Q9P0U3 (SENP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Sentrin-specific protease 1
EC=3.4.22.68

Alternative name(s):
Sentrin/SUMO-specific protease SENP1

Gene names

Name:

SENP1

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

General annotation (Comments)

Function	Protease that catalyzes two essential functions in the SUMO pathway: processing of full-length SUMO1, SUMO2 and SUMO3 to their mature forms and deconjugation of SUMO1, SUMO2 and SUMO3 from targeted proteins. Deconjugates SUMO1 from HIPK2. Deconjugates SUMO1 from HDAC1, which decreases its transcriptional repression activity. Ref.1 Ref.6 Ref.8 Ref.10
Catalytic activity	Hydrolysis of the alpha-linked peptide bond in the sequence Gly-Gly-|-Ala-Thr-Tyr at the C-terminal end of the small ubiquitin-like modifier (SUMO) propeptide, Smt3, leading to the mature form of the protein. A second reaction involves the cleavage of an epsilon-linked peptide bond between the C-terminal glycine of the mature SUMO and the lysine epsilon-amino group of the target protein.
Subcellular location	Nucleus. Cytoplasm. Note: Shuttles between cytoplasm and nucleus. Ref.1 Ref.5 Ref.8
Tissue specificity	Highly expressed in testis. Expressed at lower levels in thymus, pancreas, spleen, liver, ovary and small intestine. Ref.7
Sequence similarities	Belongs to the peptidase C48 family.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Molecular function	Hydrolase Protease Thiol protease
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	activation of cysteine-type endopeptidase activity involved in apoptotic process Inferred from mutant phenotype PubMed 1087798. Source: UniProtKB apoptotic signaling pathway Inferred from mutant phenotype PubMed 1087798. Source: UniProtKB negative regulation of proteasomal ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: Compara positive regulation of transcription from RNA polymerase II promoter Inferred from genetic interaction PubMed 17981124. Source: MGI protein desumoylation Inferred from sequence or structural similarity. Source: UniProtKB proteolysis Traceable author statement Ref.1. Source: ProtInc regulation of definitive erythrocyte differentiation Inferred from electronic annotation. Source: Compara
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay. Source: HPA
Molecular_function	SUMO-specific protease activity Inferred from sequence or structural similarity. Source: UniProtKB endopeptidase activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: Q9P0U3-1)

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: Q9P0U3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     593-593: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 644

644

Sentrin-specific protease 1

PRO_0000101716

Regions

Region

450 – 613

164

Protease

Motif

171 – 177

7

Nuclear localization signal Probable

Motif

574 – 577

4

Nuclear localization signal Potential

Motif

628 – 634

7

Nuclear localization signal Potential

Motif

635 – 644

10

Nuclear export signal Probable

Compositional bias

45 – 170

126

Ser-rich

Compositional bias

290 – 300

11

His-rich

Sites

Active site

533

1

Active site

550

1

Active site

603

1

Nucleophile

Amino acid modifications

Modified residue

157

1

Phosphoserine Ref.9

Natural variations

Alternative sequence

593

1

Missing in isoform 2.

VSP_035777

Natural variant

193

1

I → V. Ref.4
Corresponds to variant rs17854369 [ dbSNP | Ensembl ].

VAR_029648

Natural variant

280

1

A → T.
Corresponds to variant rs35130318 [ dbSNP | Ensembl ].

VAR_047547

Natural variant

350

1

D → G. Ref.4
Corresponds to variant rs17854368 [ dbSNP | Ensembl ].

VAR_029649

Experimental info

Mutagenesis

441

1

D → A: No effect on SUMO2 processing and SUMO2 deconjugating activities. Ref.10

Mutagenesis

465

1

W → A: Impairs SUMO2 processing and SUMO2 deconjugating activities. Ref.10

Mutagenesis

468

1

D → A: Slightly impairs SUMO2 processing activity. No effect on SUMO2 deconjugating activity. Ref.10

Mutagenesis

496

1

F → A: Impairs SUMO2 processing activity. No effect on SUMO2 deconjugating activity. Ref.10

Mutagenesis

511

1

R → A: Impairs SUMO2 processing activity. No effect on SUMO2 deconjugating activity. Ref.10

