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Q9ULT8

- HECD1_HUMAN

UniProt

Q9ULT8 - HECD1_HUMAN

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Protein
E3 ubiquitin-protein ligase HECTD1
Gene
HECTD1, KIAA1131
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Probable E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. May be required for development of the head mesenchyme and neural tube closure By similarity.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei2579 – 25791Glycyl thioester intermediate By similarity

GO - Molecular functioni

  1. ligase activity Source: UniProtKB-KW
  2. metal ion binding Source: InterPro
  3. protein binding Source: UniProtKB
  4. ubiquitin-protein transferase activity Source: RefGenome
Complete GO annotation...

GO - Biological processi

  1. neural tube closure Source: Ensembl
  2. protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: RefGenome
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase HECTD1 (EC:6.3.2.-)
Alternative name(s):
E3 ligase for inhibin receptor
EULIR
HECT domain-containing protein 1
Gene namesi
Name:HECTD1
Synonyms:KIAA1131
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:20157. HECTD1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: RefGenome
  2. nucleus Source: RefGenome
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134989284.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 26102610E3 ubiquitin-protein ligase HECTD1
PRO_0000083945Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei631 – 6311Phosphoserine1 Publication
Modified residuei1488 – 14881Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9ULT8.
PaxDbiQ9ULT8.
PeptideAtlasiQ9ULT8.
PRIDEiQ9ULT8.

PTM databases

PhosphoSiteiQ9ULT8.

Expressioni

Gene expression databases

ArrayExpressiQ9ULT8.
BgeeiQ9ULT8.
CleanExiHS_HECTD1.
GenevestigatoriQ9ULT8.

Organism-specific databases

HPAiHPA002929.

Interactioni

Subunit structurei

Interacts with IGSF1.1 Publication

Protein-protein interaction databases

BioGridi117359. 15 interactions.
DIPiDIP-31669N.
IntActiQ9ULT8. 8 interactions.
MINTiMINT-6783566.
STRINGi9606.ENSP00000382269.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi1270 – 12723
Beta strandi1279 – 12824
Turni1289 – 12924
Beta strandi1299 – 13013
Beta strandi1309 – 13146
Turni1315 – 13173
Beta strandi1319 – 13257
Helixi1326 – 13283
Beta strandi1332 – 13343
Helixi1883 – 18864
Helixi1896 – 19027
Beta strandi1905 – 19084
Helixi1910 – 192011
Helixi1923 – 19286
Helixi1935 – 19417
Helixi1944 – 195714
Turni1960 – 19623

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DK3NMR-A1266-1338[»]
2LC3NMR-A1879-1966[»]
3DKMX-ray1.60A1271-1341[»]
ProteinModelPortaliQ9ULT8.
SMRiQ9ULT8. Positions 1266-1338, 1879-1966.

Miscellaneous databases

EvolutionaryTraceiQ9ULT8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati395 – 42430ANK 1
Add
BLAST
Repeati426 – 45530ANK 2
Add
BLAST
Repeati459 – 49133ANK 3
Add
BLAST
Repeati579 – 61234ANK 4
Add
BLAST
Domaini1266 – 133873MIB/HERC2
Add
BLAST
Domaini2151 – 2610460HECT
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2029 – 210375K-box
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1350 – 1649300Ser-rich
Add
BLAST

Sequence similaritiesi

Belongs to the UPL family. K-HECT subfamily.
Contains 4 ANK repeats.
Contains 1 MIB/HERC2 domain.

Keywords - Domaini

ANK repeat, Repeat

Phylogenomic databases

eggNOGiCOG5021.
HOGENOMiHOG000018061.
HOVERGENiHBG067533.
InParanoidiQ9ULT8.
KOiK12231.
OMAiTKHSFTA.
PhylomeDBiQ9ULT8.
TreeFamiTF323674.

Family and domain databases

Gene3Di1.25.10.10. 2 hits.
1.25.40.20. 1 hit.
2.60.120.260. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR008979. Galactose-bd-like.
IPR000569. HECT.
IPR010606. Mib_Herc2.
IPR012919. Sad1_UNC_C.
[Graphical view]
PfamiPF12796. Ank_2. 1 hit.
PF00632. HECT. 1 hit.
PF06701. MIB_HERC2. 1 hit.
PF07738. Sad1_UNC. 1 hit.
[Graphical view]
SMARTiSM00248. ANK. 3 hits.
SM00119. HECTc. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 3 hits.
SSF48403. SSF48403. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF56204. SSF56204. 4 hits.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 2 hits.
PS50237. HECT. 1 hit.
PS51416. MIB_HERC2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9ULT8-1 [UniParc]FASTAAdd to Basket

