dikic I., Rittinger K. J. Biol. Chem. 287:20823-20829(2012) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-127, MUTAGENESIS OF VAL-114, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB052764 mRNA. Translation: BAC53797.1. Frameshift.
AB052765 mRNA. Translation: BAC53798.1. Sequence problems.
FJ655995 mRNA. Translation: ACN38058.1.
AL136816 mRNA. Translation: CAB66750.1.
AK075518 mRNA. Translation: BAC11666.1. Frameshift.
AC104592 Genomic DNA. No translation available.
CH471162 Genomic DNA. Translation: EAW82152.1.
CH471162 Genomic DNA. Translation: EAW82153.1.
CH471162 Genomic DNA. Translation: EAW82150.1.
CH471162 Genomic DNA. Translation: EAW82151.1.
BC002688 mRNA. Translation: AAH02688.2.
BC025244 mRNA. Translation: AAH25244.1.
BC034028 mRNA. Translation: AAH34028.1.

IPI

IPI00382790.
IPI00873534.

RefSeq

NP_112236.3. NM_030974.3.

UniGene

Hs.529755.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4EMO	X-ray	2.00	A/B/C/D	1-127	[»]

ProteinModelPortal

Q9H0F6.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-57842N.

IntAct

Q9H0F6. 5 interactions.

MINT

MINT-7034570.

STRING

9606.ENSP00000381698.

PTM databases

PhosphoSite

Q9H0F6.

Polymorphism databases

DMDM

74733523.

Proteomic databases

PaxDb

Q9H0F6.

PRIDE

Q9H0F6.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000359551; ENSP00000352551; ENSG00000179526.
ENST00000398712; ENSP00000381698; ENSG00000179526.

GeneID

81858.

KEGG

hsa:81858.

UCSC

uc003zba.3. human.

Organism-specific databases

CTD

81858.

GeneCards

GC08M145153.

H-InvDB

HIX0017281.
HIX0124604.

HGNC

HGNC:25321. SHARPIN.

HPA

HPA044453.

MIM

611885. gene.

neXtProt

NX_Q9H0F6.

PharmGKB

PA142670925.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG278522.

HOVERGEN

HBG093954.

OMA

HELQPPP.

OrthoDB

EOG48SGTH.

Gene expression databases

ArrayExpress

Q9H0F6.

Bgee

Q9H0F6.

CleanEx

HS_SHARPIN.

Genevestigator

Q9H0F6.

Family and domain databases

InterPro

IPR026168. SHARPIN.
IPR001876. Znf_RanBP2.
[Graphical view]

PANTHER

PTHR22770:SF11. PTHR22770:SF11. 1 hit.

Pfam

PF00641. zf-RanBP. 1 hit.
[Graphical view]

SMART

SM00547. ZnF_RBZ. 1 hit.
[Graphical view]

PROSITE

PS50053. UBIQUITIN_2. False negative.
PS01358. ZF_RANBP2_1. 1 hit.
PS50199. ZF_RANBP2_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

GenomeRNAi

81858.

NextBio

72187.

SOURCE

Search...

Entry information

Entry name

SHRPN_HUMAN

Accession

Primary (citable) accession number: Q9H0F6
Secondary accession number(s): A6NEG3 , C0L3L2, D3DWL3, Q8IXF5, Q8IXF6, Q8N2E7, Q8TB25, Q9BUE4

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 20, 2007
Last sequence update:	March 1, 2001
Last modified:	May 1, 2013
This is version 88 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.