Mutagenesis

512

1

W → A: Impairs SUMO2 processing and SUMO2 deconjugating activities. Ref.10

Mutagenesis

529

1

H → A: Impairs SUMO2 processing activity. No effect on SUMO2 deconjugating activity. Ref.10

Mutagenesis

532

1

V → A: No effect on SUMO2 processing and SUMO2 deconjugating activities. Ref.10

Mutagenesis

533

1

H → A: Abolishes SUMO2 processing and SUMO2 deconjugating activities. Ref.10

Mutagenesis

534

1

W → A: Abolishes SUMO2 processing and SUMO2 deconjugating activities. Ref.10

Mutagenesis

550

1

D → A: Abolishes SUMO2 processing and SUMO2 deconjugating activities. Ref.10

Mutagenesis

597

1

Q → A: Abolishes SUMO2 processing and SUMO2 deconjugating activities. Ref.10

Mutagenesis

603

1

C → A or S: Abolishes SUMO2 processing and SUMO2 deconjugating activities. Ref.5 Ref.10 Ref.11

Mutagenesis

603

1

C → S: Exclusively nuclear. Ref.5 Ref.10 Ref.11

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

644

Helix Strand Turn

Details...

Helix

425 – 434

10

Beta strand

435 – 438

4

Beta strand

445 – 447

3

Beta strand

450 – 452

3

Helix

454 – 458

5

Helix

468 – 481

14

Beta strand

482 – 484

3

Beta strand

490 – 492

3

Turn

495 – 498

4

Helix

499 – 502

4

Helix

506 – 509

4

Turn

510 – 515

6

Helix

518 – 520

3

Beta strand

521 – 530

10

Beta strand

533 – 540

8

Turn

541 – 544

4

Beta strand

545 – 549

5

Helix

557 – 575

19

Beta strand

585 – 588

4

Beta strand

591 – 594

4

Helix

600 – 602

3

Helix

603 – 615

13

Helix

624 – 626

3

Helix

627 – 640

14

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 25, 2008. Version 2. Checksum: 941951A8B341EC64	FASTA	644	73,481
	10 20 30 40 50 60 MDDIADRMRM DAGEVTLVNH NSVFKTHLLP QTGFPEDQLS LSDQQILSSR QGHLDRSFTC 70 80 90 100 110 120 STRSAAYNPS YYSDNPSSDS FLGSGDLRTF GQSANGQWRN STPSSSSSLQ KSRNSRSLYL 130 140 150 160 170 180 ETRKTSSGLS NSFAGKSNHH CHVSAYEKSF PIKPVPSPSW SGSCRRSLLS PKKTQRRHVS 190 200 210 220 230 240 TAEETVQEEE REIYRQLLQM VTGKQFTIAK PTTHFPLHLS RCLSSSKNTL KDSLFKNGNS 250 260 270 280 290 300 CASQIIGSDT SSSGSASILT NQEQLSHSVY SLSSYTPDVA FGSKDSGTLH HPHHHHSVPH 310 320 330 340 350 360 QPDNLAASNT QSEGSDSVIL LKVKDSQTPT PSSTFFQAEL WIKELTSVYD SRARERLRQI 370 380 390 400 410 420 EEQKALALQL QNQRLQEREH SVHDSVELHL RVPLEKEIPV TVVQETQKKG HKLTDSEDEF 430 440 450 460 470 480 PEITEEMEKE IKNVFRNGNQ DEVLSEAFRL TITRKDIQTL NHLNWLNDEI INFYMNMLME 490 500 510 520 530 540 RSKEKGLPSV HAFNTFFFTK LKTAGYQAVK RWTKKVDVFS VDILLVPIHL GVHWCLAVVD 550 560 570 580 590 600 FRKKNITYYD SMGGINNEAC RILLQYLKQE SIDKKRKEFD TNGWQLFSKK SQEIPQQMNG 610 620 630 640 SDCGMFACKY ADCITKDRPI NFTQQHMPYF RKRMVWEILH RKLL
	Isoform 2 [UniParc]. Checksum: 1556864F1BDEE337	FASTA	643	73,351
	10 20 30 40 50 60 MDDIADRMRM DAGEVTLVNH NSVFKTHLLP QTGFPEDQLS LSDQQILSSR QGHLDRSFTC 70 80 90 100 110 120 STRSAAYNPS YYSDNPSSDS FLGSGDLRTF GQSANGQWRN STPSSSSSLQ KSRNSRSLYL 130 140 150 160 170 180 ETRKTSSGLS NSFAGKSNHH CHVSAYEKSF PIKPVPSPSW SGSCRRSLLS PKKTQRRHVS 190 200 210 220 230 240 TAEETVQEEE REIYRQLLQM VTGKQFTIAK PTTHFPLHLS RCLSSSKNTL KDSLFKNGNS 250 260 270 280 290 300 CASQIIGSDT SSSGSASILT NQEQLSHSVY SLSSYTPDVA FGSKDSGTLH HPHHHHSVPH 310 320 330 340 350 360 QPDNLAASNT QSEGSDSVIL LKVKDSQTPT PSSTFFQAEL WIKELTSVYD SRARERLRQI 370 380 390 400 410 420 EEQKALALQL QNQRLQEREH SVHDSVELHL RVPLEKEIPV TVVQETQKKG HKLTDSEDEF 430 440 450 460 470 480 PEITEEMEKE IKNVFRNGNQ DEVLSEAFRL TITRKDIQTL NHLNWLNDEI