« Hide

MADVDPDTLL EWLQMGQGDE RDMQLIALEQ LCMLLLMSDN VDRCFETCPP     50
RTFLPALCKI FLDESAPDNV LEVTARAITY YLDVSAECTR RIVGVDGAIK 100
ALCNRLVVVE LNNRTSRDLA EQCVKVLELI CTRESGAVFE AGGLNCVLTF 150
IRDSGHLVHK DTLHSAMAVV SRLCGKMEPQ DSSLEICVES LSSLLKHEDH 200
QVSDGALRCF ASLADRFTRR GVDPAPLAKH GLTEELLSRM AAAGGTVSGP 250
SSACKPGRST TGAPSTTADS KLSNQVSTIV SLLSTLCRGS PVVTHDLLRS 300
ELPDSIESAL QGDERCVLDT MRLVDLLLVL LFEGRKALPK SSAGSTGRIP 350
GLRRLDSSGE RSHRQLIDCI RSKDTDALID AIDTGAFEVN FMDDVGQTLL 400
NWASAFGTQE MVEFLCERGA DVNRGQRSSS LHYAACFGRP QVAKTLLRHG 450
ANPDLRDEDG KTPLDKARER GHSEVVAILQ SPGDWMCPVN KGDDKKKKDT 500
NKDEEECNEP KGDPEMAPIY LKRLLPVFAQ TFQQTMLPSI RKASLALIRK 550
MIHFCSEALL KEVCDSDVGH NLPTILVEIT ATVLDQEDDD DGHLLALQII 600
RDLVDKGGDI FLDQLARLGV ISKVSTLAGP SSDDENEEES KPEKEDEPQE 650
DAKELQQGKP YHWRDWSIIR GRDCLYIWSD AAALELSNGS NGWFRFILDG 700
KLATMYSSGS PEGGSDSSES RSEFLEKLQR ARGQVKPSTS SQPILSAPGP 750
TKLTVGNWSL TCLKEGEIAI HNSDGQQATI LKEDLPGFVF ESNRGTKHSF 800
TAETSLGSEF VTGWTGKRGR KLKSKLEKTK QKVRTMARDL YDDHFKAVES 850
MPRGVVVTLR NIATQLESSW ELHTNRQCIE SENTWRDLMK TALENLIVLL 900
KDENTISPYE MCSSGLVQAL LTVLNNSMDL DMKQDCSQLV ERINVFKTAF 950
SENEDDESRP AVALIRKLIA VLESIERLPL HLYDTPGSTY NLQILTRRLR 1000
FRLERAPGET ALIDRTGRML KMEPLATVES LEQYLLKMVA KQWYDFDRSS 1050
FVFVRKLREG QNFIFRHQHD FDENGIIYWI GTNAKTAYEW VNPAAYGLVV 1100
VTSSEGRNLP YGRLEDILSR DNSALNCHSN DDKNAWFAID LGLWVIPSAY 1150
TLRHARGYGR SALRNWVFQV SKDGQNWTSL YTHVDDCSLN EPGSTATWPL 1200
DPPKDEKQGW RHVRIKQMGK NASGQTHYLS LSGFELYGTV NGVCEDQLGK 1250
AAKEAEANLR RQRRLVRSQV LKYMVPGARV IRGLDWKWRD QDGSPQGEGT 1300
VTGELHNGWI DVTWDAGGSN SYRMGAEGKF DLKLAPGYDP DTVASPKPVS 1350
STVSGTTQSW SSLVKNNCPD KTSAAAGSSS RKGSSSSVCS VASSSDISLG 1400
STKTERRSEI VMEHSIVSGA DVHEPIVVLS SAENVPQTEV GSSSSASTST 1450
LTAETGSENA ERKLGPDSSV RTPGESSAIS MGIVSVSSPD VSSVSELTNK 1500
EAASQRPLSS SASNRLSVSS LLAAGAPMSS SASVPNLSSR ETSSLESFVR 1550
RVANIARTNA TNNMNLSRSS SDNNTNTLGR NVMSTATSPL MGAQSFPNLT 1600
TPGTTSTVTM STSSVTSSSN VATATTVLSV GQSLSNTLTT SLTSTSSESD 1650
TGQEAEYSLY DFLDSCRAST LLAELDDDED LPEPDEEDDE NEDDNQEDQE 1700
YEEVMILRRP SLQRRAGSRS DVTHHAVTSQ LPQVPAGAGS RPIGEQEEEE 1750
YETKGGRRRT WDDDYVLKRQ FSALVPAFDP RPGRTNVQQT TDLEIPPPGT 1800
PHSELLEEVE CTPSPRLALT LKVTGLGTTR EVELPLTNFR STIFYYVQKL 1850
LQLSCNGNVK SDKLRRIWEP TYTIMYREMK DSDKEKENGK MGCWSIEHVE 1900
QYLGTDELPK NDLITYLQKN ADAAFLRHWK LTGTNKSIRK NRNCSQLIAA 1950
YKDFCEHGTK SGLNQGAIST LQSSDILNLT KEQPQAKAGN GQNSCGVEDV 2000
LQLLRILYIV ASDPYSRISQ EDGDEQLQFT FPPDEFTSKK ITTKILQQIE 2050
EPLALASGAL PDWCEQLTSK CPFLIPFETR QLYFTCTAFG ASRAIVWLQN 2100
RREATVERTR TTSSVRRDDP GEFRVGRLKH ERVKVPRGES LMEWAENVMQ 2150
IHADRKSVLE VEFLGEEGTG LGPTLEFYAL VAAEFQRTDL GAWLCDDNFP 2200
DDESRHVDLG GGLKPPGYYV QRSCGLFTAP FPQDSDELER ITKLFHFLGI 2250
FLAKCIQDNR LVDLPISKPF FKLMCMGDIK SNMSKLIYES RGDRDLHCTE 2300
SQSEASTEEG HDSLSVGSFE EDSKSEFILD PPKPKPPAWF NGILTWEDFE 2350
LVNPHRARFL KEIKDLAIKR RQILSNKGLS EDEKNTKLQE LVLKNPSGSG 2400
PPLSIEDLGL NFQFCPSSRI YGFTAVDLKP SGEDEMITMD NAEEYVDLMF 2450
DFCMHTGIQK QMEAFRDGFN KVFPMEKLSS FSHEEVQMIL CGNQSPSWAA 2500
EDIINYTEPK LGYTRDSPGF LRFVRVLCGM SSDERKAFLQ FTTGCSTLPP 2550
GGLANLHPRL TVVRKVDATD ASYPSVNTCV HYLKLPEYSS EEIMRERLLA 2600
ATMEKGFHLN 2610
Length:2,610
Mass (Da):289,384
Last modified:November 30, 2010 - v3
Checksum:i27E56401E07E158C
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti656 – 6561Q → H.
Corresponds to variant rs11620816 [ dbSNP | Ensembl ].
VAR_059666
Natural varianti2027 – 20271L → P.3 Publications
Corresponds to variant rs1315794 [ dbSNP | Ensembl ].
VAR_067707