INFYMNMLME 490 500 510 520 530 540 RSKEKGLPSV HAFNTFFFTK LKTAGYQAVK RWTKKVDVFS VDILLVPIHL GVHWCLAVVD 550 560 570 580 590 600 FRKKNITYYD SMGGINNEAC RILLQYLKQE SIDKKRKEFD TNGWQLFSKK SQIPQQMNGS 610 620 630 640 DCGMFACKYA DCITKDRPIN FTQQHMPYFR KRMVWEILHR KLL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Differential regulation of sentrinized proteins by a novel sentrin-specific protease." Gong L., Millas S., Maul G.G., Yeh E.T.H. J. Biol. Chem. 275:3355-3359(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION. Tissue: Placenta.
[2]	"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: Stomach.
[3]	"The finished DNA sequence of human chromosome 12." Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A. Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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), VARIANTS VAL-193 AND GLY-350. Tissue: Testis.
[5]	"Characterization of the localization and proteolytic activity of the SUMO-specific protease, SENP1." Bailey D., O'Hare P. J. Biol. Chem. 279:692-703(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEAR LOCALIZATION SIGNAL, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-603.
[6]	"SENP1 enhances androgen receptor-dependent transcription through desumoylation of histone deacetylase 1." Cheng J., Wang D., Wang Z., Yeh E.T.H. Mol. Cell. Biol. 24:6021-6028(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[7]	"Mapping residues of SUMO precursors essential in differential maturation by SUMO-specific protease, SENP1." Xu Z., Au S.W.N. Biochem. J. 386:325-330(2005) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[8]	"Desumoylation of homeodomain-interacting protein kinase 2 (HIPK2) through the cytoplasmic-nuclear shuttling of the SUMO-specific protease SENP1." Kim Y.H., Sung K.S., Lee S.-J., Kim Y.-O., Choi C.Y., Kim Y. FEBS Lett. 579:6272-6278(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEAR EXPORT SIGNAL, SUBCELLULAR LOCATION, FUNCTION.
[9]	"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-157, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"The structure of SENP1-SUMO-2 complex suggests a structural basis for discrimination between SUMO paralogues during processing." Shen L.N., Dong C., Liu H., Naismith J.H., Hay R.T. Biochem. J. 397:279-288(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 419-644, X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 419-644 IN COMPLEX WITH SUMO3, MUTAGENESIS OF ASP-441; TRP-465; ASP-468; PHE-496; ARG-511; TRP-512; HIS-529; VAL-532; HIS-533; TRP-534; ASP-550; GLN-597 AND CYS-603, FUNCTION.
[11]	"Crystal structure of the SENP1 mutant C603S-SUMO complex reveals the hydrolytic mechanism of SUMO-specific protease." Xu Z., Chau S.F., Lam K.H., Chan H.Y., Ng T.B., Au S.W.N. Biochem. J. 398:345-352(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 439-644 IN COMPLEX WITH SUMO1, MUTAGENESIS OF CYS-603.
[12]	"SUMO protease SENP1 induces isomerization of the scissile peptide bond." Shen L., Tatham M.H., Dong C., Zagorska A., Naismith J.H., Hay R.T. Nat. Struct. Mol. Biol. 13:1069-1077(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.77 ANGSTROMS) OF 439-644 IN COMPLEX WITH RANGAP1 AND SUMO1.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF149770 mRNA. Translation: AAF31171.1.
AK292060 mRNA. Translation: BAF84749.1.
AC074029 Genomic DNA. No translation available.
BC045639 mRNA. Translation: AAH45639.2.