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti561 – 5611K → Q in AAP13073. 1 Publication
Sequence conflicti603 – 6031L → I in AAP13073. 1 Publication
Sequence conflicti611 – 6133FLD → YKH in AAP13073. 1 Publication
Sequence conflicti653 – 6531K → Q in AAP13073. 1 Publication
Sequence conflicti894 – 8941E → K in AAP13073. 1 Publication
Sequence conflicti927 – 94418SMDLD…VERIN → VSIFRATKQKQNEVPKVILS in AAP13073. 1 Publication
Add
BLAST
Sequence conflicti951 – 9511S → T in AAP13073. 1 Publication
Sequence conflicti1281 – 12811I → T in BAA86445. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY254380 mRNA. Translation: AAP13073.1.
AL121808 Genomic DNA. No translation available.
AL136418 Genomic DNA. No translation available.
CH471078 Genomic DNA. Translation: EAW65950.1.
CH471078 Genomic DNA. Translation: EAW65952.1.
AB032957 mRNA. Translation: BAA86445.2.
AL110222 mRNA. Translation: CAB53681.1.
BC011658 mRNA. Translation: AAH11658.2.
BC063686 mRNA. Translation: AAH63686.1.
CCDSiCCDS41939.1.
PIRiT14761.
RefSeqiNP_056197.3. NM_015382.3.
XP_005267559.2. XM_005267502.2.
UniGeneiHs.708017.

Genome annotation databases

EnsembliENST00000399332; ENSP00000382269; ENSG00000092148.
ENST00000553700; ENSP00000450697; ENSG00000092148.
GeneIDi25831.
KEGGihsa:25831.
UCSCiuc001wrc.1. human.