IPI

IPI00005101.
IPI00914975.

RefSeq

NP_001254523.1. NM_001267594.1.
NP_001254524.1. NM_001267595.1.

UniGene

Hs.371957.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2CKG	X-ray	2.45	A/B	419-644	[»]
2CKH	X-ray	3.20	A	419-644	[»]
2G4D	X-ray	2.80	A/C	440-644	[»]
2IY0	X-ray	2.77	A	419-643	[»]
2IY1	X-ray	2.46	A/C	419-643	[»]
2IYC	X-ray	2.45	A/B	419-643	[»]
2IYD	X-ray	3.20	A	419-643	[»]
2XPH	X-ray	2.40	A/B	415-644	[»]
2XRE	X-ray	2.45	A/B	415-644	[»]

ProteinModelPortal

Q9P0U3.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29252N.

IntAct

Q9P0U3. 2 interactions.

MINT

MINT-1714015.

STRING

9606.ENSP00000394791.

Protein family/group databases

MEROPS

C48.002.

PTM databases

PhosphoSite

Q9P0U3.

Polymorphism databases

DMDM

215273882.

Proteomic databases

PaxDb

Q9P0U3.

PRIDE

Q9P0U3.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000004980; ENSP00000004980; ENSG00000079387.
ENST00000448372; ENSP00000394791; ENSG00000079387.
ENST00000549518; ENSP00000447328; ENSG00000079387.
ENST00000549595; ENSP00000450076; ENSG00000079387.
ENST00000551330; ENSP00000446681; ENSG00000079387.

GeneID

29843.

KEGG

hsa:29843.

UCSC

uc001rqw.3. human.
uc001rqx.3. human.

Organism-specific databases

CTD

29843.

GeneCards

GC12M048436.

HGNC

HGNC:17927. SENP1.

HPA

HPA011765.

MIM

612157. gene.

neXtProt

NX_Q9P0U3.

PharmGKB

PA134947038.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5160.

HOGENOM

HOG000154286.

HOVERGEN

HBG057384.

InParanoid

Q9P0U3.

KO

K08592.

OMA

CHMSAYE.

OrthoDB

EOG4JWVD6.

Enzyme and pathway databases

BRENDA

3.4.22.68. 2681.

Pathway_Interaction_DB

ar_tf_pathway. Regulation of Androgen receptor activity.

Gene expression databases

ArrayExpress

Q9P0U3.

Bgee

Q9P0U3.

CleanEx

HS_SENP1.

Genevestigator

Q9P0U3.

GermOnline

ENSG00000079387. Homo sapiens.

Family and domain databases

InterPro

IPR003653. Peptidase_C48.
[Graphical view]

Pfam

PF02902. Peptidase_C48. 1 hit.
[Graphical view]

PROSITE

PS50600. ULP_PROTEASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q9P0U3.

ChEMBL

CHEMBL1909484.

ChiTaRS

SENP1. human.

EvolutionaryTrace

Q9P0U3.

GenomeRNAi

29843.

NextBio

52379.

SOURCE

Search...

Entry information

Entry name

SENP1_HUMAN

Accession

Primary (citable) accession number: Q9P0U3
Secondary accession number(s): A8K7P5, Q86XC8

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2002
Last sequence update:	November 25, 2008
Last modified:	May 1, 2013
This is version 103 of the entry and version 2 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.