Polymorphism databases

DMDMi313104227.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY254380 mRNA. Translation: AAP13073.1 .
AL121808 Genomic DNA. No translation available.
AL136418 Genomic DNA. No translation available.
CH471078 Genomic DNA. Translation: EAW65950.1 .
CH471078 Genomic DNA. Translation: EAW65952.1 .
AB032957 mRNA. Translation: BAA86445.2 .
AL110222 mRNA. Translation: CAB53681.1 .
BC011658 mRNA. Translation: AAH11658.2 .
BC063686 mRNA. Translation: AAH63686.1 .
CCDSi CCDS41939.1.
PIRi T14761.
RefSeqi NP_056197.3. NM_015382.3.
XP_005267559.2. XM_005267502.2.
UniGenei Hs.708017.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2DK3 NMR - A 1266-1338 [» ]
2LC3 NMR - A 1879-1966 [» ]
3DKM X-ray 1.60 A 1271-1341 [» ]
ProteinModelPortali Q9ULT8.
SMRi Q9ULT8. Positions 1266-1338, 1879-1966.
ModBasei Search...

Protein-protein interaction databases

BioGridi 117359. 15 interactions.
DIPi DIP-31669N.
IntActi Q9ULT8. 8 interactions.
MINTi MINT-6783566.
STRINGi 9606.ENSP00000382269.

PTM databases

PhosphoSitei Q9ULT8.

Polymorphism databases

DMDMi 313104227.

Proteomic databases

MaxQBi Q9ULT8.
PaxDbi Q9ULT8.
PeptideAtlasi Q9ULT8.
PRIDEi Q9ULT8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000399332 ; ENSP00000382269 ; ENSG00000092148 .
ENST00000553700 ; ENSP00000450697 ; ENSG00000092148 .
GeneIDi 25831.
KEGGi hsa:25831.
UCSCi uc001wrc.1. human.

Organism-specific databases

CTDi 25831.
GeneCardsi GC14M031569.
HGNCi HGNC:20157. HECTD1.
HPAi HPA002929.
neXtProti NX_Q9ULT8.
PharmGKBi PA134989284.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5021.
HOGENOMi HOG000018061.
HOVERGENi HBG067533.
InParanoidi Q9ULT8.
KOi K12231.
OMAi TKHSFTA.
PhylomeDBi Q9ULT8.
TreeFami TF323674.

Enzyme and pathway databases

UniPathwayi UPA00143 .

Miscellaneous databases

ChiTaRSi HECTD1. human.
EvolutionaryTracei Q9ULT8.
GenomeRNAii 25831.
NextBioi 47125.
PROi Q9ULT8.

Gene expression databases

ArrayExpressi Q9ULT8.
Bgeei Q9ULT8.
CleanExi HS_HECTD1.
Genevestigatori Q9ULT8.

Family and domain databases

Gene3Di 1.25.10.10. 2 hits.
1.25.40.20. 1 hit.
2.60.120.260. 1 hit.
InterProi IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR008979. Galactose-bd-like.
IPR000569. HECT.
IPR010606. Mib_Herc2.
IPR012919. Sad1_UNC_C.
[Graphical view ]
Pfami PF12796. Ank_2. 1 hit.
PF00632. HECT. 1 hit.
PF06701. MIB_HERC2. 1 hit.
PF07738. Sad1_UNC. 1 hit.
[Graphical view ]
SMARTi SM00248. ANK. 3 hits.
SM00119. HECTc. 1 hit.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 3 hits.
SSF48403. SSF48403. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF56204. SSF56204. 4 hits.
PROSITEi PS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 2 hits.
PS50237. HECT. 1 hit.
PS51416. MIB_HERC2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "EULIR is an E3 ubiquitin ligase for inhibin receptor."
    Zhang H.
    Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The DNA sequence and analysis of human chromosome 14."
    Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
    , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
    Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT PRO-2027.
  4. "Characterization of cDNA clones selected by the GeneMark analysis from size-fractionated cDNA libraries from human brain."
    Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.
    DNA Res. 6:329-336(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 443-2610, VARIANT PRO-2027.
    Tissue: Brain.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1652-2610, VARIANT PRO-2027.
    Tissue: Testis.
  6. "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] OF 2091-2610.
    Tissue: Muscle and Urinary bladder.
  7. "Protein-protein interactions between large proteins: two-hybrid screening using a functionally classified library composed of long cDNAs."
    Nakayama M., Kikuno R., Ohara O.
    Genome Res. 12:1773-1784(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IGSF1.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1488, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "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].
  10. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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-631, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Solution structure of MIB-HERC2 domain in HECT domain containing protein 1."
    RIKEN structural genomics initiative (RSGI)
    Submitted (OCT-2006) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 1266-1338.

Entry informationi

Entry nameiHECD1_HUMAN
AccessioniPrimary (citable) accession number: Q9ULT8
Secondary accession number(s): D3DS86
, Q6P445, Q86VJ1, Q96F34, Q9UFZ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 12, 2003
Last sequence update: November 30, 2010
Last modified: September 3, 2014
This is version 131 of the entry and version 3 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 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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